ID MUC2_HUMAN Reviewed; 5289 AA.
AC Q02817; Q14878;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2023, sequence version 3.
DT 27-MAR-2024, entry version 190.
DE RecName: Full=Mucin-2 {ECO:0000303|PubMed:8300571};
DE Short=MUC-2 {ECO:0000303|PubMed:1885763};
DE AltName: Full=Intestinal mucin-2 {ECO:0000303|PubMed:8300571};
DE Flags: Precursor;
GN Name=MUC2 {ECO:0000303|PubMed:8300571, ECO:0000312|HGNC:HGNC:7512};
GN Synonyms=SMUC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Intestine;
RX PubMed=8300571; DOI=10.1016/s0021-9258(17)41965-x;
RA Gum J.R. Jr., Hicks J.W., Toribara N.W., Siddiki B., Kim Y.S.;
RT "Molecular cloning of human intestinal mucin (MUC2) cDNA. Identification of
RT the amino terminus and overall sequence similarity to prepro-von Willebrand
RT factor.";
RL J. Biol. Chem. 269:2440-2446(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 626-1895 AND 4306-5289.
RC TISSUE=Colon;
RX PubMed=1400449; DOI=10.1016/s0021-9258(19)36620-7;
RA Gum J.R. Jr., Hicks J.W., Toribara N.W., Rothe E.-M., Lagace R.E.,
RA Kim Y.S.;
RT "The human MUC2 intestinal mucin has cysteine-rich subdomains located both
RT upstream and downstream of its central repetitive region.";
RL J. Biol. Chem. 267:21375-21383(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1343-1895 AND 4286-4305.
RX PubMed=1885763; DOI=10.1172/jci115360;
RA Toribara N.W., Gum J.R. Jr., Culhane P.J., Lagace R.E., Hicks J.W.,
RA Petersen G.M., Kim Y.S.;
RT "MUC-2 human small intestinal mucin gene structure. Repeated arrays and
RT polymorphism.";
RL J. Clin. Invest. 88:1005-1013(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4185-4462.
RX PubMed=2703501; DOI=10.1016/s0021-9258(18)83373-7;
RA Gum J.R. Jr., Byrd J.C., Hicks J.W., Toribara N.W., Lamport D.T.A.,
RA Kim Y.S.;
RT "Molecular cloning of human intestinal mucin cDNAs. Sequence analysis and
RT evidence for genetic polymorphism.";
RL J. Biol. Chem. 264:6480-6487(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4597-4737.
RX PubMed=1550588; DOI=10.1016/0006-291x(92)90557-2;
RA Xu G., Huan L., Khatri I., Sajjan U.S., McCool D., Wang D., Jones C.,
RA Forstner G., Forstner J.;
RT "Human intestinal mucin-like protein (MLP) is homologous with rat MLP in
RT the C-terminal region, and is encoded by a gene on chromosome 11 p 15.5.";
RL Biochem. Biophys. Res. Commun. 183:821-828(1992).
RN [7]
RP STRUCTURE OF O-LINKED CARBOHYDRATES.
RX PubMed=11445551; DOI=10.1093/glycob/11.6.459;
RA Silverman H.S., Parry S., Sutton-Smith M., Burdick M.D., McDermott K.,
RA Reid C.J., Batra S.K., Morris H.R., Hollingsworth M.A., Dell A., Harris A.;
RT "In vivo glycosylation of mucin tandem repeats.";
RL Glycobiology 11:459-471(2001).
RN [8]
RP SUBUNIT.
RX PubMed=12374796; DOI=10.1074/jbc.m208483200;
RA Godl K., Johansson M.E.V., Lidell M.E., Moergelin M., Karlsson H.,
RA Olson F.J., Gum J.R. Jr., Kim Y.S., Hansson G.C.;
RT "The N terminus of the MUC2 mucin forms trimers that are held together
RT within a trypsin-resistant core fragment.";
RL J. Biol. Chem. 277:47248-47256(2002).
RN [9]
RP AUTOCATALYTIC CLEAVAGE.
RX PubMed=12582180; DOI=10.1074/jbc.m210069200;
RA Lidell M.E., Johansson M.E.V., Hansson G.C.;
RT "An autocatalytic cleavage in the C terminus of the human MUC2 mucin occurs
RT at the low pH of the late secretory pathway.";
RL J. Biol. Chem. 278:13944-13951(2003).
RN [10]
RP FUNCTION.
RX PubMed=17058067; DOI=10.1007/s00109-006-0100-2;
RA Moehle C., Ackermann N., Langmann T., Aslanidis C., Kel A.,
RA Kel-Margoulis O., Schmitz-Madry A., Zahn A., Stremmel W., Schmitz G.;
RT "Aberrant intestinal expression and allelic variants of mucin genes
RT associated with inflammatory bowel disease.";
RL J. Mol. Med. 84:1055-1066(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP SUBUNIT (MICROBIAL INFECTION).
RX PubMed=18327567; DOI=10.1007/s00203-008-0358-6;
RA Linden S.K., Bierne H., Sabet C., Png C.W., Florin T.H., McGuckin M.A.,
RA Cossart P.;
RT "Listeria monocytogenes internalins bind to the human intestinal mucin
RT MUC2.";
RL Arch. Microbiol. 190:101-104(2008).
RN [13]
RP INTERACTION WITH AGR2.
RX PubMed=19359471; DOI=10.1073/pnas.0808722106;
RA Park S.-W., Zhen G., Verhaeghe C., Nakagami Y., Nguyenvu L.T.,
RA Barczak A.J., Killeen N., Erle D.J.;
RT "The protein disulfide isomerase AGR2 is essential for production of
RT intestinal mucus.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:6950-6955(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH FCGBP.
RX PubMed=19432394; DOI=10.1021/pr9002504;
RA Johansson M.E.V., Thomsson K.A., Hansson G.C.;
RT "Proteomic analyses of the two mucus layers of the colon barrier reveal
RT that their main component, the Muc2 mucin, is strongly bound to the Fcgbp
RT protein.";
RL J. Proteome Res. 8:3549-3557(2009).
RN [15] {ECO:0007744|PDB:6RBF}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 858-1259, DISULFIDE BOND, AND
RP GLYCOSYLATION AT ASN-894 AND ASN-1154.
RX PubMed=31310764; DOI=10.1016/j.jmb.2019.07.018;
RA Javitt G., Calvo M.L.G., Albert L., Reznik N., Ilani T., Diskin R.,
RA Fass D.;
RT "Intestinal gel-forming Mucins polymerize by disulfide-mediated
RT dimerization of D3 domains.";
RL J. Mol. Biol. 431:3740-3752(2019).
RN [16] {ECO:0007744|PDB:6TM6, ECO:0007744|PDB:7A5O}
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 21-1395 IN COMPLEX WITH CA(2+),
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION AT ASN-163; ASN-670;
RP ASN-1154 AND THR-1266; THR-1267; THR-1269; THR-1270; THR-1272; THR-1275;
RP THR-1276; THR-1281; THR-1282; THR-1287; SER-1291; SER-1292; THR-1293;
RP SER-1296 AND THR-1297, AND MUTAGENESIS OF CYS-1088 AND CYS-1130.
RX PubMed=33031746; DOI=10.1016/j.cell.2020.09.021;
RA Javitt G., Khmelnitsky L., Albert L., Bigman L.S., Elad N., Morgenstern D.,
RA Ilani T., Levy Y., Diskin R., Fass D.;
RT "Assembly Mechanism of Mucin and von Willebrand Factor Polymers.";
RL Cell 183:717-717(2020).
RN [17] {ECO:0007744|PDB:7POV, ECO:0007744|PDB:7PP6}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF 21-1259 IN COMPLEX
RP WITH CA(2+), AND GLYCOSYLATION AT ASN-163; ASN-670 AND ASN-1154.
RX PubMed=35377815; DOI=10.1073/pnas.2116790119;
RA Javitt G., Fass D.;
RT "Helical self-assembly of a mucin segment suggests an evolutionary origin
RT for von Willebrand factor tubules.";
RL Proc. Natl. Acad. Sci. U.S.A. 119:e2116790119-e2116790119(2022).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) IN COMPLEX WITH CU(2+), FUNCTION,
RP COPPER-BINDING, AND MUTAGENESIS OF HIS-32; HIS-34; MET-146; MET-154;
RP HIS-277; GLU-322 AND MET-326.
RX PubMed=36206754; DOI=10.1016/j.cell.2022.09.021;
RA Reznik N., Gallo A.D., Rush K.W., Javitt G., Fridmann-Sirkis Y., Ilani T.,
RA Nairner N.A., Fishilevich S., Gokhman D., Chacon K.N., Franz K.J., Fass D.;
RT "Intestinal mucin is a chaperone of multivalent copper.";
RL Cell 0:0-0(2022).
CC -!- FUNCTION: Coats the epithelia of the intestines and other mucus
CC membrane-containing organs to provide a protective, lubricating barrier
CC against particles and infectious agents at mucosal surfaces
CC (PubMed:17058067, PubMed:19432394, PubMed:33031746). Major constituent
CC of the colon mucus, which is mainly formed by large polymeric networks
CC of MUC2 secreted by goblet cells that cover the exposed surfaces of
CC intestine (PubMed:19432394, PubMed:33031746). MUC2 networks form
CC hydrogels that guard the underlying epithelium from pathogens and other
CC hazardous matter entering from the outside world, while permitting
CC nutrient absorption and gas exchange (PubMed:33031746,
CC PubMed:36206754). Acts as a divalent copper chaperone that protects
CC intestinal cells from copper toxicity and facilitates nutritional
CC copper unptake into cells (PubMed:36206754). Binds both Cu(2+) and its
CC reduced form, Cu(1+), at two juxtaposed binding sites: Cu(2+), once
CC reduced to Cu(1+) by vitamin C (ascorbate) or other dietary
CC antioxidants, transits to the other binding site (PubMed:36206754).
CC MUC2-bound Cu(1+) is protected from oxidation in aerobic environments,
CC and can be released for nutritional delivery to cells
CC (PubMed:36206754). Mucin gels store antimicrobial molecules that
CC participate in innate immunity (PubMed:33031746). Mucin glycoproteins
CC also house and feed the microbiome, lubricate tissue surfaces, and may
CC facilitate the removal of contaminants and waste products from the body
CC (PubMed:33031746). Goblet cells synthesize two forms of MUC2 mucin that
CC differ in branched chain O-glycosylation and the site of production in
CC the colon: a (1) 'thick' mucus that wraps the microbiota to form fecal
CC pellets is produced in the proximal, ascending colon (By similarity).
CC 'Thick' mucus transits along the descending colon and is lubricated by
CC a (2) 'thin' MUC2 mucus produced in the distal colon which adheres to
CC the 'thick' mucus (By similarity). {ECO:0000250|UniProtKB:Q80Z19,
CC ECO:0000269|PubMed:17058067, ECO:0000269|PubMed:19432394,
CC ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:36206754}.
CC -!- SUBUNIT: Homomultimer; disulfide-linked (PubMed:12374796,
CC PubMed:31310764, PubMed:33031746, PubMed:35377815). The N- and C-
CC terminus mediate their assembly into higher order structures to form
CC filaments (PubMed:33031746, PubMed:35377815). The CTCK domains of two
CC polypeptides associate in the endoplasmic reticulum to generate
CC intermolecularly disulfide-bonded dimers (By similarity). These dimers
CC progress to the Golgi apparatus, which is a more acidic environment
CC than the endoplasmic reticulum (PubMed:33031746). Under acidic
CC conditions, the N-termini form non-covalent intermolecular interactions
CC that juxtapose assemblies of the third VWD domain (VWD3) from different
CC CTCK-linked dimers (PubMed:33031746). The VWD3 assemblies then become
CC disulfide bonded to one another to produce long, disulfide-linked
CC polymers that remain highly compact until secretion (PubMed:33031746).
CC Interacts with FCGBP (PubMed:19432394). Interacts with AGR2; disulfide-
CC linked (PubMed:19359471). {ECO:0000250|UniProtKB:Q9HC84,
CC ECO:0000269|PubMed:12374796, ECO:0000269|PubMed:19359471,
CC ECO:0000269|PubMed:19432394, ECO:0000269|PubMed:31310764,
CC ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815}.
CC -!- SUBUNIT: (Microbial infection) Interacts in vitro with L.monocytogenes
CC internalin proteins InlB, InlC and InlJ; for InlC binding is slightly
CC better at pH 5.5, (the pH of the intestine) than at pH 7.4.
CC {ECO:0000269|PubMed:18327567}.
CC -!- INTERACTION:
CC Q02817; O95994: AGR2; NbExp=3; IntAct=EBI-2105803, EBI-712648;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33031746}. Note=In
CC the intestine, secreted into the inner and outer mucus layers (By
CC similarity). Before secretion, mucin polymers are stored in dedicated
CC secretory vesicles (PubMed:33031746). {ECO:0000250|UniProtKB:Q80Z19,
CC ECO:0000269|PubMed:33031746}.
CC -!- TISSUE SPECIFICITY: Colon, small intestine, colonic tumors, bronchus,
CC cervix and gall bladder. {ECO:0000269|PubMed:8300571}.
CC -!- DOMAIN: The CTCK domain mediates interchain disulfide bonds with
CC another molecule of MUC2. {ECO:0000250|UniProtKB:Q9HC84}.
CC -!- PTM: O-glycosylated (PubMed:11445551, PubMed:33031746). O-glycosylation
CC is required for mucin assembly (PubMed:33031746). Goblet cells
CC synthesize two forms of mucin that differ in branched chain O-
CC glycosylation and the site of production in the colon (By similarity).
CC {ECO:0000250|UniProtKB:Q80Z19, ECO:0000269|PubMed:11445551,
CC ECO:0000269|PubMed:33031746}.
CC -!- PTM: May undergo proteolytic cleavage in the outer mucus layer of the
CC colon, contributing to the expanded volume and loose nature of this
CC layer which allows for bacterial colonization in contrast to the inner
CC mucus layer which is dense and devoid of bacteria.
CC {ECO:0000250|UniProtKB:Q80Z19}.
CC -!- PTM: At low pH of 6 and under, undergoes autocatalytic cleavage in
CC vitro in the N-terminal region of the fourth VWD domain. It is likely
CC that this also occurs in vivo and is triggered by the low pH of the
CC late secretory pathway. {ECO:0000269|PubMed:12582180}.
CC -!- POLYMORPHISM: The number of repeats is highly polymorphic and varies
CC among different alleles.
CC -!- WEB RESOURCE: Name=Mucin database;
CC URL="http://www.medkem.gu.se/mucinbiology/databases/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/41457/MUC2";
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DR EMBL; L21998; AAB95295.1; -; mRNA.
DR EMBL; AC139749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC239832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC256300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M74027; AAA59875.1; -; Genomic_DNA.
DR EMBL; M94131; AAA59163.1; -; mRNA.
DR EMBL; M94132; AAA59164.1; -; mRNA.
DR PIR; A49963; A43932.
DR RefSeq; NP_002448.4; NM_002457.4.
DR PDB; 6RBF; X-ray; 2.70 A; A/B/C/D=858-1259.
DR PDB; 6TM2; EM; 2.95 A; A/B=21-749, C/D=750-1197, E/F=1198-1397.
DR PDB; 6TM6; X-ray; 1.63 A; A=1301-1395.
DR PDB; 7A5O; EM; 2.95 A; A/B/C/D/E/F/G/H/I/J=21-1397.
DR PDB; 7POV; EM; 3.80 A; A/B/C/D=21-1259.
DR PDB; 7PP6; EM; 3.40 A; A/B/C/D/E/G=21-1259.
DR PDB; 7PRL; X-ray; 2.48 A; A=1-389.
DR PDB; 7QCL; EM; 3.36 A; A/B=4408-4990.
DR PDB; 7QCN; EM; 3.40 A; A/B=4409-4851.
DR PDB; 7QCU; EM; 3.25 A; A/B=4406-5179.
DR PDBsum; 6RBF; -.
DR PDBsum; 6TM2; -.
DR PDBsum; 6TM6; -.
DR PDBsum; 7A5O; -.
DR PDBsum; 7POV; -.
DR PDBsum; 7PP6; -.
DR PDBsum; 7PRL; -.
DR PDBsum; 7QCL; -.
DR PDBsum; 7QCN; -.
DR PDBsum; 7QCU; -.
DR EMDB; EMD-10517; -.
DR EMDB; EMD-11658; -.
DR EMDB; EMD-13575; -.
DR EMDB; EMD-13580; -.
DR EMDB; EMD-13896; -.
DR EMDB; EMD-13897; -.
DR EMDB; EMD-13899; -.
DR SASBDB; Q02817; -.
DR SMR; Q02817; -.
DR BioGRID; 110670; 3.
DR DIP; DIP-48824N; -.
DR IntAct; Q02817; 4.
DR MINT; Q02817; -.
DR STRING; 9606.ENSP00000494061; -.
DR DrugBank; DB02587; Colforsin.
DR DrugBank; DB01411; Pranlukast.
DR MEROPS; I08.951; -.
DR MEROPS; I08.954; -.
DR GlyConnect; 1519; 2 N-Linked glycans (3 sites), 27 O-Linked glycans.
DR GlyConnect; 373; 8 O-Linked glycans.
DR GlyCosmos; Q02817; 30 sites, 53 glycans.
DR GlyGen; Q02817; 46 sites, 51 O-linked glycans (1 site).
DR iPTMnet; Q02817; -.
DR PhosphoSitePlus; Q02817; -.
DR SwissPalm; Q02817; -.
DR BioMuta; MUC2; -.
DR DMDM; 2506877; -.
DR CPTAC; CPTAC-1497; -.
DR EPD; Q02817; -.
DR jPOST; Q02817; -.
DR MassIVE; Q02817; -.
DR PeptideAtlas; Q02817; -.
DR ProteomicsDB; 58127; -.
DR GeneID; 4583; -.
DR KEGG; hsa:4583; -.
DR AGR; HGNC:7512; -.
DR CTD; 4583; -.
DR GeneCards; MUC2; -.
DR HGNC; HGNC:7512; MUC2.
DR MalaCards; MUC2; -.
DR MIM; 158370; gene.
DR neXtProt; NX_Q02817; -.
DR PharmGKB; PA31316; -.
DR InParanoid; Q02817; -.
DR PathwayCommons; Q02817; -.
DR Reactome; R-HSA-5083625; Defective GALNT3 causes HFTC.
DR Reactome; R-HSA-5083632; Defective C1GALT1C1 causes TNPS.
DR Reactome; R-HSA-5083636; Defective GALNT12 causes CRCS1.
DR Reactome; R-HSA-5621480; Dectin-2 family.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR Reactome; R-HSA-977068; Termination of O-glycan biosynthesis.
DR SignaLink; Q02817; -.
DR SIGNOR; Q02817; -.
DR ChiTaRS; MUC2; human.
DR GeneWiki; MUC2; -.
DR Pharos; Q02817; Tdark.
DR PRO; PR:Q02817; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q02817; Protein.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0070702; C:inner mucus layer; ISS:UniProtKB.
DR GO; GO:0070703; C:outer mucus layer; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:1903135; F:cupric ion binding; IDA:UniProtKB.
DR GO; GO:1903136; F:cuprous ion binding; IDA:UniProtKB.
DR GO; GO:0010273; P:detoxification of copper ion; IDA:UniProtKB.
DR GO; GO:0048874; P:host-mediated regulation of intestinal microbiota composition; ISS:UniProtKB.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IMP:UniProtKB.
DR GO; GO:0070254; P:mucus secretion; IMP:UniProt.
DR CDD; cd19941; TIL; 3.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR014853; VWF/SSPO/ZAN-like_Cys-rich_dom.
DR InterPro; IPR001007; VWF_dom.
DR InterPro; IPR001846; VWF_type-D.
DR InterPro; IPR025155; WxxW_domain.
DR PANTHER; PTHR11339; EXTRACELLULAR MATRIX GLYCOPROTEIN RELATED; 1.
DR PANTHER; PTHR11339:SF399; MUCIN-2; 1.
DR Pfam; PF08742; C8; 4.
DR Pfam; PF13330; Mucin2_WxxW; 2.
DR Pfam; PF01826; TIL; 1.
DR Pfam; PF00094; VWD; 4.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00832; C8; 4.
DR SMART; SM00041; CT; 1.
DR SMART; SM00214; VWC; 3.
DR SMART; SM00215; VWC_out; 2.
DR SMART; SM00216; VWD; 4.
DR SUPFAM; SSF57603; FnI-like domain; 2.
DR SUPFAM; SSF57567; Serine protease inhibitors; 4.
DR PROSITE; PS01185; CTCK_1; 1.
DR PROSITE; PS01225; CTCK_2; 1.
DR PROSITE; PS01208; VWFC_1; 2.
DR PROSITE; PS50184; VWFC_2; 2.
DR PROSITE; PS51233; VWFD; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Calcium; Copper; Disulfide bond;
KW Glycoprotein; Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..5289
FT /note="Mucin-2"
FT /id="PRO_0000019281"
FT DOMAIN 35..207
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 295..351
FT /note="TIL"
FT DOMAIN 389..564
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 858..1028
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REPEAT 1401..1416
FT /note="1"
FT REPEAT 1417..1432
FT /note="2"
FT REPEAT 1433..1448
FT /note="3"
FT REPEAT 1449..1464
FT /note="4"
FT REPEAT 1465..1471
FT /note="5"
FT REPEAT 1472..1478
FT /note="6"
FT REPEAT 1479..1494
FT /note="7A"
FT REPEAT 1495..1517
FT /note="7B"
FT REPEAT 1518..1533
FT /note="8A"
FT REPEAT 1534..1556
FT /note="8B"
FT REPEAT 1557..1572
FT /note="9A"
FT REPEAT 1573..1596
FT /note="9B"
FT REPEAT 1597..1612
FT /note="10A"
FT REPEAT 1613..1635
FT /note="10B"
FT REPEAT 1636..1651
FT /note="11A"
FT REPEAT 1652..1675
FT /note="11B"
FT REPEAT 1676..1683
FT /note="12"
FT REPEAT 1684..1699
FT /note="13"
FT REPEAT 1700..1715
FT /note="14"
FT REPEAT 1716..1731
FT /note="15"
FT REPEAT 1732..1747
FT /note="16"
FT DOMAIN 4589..4772
FT /note="VWFD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 4927..4996
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 5034..5101
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 5185..5270
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT REGION 1399..1773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1401..1747
FT /note="Approximate repeats"
FT REGION 1885..4238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4269..4430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4492..4524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4770..4795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1401..1698
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1718..1744
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1745..1759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1885..2161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2169..4238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4269..4381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4389..4430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4492..4523
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /evidence="ECO:0000269|PubMed:36206754"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:7POV"
FT BINDING 146
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000305|PubMed:36206754"
FT BINDING 154
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000305|PubMed:36206754"
FT BINDING 156
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /evidence="ECO:0000269|PubMed:36206754"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0007744|PDB:7A5O"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7A5O,
FT ECO:0007744|PDB:7POV"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7A5O,
FT ECO:0007744|PDB:7POV"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7A5O,
FT ECO:0007744|PDB:7POV"
FT BINDING 277
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /evidence="ECO:0000269|PubMed:36206754"
FT BINDING 324
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /evidence="ECO:0000269|PubMed:36206754"
FT BINDING 326
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000305|PubMed:36206754"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:7POV"
FT BINDING 530
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7A5O,
FT ECO:0007744|PDB:7POV"
FT BINDING 532
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7A5O,
FT ECO:0007744|PDB:7POV"
FT BINDING 534
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7A5O,
FT ECO:0007744|PDB:7POV"
FT BINDING 537
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7A5O,
FT ECO:0007744|PDB:7POV"
FT BINDING 538
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7A5O,
FT ECO:0007744|PDB:7POV"
FT BINDING 872
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:6RBF,
FT ECO:0007744|PDB:7POV"
FT BINDING 994
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7A5O,
FT ECO:0007744|PDB:7POV"
FT BINDING 996
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7A5O,
FT ECO:0007744|PDB:7POV"
FT BINDING 998
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7A5O,
FT ECO:0007744|PDB:7POV"
FT BINDING 1001
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7A5O,
FT ECO:0007744|PDB:7POV"
FT BINDING 1002
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7A5O,
FT ECO:0007744|PDB:7POV"
FT BINDING 1310
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0007744|PDB:6TM2, ECO:0007744|PDB:7A5O"
FT BINDING 1312
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0007744|PDB:6TM2, ECO:0007744|PDB:7A5O"
FT BINDING 1312
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0007744|PDB:6TM2, ECO:0007744|PDB:7A5O"
FT BINDING 1313
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0007744|PDB:6TM2, ECO:0007744|PDB:7A5O"
FT BINDING 1316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0007744|PDB:6TM2, ECO:0007744|PDB:7A5O"
FT BINDING 1319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0007744|PDB:6TM2, ECO:0007744|PDB:7A5O"
FT BINDING 1321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0007744|PDB:6TM2, ECO:0007744|PDB:7A5O"
FT BINDING 1322
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0007744|PDB:6TM2, ECO:0007744|PDB:7A5O"
FT BINDING 1324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0007744|PDB:6TM2, ECO:0007744|PDB:7A5O"
FT BINDING 1381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0007744|PDB:6TM2, ECO:0007744|PDB:7A5O"
FT BINDING 1382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0007744|PDB:6TM2, ECO:0007744|PDB:7A5O"
FT SITE 4596..4597
FT /note="Cleavage; by autolysis; in vitro"
FT /evidence="ECO:0000269|PubMed:12582180"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7A5O,
FT ECO:0007744|PDB:7POV"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7A5O,
FT ECO:0007744|PDB:7POV"
FT CARBOHYD 770
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 894
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0007744|PDB:6RBF"
FT CARBOHYD 1139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7A5O,
FT ECO:0007744|PDB:7POV"
FT CARBOHYD 1215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1266
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:33031746"
FT CARBOHYD 1267
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:33031746"
FT CARBOHYD 1269
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:33031746"
FT CARBOHYD 1270
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:33031746"
FT CARBOHYD 1272
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:33031746"
FT CARBOHYD 1275
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:33031746"
FT CARBOHYD 1276
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:33031746"
FT CARBOHYD 1281
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:33031746"
FT CARBOHYD 1282
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:33031746"
FT CARBOHYD 1287
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:33031746"
FT CARBOHYD 1291
FT /note="O-linked (GalNAc) serine"
FT /evidence="ECO:0000269|PubMed:33031746"
FT CARBOHYD 1292
FT /note="O-linked (GalNAc) serine"
FT /evidence="ECO:0000269|PubMed:33031746"
FT CARBOHYD 1293
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:33031746"
FT CARBOHYD 1296
FT /note="O-linked (GalNAc) serine"
FT /evidence="ECO:0000269|PubMed:33031746"
FT CARBOHYD 1297
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:33031746"
FT CARBOHYD 1787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4726
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4862
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4991
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4998
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5065
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5080
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:7POV, ECO:0007744|PDB:7PP6"
FT DISULFID 59..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:7POV, ECO:0007744|PDB:7PP6"
FT DISULFID 67..166
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 218..255
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 225..250
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 237..275
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 257..263
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 265..291
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 295..329
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 308..321
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 312..351
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 331..345
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 353..375
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 370..387
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 373..382
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 391..528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:7POV, ECO:0007744|PDB:7PP6"
FT DISULFID 413..563
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 435..443
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:7POV, ECO:0007744|PDB:7PP6"
FT DISULFID 574..619
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 588..614
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 601..639
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 621..627
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 629..654
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 661..698
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 674..688
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 678..718
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 700..712
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 720..742
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 740..749
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 784..820
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 802..814
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 822..844
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 839..856
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 842..851
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 860..992
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580,
FT ECO:0000269|PubMed:31310764, ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:6RBF,
FT ECO:0007744|PDB:7POV, ECO:0007744|PDB:7PP6"
FT DISULFID 882..1027
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580,
FT ECO:0000269|PubMed:31310764, ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:6RBF,
FT ECO:0007744|PDB:7POV, ECO:0007744|PDB:7PP6"
FT DISULFID 891..989
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580,
FT ECO:0000269|PubMed:31310764, ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:6RBF,
FT ECO:0007744|PDB:7POV, ECO:0007744|PDB:7PP6"
FT DISULFID 909..916
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580,
FT ECO:0000269|PubMed:31310764, ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:6RBF,
FT ECO:0007744|PDB:7POV, ECO:0007744|PDB:7PP6"
FT DISULFID 1037..1080
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 1051..1075
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 1062..1102
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 1082..1090
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 1088
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:33031746"
FT DISULFID 1092..1117
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 1108..1137
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 1121..1163
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 1130
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:33031746,
FT ECO:0000269|PubMed:35377815, ECO:0007744|PDB:7POV"
FT DISULFID 1145..1187
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 1167..1181
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 1189..1213
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 1208..1238
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 1211..1221
FT /evidence="ECO:0000269|PubMed:31310764,
FT ECO:0000269|PubMed:33031746, ECO:0000269|PubMed:35377815,
FT ECO:0007744|PDB:6RBF, ECO:0007744|PDB:7POV,
FT ECO:0007744|PDB:7PP6"
FT DISULFID 4591..4732
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 4613..4771
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 4637..4645
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 5185..5232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 5199..5246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 5208..5262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 5212..5264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT VARIANT 58
FT /note="L -> P (in dbSNP:rs2856111)"
FT /id="VAR_056582"
FT VARIANT 116
FT /note="V -> M (in dbSNP:rs11825977)"
FT /id="VAR_056583"
FT VARIANT 832
FT /note="G -> S (in dbSNP:rs11245936)"
FT /id="VAR_056584"
FT VARIANT 1619
FT /note="S -> R (in dbSNP:rs11245947)"
FT /id="VAR_059531"
FT VARIANT 1689
FT /note="P -> L (in dbSNP:rs11245949)"
FT /id="VAR_059532"
FT VARIANT 1768
FT /note="P -> H (in dbSNP:rs34493663)"
FT /id="VAR_061487"
FT VARIANT 2243
FT /note="I -> T (in dbSNP:rs6421972)"
FT /id="VAR_059533"
FT VARIANT 2613
FT /note="T -> P (in dbSNP:rs7480563)"
FT /id="VAR_059534"
FT VARIANT 2613
FT /note="T -> S (in dbSNP:rs7480563)"
FT /id="VAR_059535"
FT VARIANT 2742
FT /note="Q -> L (in dbSNP:rs7126405)"
FT /id="VAR_059536"
FT VARIANT 2742
FT /note="Q -> P (in dbSNP:rs7126405)"
FT /id="VAR_059537"
FT MUTAGEN 32
FT /note="H->A: Decreased binding to Cu(2+)."
FT /evidence="ECO:0000269|PubMed:36206754"
FT MUTAGEN 34
FT /note="H->A,R: Slightly Decreased binding to Cu(2+)."
FT /evidence="ECO:0000269|PubMed:36206754"
FT MUTAGEN 146
FT /note="M->L: Decreased binding to Cu(1+) without affecting
FT binding to Cu(2+). Abolished binding to Cu(1+); when
FT associated with L-154 and V-326."
FT /evidence="ECO:0000269|PubMed:36206754"
FT MUTAGEN 154
FT /note="M->L: Decreased binding to Cu(1+) without affecting
FT binding to Cu(2+). Abolished binding to Cu(1+); when
FT associated with L-146 and V-326."
FT /evidence="ECO:0000269|PubMed:36206754"
FT MUTAGEN 277
FT /note="H->A: Decreased binding to Cu(2+)."
FT /evidence="ECO:0000269|PubMed:36206754"
FT MUTAGEN 322
FT /note="E->A: Decreased binding to Cu(2+)."
FT /evidence="ECO:0000269|PubMed:36206754"
FT MUTAGEN 326
FT /note="M->V: Decreased binding to Cu(1+) without affecting
FT binding to Cu(2+). Abolished binding to Cu(1+); when
FT associated with L-146 and L-154."
FT /evidence="ECO:0000269|PubMed:36206754"
FT MUTAGEN 1088
FT /note="C->A: Does not abolish homodimerization. Does not
FT abolish ability to form filaments; when associated with A-
FT 1130."
FT /evidence="ECO:0000269|PubMed:33031746"
FT MUTAGEN 1130
FT /note="C->A: Impaired formation of intermolecular disulfide
FT bonds; inducing a mixture of monomers and homodimers. Does
FT not abolish ability to form filaments; when associated with
FT A-1088."
FT /evidence="ECO:0000269|PubMed:33031746"
FT CONFLICT 31..34
FT /note="NHGH -> YHGR (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="V -> A (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="E -> Q (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 1279
FT /note="T -> S (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 1325
FT /note="T -> P (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 1351
FT /note="L -> H (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 1412
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 1449
FT /note="P -> L (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 1504
FT /note="T -> M (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 1896
FT /note="T -> PTTT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 1912..1918
FT /note="STQSTTP -> GTQTPTT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 1925
FT /note="N -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 1941..1989
FT /note="PTPITTTTTMVTPTPTITSTQTPTPTPITTTTVTPTPTPTSTQRTTPTS ->
FT TTP (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2037..2041
FT /note="STTTM -> TTTTT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2054..2056
FT /note="LTP -> PTT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2079..2083
FT /note="STPIS -> TTPIT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2102
FT /note="L -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2144..2150
FT /note="KSTTPTS -> QTPTTTP (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2156
FT /note="M -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2162
FT /note="P -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2194
FT /note="P -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2217
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2223
FT /note="N -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2236..2240
FT /note="PSTTL -> QTPTT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2248
FT /note="M -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2263..2267
FT /note="STPIS -> TTPIT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2286..2290
FT /note="PTPIS -> TTPIT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2303
FT /note="S -> G (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2321
FT /note="N -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2359
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2380
FT /note="A -> P (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2401
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2424..2429
FT /note="STPISN -> TTPITT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2447
FT /note="V -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2456..2478
FT /note="Missing (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2489
FT /note="H -> Q (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2516
FT /note="P -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2539
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2568
FT /note="N -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2586..2587
FT /note="VL -> TP (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2594
FT /note="M -> V (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2602..2608
FT /note="STKSTTV -> GTQTPTT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2628..2631
FT /note="STTL -> TPTT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2658
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2664
FT /note="I -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2677
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2700..2704
FT /note="STPIS -> TTPIT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2713
FT /note="A -> P (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2723
FT /note="L -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2734
FT /note="S -> P (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2746
FT /note="P -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2763
FT /note="S -> G (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2769
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2794
FT /note="H -> P (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2812..2817
FT /note="APTPTA -> TPTTTP (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2848..2870
FT /note="Missing (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2904..2907
FT /note="STTL -> TPTT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2919
FT /note="I -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2930
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2937
FT /note="I -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 2953..2957
FT /note="PTPIS -> TTPIT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3003
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3022
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3045
FT /note="P -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3068
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3091
FT /note="P -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3114
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3157..3160
FT /note="STTL -> TPTT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3183
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3194
FT /note="P -> PTP (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3204..3208
FT /note="PTPIS -> TTPIT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3227
FT /note="M -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3254
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3273
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3316..3319
FT /note="STTL -> TPTT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3342..3346
FT /note="PTPIS -> TTPIT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3392
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3411
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3454..3459
FT /note="APTPTA -> TPTTTP (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3488
FT /note="M -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3503
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3526..3530
FT /note="PTPIS -> TTPIT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3576
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3595
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3618
FT /note="P -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3641
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3669..3691
FT /note="Missing (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3710
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3733..3740
FT /note="PTPISTTS -> TTPITTTT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3756
FT /note="M -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3779
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3802
FT /note="M -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3822..3827
FT /note="APTPTA -> TPTTTP (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3868..3871
FT /note="STTL -> TPTT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3894..3898
FT /note="PTPIS -> TTPIT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3917
FT /note="M -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3944
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 3990
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 4036
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 4055
FT /note="S -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 4098..4108
FT /note="APTPTAITTTS -> TPTTTPITTTT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 4144..4149
FT /note="SPTPTA -> TPTTTP (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 4170
FT /note="L -> T (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 4193..4197
FT /note="PTPIS -> TTPIT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 4240..4241
FT /note="VL -> TP (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 4248
FT /note="M -> V (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 4256..4262
FT /note="STKSTTV -> GTQTPTT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 4273
FT /note="A -> P (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 4285..4289
FT /note="MIPIS -> TTPIT (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT CONFLICT 4302..4304
FT /note="TGS -> GTQ (in Ref. 1; AAB95295)"
FT /evidence="ECO:0000305"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:7PRL"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:7PRL"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:7PRL"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:7PRL"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:6TM2"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:7PRL"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:7PRL"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:7PRL"
FT HELIX 222..229
FT /evidence="ECO:0007829|PDB:7PRL"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:7PRL"
FT TURN 235..240
FT /evidence="ECO:0007829|PDB:7PRL"
FT HELIX 243..256
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:7PRL"
FT HELIX 262..277
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:7PP6"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:7PRL"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:7PRL"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:7PRL"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 369..376
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 379..384
FT /evidence="ECO:0007829|PDB:7PRL"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:6TM2"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 413..425
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 427..434
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 442..451
FT /evidence="ECO:0007829|PDB:6TM2"
FT TURN 452..455
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 466..472
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:7PP6"
FT STRAND 480..485
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 487..505
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 511..516
FT /evidence="ECO:0007829|PDB:6TM2"
FT HELIX 518..520
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:6TM2"
FT TURN 536..539
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:7PP6"
FT HELIX 550..553
FT /evidence="ECO:0007829|PDB:6TM2"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 557..560
FT /evidence="ECO:0007829|PDB:6TM2"
FT HELIX 573..576
FT /evidence="ECO:0007829|PDB:6TM2"
FT HELIX 580..588
FT /evidence="ECO:0007829|PDB:6TM2"
FT HELIX 589..591
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:6TM2"
FT HELIX 599..601
FT /evidence="ECO:0007829|PDB:6TM2"
FT TURN 602..604
FT /evidence="ECO:0007829|PDB:6TM2"
FT TURN 607..609
FT /evidence="ECO:0007829|PDB:6TM2"
FT HELIX 610..620
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:6TM2"
FT HELIX 624..635
FT /evidence="ECO:0007829|PDB:6TM2"
FT HELIX 637..640
FT /evidence="ECO:0007829|PDB:6TM2"
FT TURN 641..643
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 651..654
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 656..658
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 666..671
FT /evidence="ECO:0007829|PDB:7PP6"
FT HELIX 678..683
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 684..687
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 695..699
FT /evidence="ECO:0007829|PDB:7PP6"
FT STRAND 702..704
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 708..711
FT /evidence="ECO:0007829|PDB:6TM2"
FT HELIX 715..717
FT /evidence="ECO:0007829|PDB:7PP6"
FT STRAND 744..747
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 784..786
FT /evidence="ECO:0007829|PDB:6TM2"
FT TURN 787..789
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 810..813
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 822..824
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 827..829
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 834..837
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 840..844
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 846..849
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 858..863
FT /evidence="ECO:0007829|PDB:6RBF"
FT TURN 864..866
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 867..869
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 875..877
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 881..889
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 899..908
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 910..913
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 915..924
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 927..932
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 935..940
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 943..945
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 949..954
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 957..962
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 965..970
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 972..974
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 976..980
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 982..984
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 999..1001
FT /evidence="ECO:0007829|PDB:6TM2"
FT HELIX 1014..1020
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1022..1024
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1036..1039
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1041..1043
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1044..1051
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1052..1055
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1057..1059
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1062..1065
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1069..1081
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1087..1105
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1114..1117
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1121..1124
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1133..1135
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1145..1149
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1162..1164
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1169..1171
FT /evidence="ECO:0007829|PDB:7PP6"
FT STRAND 1173..1175
FT /evidence="ECO:0007829|PDB:6RBF"
FT TURN 1176..1179
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1180..1182
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1184..1186
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1189..1193
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1198..1202
FT /evidence="ECO:0007829|PDB:7PP6"
FT STRAND 1205..1213
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1219..1223
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1301..1305
FT /evidence="ECO:0007829|PDB:6TM6"
FT STRAND 1316..1324
FT /evidence="ECO:0007829|PDB:6TM6"
FT TURN 1327..1329
FT /evidence="ECO:0007829|PDB:6TM6"
FT STRAND 1334..1343
FT /evidence="ECO:0007829|PDB:6TM6"
FT HELIX 1348..1351
FT /evidence="ECO:0007829|PDB:6TM6"
FT STRAND 1356..1358
FT /evidence="ECO:0007829|PDB:6TM6"
FT TURN 1359..1361
FT /evidence="ECO:0007829|PDB:6TM6"
FT STRAND 1362..1366
FT /evidence="ECO:0007829|PDB:6TM6"
FT HELIX 1367..1369
FT /evidence="ECO:0007829|PDB:6TM6"
FT TURN 1371..1373
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 1374..1376
FT /evidence="ECO:0007829|PDB:6TM2"
FT STRAND 1382..1391
FT /evidence="ECO:0007829|PDB:6TM6"
FT HELIX 1392..1394
FT /evidence="ECO:0007829|PDB:6TM6"
FT TURN 4428..4430
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4431..4445
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4457..4460
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4463..4466
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4473..4476
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4479..4484
FT /evidence="ECO:0007829|PDB:7QCL"
FT TURN 4485..4487
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4488..4490
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4496..4498
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4505..4512
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4518..4527
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4529..4531
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4536..4543
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4546..4551
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4558..4561
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4571..4575
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4578..4583
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4586..4590
FT /evidence="ECO:0007829|PDB:7QCL"
FT TURN 4592..4594
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4597..4600
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4602..4609
FT /evidence="ECO:0007829|PDB:7QCL"
FT TURN 4611..4613
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4614..4616
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4618..4620
FT /evidence="ECO:0007829|PDB:7QCL"
FT HELIX 4629..4631
FT /evidence="ECO:0007829|PDB:7QCL"
FT HELIX 4644..4648
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4656..4658
FT /evidence="ECO:0007829|PDB:7QCL"
FT HELIX 4691..4694
FT /evidence="ECO:0007829|PDB:7QCL"
FT HELIX 4695..4697
FT /evidence="ECO:0007829|PDB:7QCL"
FT HELIX 4699..4701
FT /evidence="ECO:0007829|PDB:7QCL"
FT HELIX 4702..4705
FT /evidence="ECO:0007829|PDB:7QCL"
FT HELIX 4711..4723
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4724..4728
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4730..4732
FT /evidence="ECO:0007829|PDB:7QCL"
FT HELIX 4733..4743
FT /evidence="ECO:0007829|PDB:7QCL"
FT TURN 4751..4755
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4756..4758
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4766..4772
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4792..4796
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4811..4814
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4829..4831
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4834..4840
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4842..4851
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4877..4879
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4911..4915
FT /evidence="ECO:0007829|PDB:7QCL"
FT TURN 4930..4933
FT /evidence="ECO:0007829|PDB:7QCL"
FT STRAND 4941..4944
FT /evidence="ECO:0007829|PDB:7QCL"
FT TURN 4954..4956
FT /evidence="ECO:0007829|PDB:7QCL"
FT HELIX 4957..4960
FT /evidence="ECO:0007829|PDB:7QCL"
SQ SEQUENCE 5289 AA; 550850 MW; 7AFBC09DA626F0A5 CRC64;
MGLPLARLAA VCLALSLAGG SELQTEGRTR NHGHNVCSTW GNFHYKTFDG DVFRFPGLCD
YNFASDCRGS YKEFAVHLKR GPGQAEAPAG VESILLTIKD DTIYLTRHLA VLNGAVVSTP
HYSPGLLIEK SDAYTKVYSR AGLTLMWNRE DALMLELDTK FRNHTCGLCG DYNGLQSYSE
FLSDGVLFSP LEFGNMQKIN QPDVVCEDPE EEVAPASCSE HRAECERLLT AEAFADCQDL
VPLEPYLRAC QQDRCRCPGG DTCVCSTVAE FSRQCSHAGG RPGNWRTATL CPKTCPGNLV
YLESGSPCMD TCSHLEVSSL CEEHRMDGCF CPEGTVYDDI GDSGCVPVSQ CHCRLHGHLY
TPGQEITNDC EQCVCNAGRW VCKDLPCPGT CALEGGSHIT TFDGKTYTFH GDCYYVLAKG
DHNDSYALLG ELAPCGSTDK QTCLKTVVLL ADKKKNVVVF KSDGSVLLNE LQVNLPHVTA
SFSVFRPSSY HIMVSMAIGV RLQVQLAPVM QLFVTLDQAS QGQVQGLCGN FNGLEGDDFK
TASGLVEATG AGFANTWKAQ SSCHDKLDWL DDPCSLNIES ANYAEHWCSL LKKTETPFGR
CHSAVDPAEY YKRCKYDTCN CQNNEDCLCA ALSSYARACT AKGVMLWGWR EHVCNKDVGS
CPNSQVFLYN LTTCQQTCRS LSEADSHCLE GFAPVDGCGC PDHTFLDEKG RCVPLAKCSC
YHRGLYLEAG DVVVRQEERC VCRDGRLHCR QIRLIGQSCT APKIHMDCSN LTALATSKPR
ALSCQTLAAG YYHTECVSGC VCPDGLMDDG RGGCVVEKEC PCVHNNDLYS SGAKIKVDCN
TCTCKRGRWV CTQAVCHGTC SIYGSGHYIT FDGKYYDFDG HCSYVAVQDY CGQNSSLGSF
SIITENVPCG TTGVTCSKAI KIFMGRTELK LEDKHRVVIQ RDEGHHVAYT TREVGQYLVV
ESSTGIIVIW DKRTTVFIKL APSYKGTVCG LCGNFDHRSN NDFTTRDHMV VSSELDFGNS
WKEAPTCPDV STNPEPCSLN PHRRSWAEKQ CSILKSSVFS ICHSKVDPKP FYEACVHDSC
SCDTGGDCEC FCSAVASYAQ ECTKEGACVF WRTPDLCPIF CDYYNPPHEC EWHYEPCGNR
SFETCRTING IHSNISVSYL EGCYPRCPKD RPIYEEDLKK CVTADKCGCY VEDTHYPPGA
SVPTEETCKS CVCTNSSQVV CRPEEGKILN QTQDGAFCYW EICGPNGTVE KHFNICSITT
RPSTLTTFTT ITLPTTPTTF TTTTTTTTPT SSTVLSTTPK LCCLWSDWIN EDHPSSGSDD
GDRETFDGVC GAPEDIECRS VKDPHLSLEQ LGQKVQCDVS VGFICKNEDQ FGNGPFGLCY
DYKIRVNCCW PMDKCITTPS PPTTTPSPPP TSTTTLPPTT TPSPPTTTTT TPPPTTTPSP
PITTTTTPPP TTTPSPPIST TTTPPPTTTP SPPTTTPSPP TTTPSPPTTT TTTPPPTTTP
SPPTTTPITP PASTTTLPPT TTPSPPTTTT TTPPPTTTPS PPTTTPITPP TSTTTLPPTT
TPSPPPTTTT TPPPTTTPSP PTTTTPSPPT ITTTTPPPTT TPSPPTTTTT TPPPTTTPSP
PTTTPITPPT STTTLPPTTT PSPPPTTTTT PPPTTTPSPP TTTTPSPPIT TTTTPPPTTT
PSSPITTTPS PPTTTMTTPS PTTTPSSPIT TTTTPSSTTT PSPPPTTMTT PSPTTTPSPP
TTTMTTLPPT TTSSPLTTTP LPPSITPPTF SPFSTTTPTT PCVPLCNWTG WLDSGKPNFH
KPGGDTELIG DVCGPGWAAN ISCRATMYPD VPIGQLGQTV VCDVSVGLIC KNEDQKPGGV
IPMAFCLNYE INVQCCECVT QPTTMTTTTT ENPTPTPITT TTTVTPTPTP TSTQSTTPTP
ITTTNTVTPT PTPTGTQTPT PTPITTTTTM VTPTPTITST QTPTPTPITT TTVTPTPTPT
STQRTTPTSI TTTTTVTPTP TPTGTQTPTT TPITTTTTVT PTPTPTGTQT PTTTPISTTT
MVTPTPTPTG TQTLTPTPIT TTTTVTPTPT PTGTQTPTST PISTTTTVTP TPTPTGTQTP
TLTPITTTTT VTPTPTPTGT QTPTTTPITT TTTVTPTPTP TGTKSTTPTS ITTTTMVTPT
PPPTGTQTPT TTPITTTTTV TPTPTPTGTQ TPTPTPITTT TTVTPTPTPT GTQTPTSTPI
TTNTTVTPTP TPTGTPSTTL TPITTTTMVT PTPTPTGTQT PTSTPISTTT TVTPTPTPTG
TQTPTPTPIS TTTTVTPTPT PTSTQTPTTT PITTTTTVTP NPTPTGTQTP TTTPITTTTT
VTPTPTPTGT QTPTTTPIST TTTVTPTPTP TGTQTPTTTA ITTTTTVTPT PTPTGTQTPT
STPITTTTTV TPTPTPTGTQ TPTSTPISNT TTVTPTPTPT GTQTPTVTPI TTTTTVTPTR
TPTGTKSTTP TSITTTTMVT PTPTPTGTHT PTTTPITTTT TVTPTPTPTG TQTPTPTPIT
TTTTVTPTPT PTGTQTPTST PITTTTTVTP TPTPTGTQTP TTTPITTNTT VTPTPTPTGT
QTPTTVLITT TTTMTPTPTP TSTKSTTVTP ITTTTTVTPT PTPTGTQSTT LTPITTTTTV
TPTPTPTGTQ TPTTTPISTT TTVIPTPTPT GTQTPTSTPI TTTTTVTPTP TPTGTQTPTS
TPISTTTTVT PTATPTGTQT PTLTPITTTT TVTSTPTPTG TQTPTPTPIT TTTTVTPTPT
PTSTQTPTST PITTTTTVTP TPTPTGTQTP TTTHITTTTT VTPTPTPTGT QAPTPTAITT
TTTVTPTPTP TGTQTPTTTP ITTTTTVTPT PTPTGTQSPT PTAITTTTTV TPTPTPTGTQ
TPTTTPITTT TTVTPTPTPT GTQSTTLTPI TTTTTVTPIP TPTGTQTPTS TPITTTITVT
PTPTPTGTQT PTPTPISTTT TVTPTPTPTG TQTPTTTPIT TTTTVTPTPT PTGTQTPTTT
PISTTTTVTP TPTPTGTQTP TSTPITTTTT VTPTPTPTGT QTPTPTPITT TTTVTPTPTP
TGTQTPTSTP ITTTTTVTPT PTPTGTQTPT PTPITTTTTV TPTPTPTGTQ TPTSTPITTT
TTVTPTPTPT GTQTPTTTPI TTTTTVTPTP TPTGTQSTTL TPITTTTTVT PTPTPTGTQT
PTSTPITTTT TVTPTPTGTQ TPTPTPISTT TTVTPTPTPT GTQTPTMTPI TTTTTVTPTP
TPTGTQTPTT TPISTTTTVT PTPTPTGTQT PTSTPITTTT TVTPTPTPTG TQTPTTTPIT
TTTTVTPTPT PTGTQSTTLT PITTTTTVTP TPTPTGTQTP TPTPISTTTT VTPTPTPTGT
QTPTTTPITT TTTVTPTPTP TGTQTPTTTP ISTTTTVTPT PTPTGTQTPT STPITTTTTV
TPTPTPTGTQ TPTTTPITTT TTVTPTPTPT GTQAPTPTAI TTTTTVTPTP TPTGTQTPTT
TPITTTTMVT PTPTPTGTQT PTSTPITTTT TVTPTPTPTG TQTPTPTPIS TTTTVTPTPT
PTGTQTPTTT PITTTTTVTP TPTPTGTQTP TTTPISTTTT VTPTPTPTGT QTPTSTPITT
TTTVTPTPTP TGTQTPTPTP ITTTTTVTPT PTPTGTQTPT STPITTTTTV TPTPTPTGTQ
TPTTTPITTT TTVTPTPTPT GTQSTTLTPI TTTTTVTPTP TPTGTQTPTS TPITTTTTVT
PTPTPTGTQT PTPTPISTTS TVTPTPTPTG TQTPTMTPIT TTTTVTPTPT PTGTQTPTST
PITTTTTVTP TPTPTGTQTP TMTPITTTTT VTPTPTPTGT QAPTPTAITT TTTVTPTPTP
TGTQTPTTTP ITTTTTVTPT PTPTGTQSTT LTPITTTTTV TPTPTPTGTQ TPTPTPISTT
TTVTPTPTPT GTQTPTMTPI TTTTTVTPTP TPTGTQTPTT TPISTTTTVT PTPTPTGTQT
PTTTPITTTT TVTPTPTPTG TQTPTTTPIS TTTTVTPTPT PTGTQTPTTT PITTTTTVTP
TPTPTGTQTP TTTPISTTTT VTPTPTPTGT QTPTSTPITT TTTVTPTPTP TGTQTPTTTP
ITTTTTVTPT PTPTGTQAPT PTAITTTSTV TPTPTPTGTQ TPTTTPITTT TTVTPTPTPT
GTQSPTPTAI TTTTTVTPTP TPTGTQTPTL TPITTTTTVT PTPTPTGTQT PTPTPISTTT
TVTPTPTPTG TQTPTTTPIT TTTTVTPTPT PTGTQTPTTV LITTTTTMTP TPTPTSTKST
TVTPITTTTT VTATPTPTGT QTPTMIPIST TTTVTPTPTP TTGSTGPPTH TSTAPIAELT
TSNPPPESST PQTSRSTSSP LTESTTLLST LPPAIEMTST APPSTPTAPT TTSGGHTLSP
PPSTTTSPPG TPTRGTTTGS SSAPTPSTVQ TTTTSAWTPT PTPLSTPSII RTTGLRPYPS
SVLICCVLND TYYAPGEEVY NGTYGDTCYF VNCSLSCTLE FYNWSCPSTP SPTPTPSKST
PTPSKPSSTP SKPTPGTKPP ECPDFDPPRQ ENETWWLCDC FMATCKYNNT VEIVKVECEP
PPMPTCSNGL QPVRVEDPDG CCWHWECDCY CTGWGDPHYV TFDGLYYSYQ GNCTYVLVEE
ISPSVDNFGV YIDNYHCDPN DKVSCPRTLI VRHETQEVLI KTVHMMPMQV QVQVNRQAVA
LPYKKYGLEV YQSGINYVVD IPELGVLVSY NGLSFSVRLP YHRFGNNTKG QCGTCTNTTS
DDCILPSGEI VSNCEAAADQ WLVNDPSKPH CPHSSSTTKR PAVTVPGGGK TTPHKDCTPS
PLCQLIKDSL FAQCHALVPP QHYYDACVFD SCFMPGSSLE CASLQAYAAL CAQQNICLDW
RNHTHGACLV ECPSHREYQA CGPAEEPTCK SSSSQQNNTV LVEGCFCPEG TMNYAPGFDV
CVKTCGCVGP DNVPREFGEH FEFDCKNCVC LEGGSGIICQ PKRCSQKPVT HCVEDGTYLA
TEVNPADTCC NITVCKCNTS LCKEKPSVCP LGFEVKSKMV PGRCCPFYWC ESKGVCVHGN
AEYQPGSPVY SSKCQDCVCT DKVDNNTLLN VIACTHVPCN TSCSPGFELM EAPGECCKKC
EQTHCIIKRP DNQHVILKPG DFKSDPKNNC TFFSCVKIHN QLISSVSNIT CPNFDASICI
PGSITFMPNG CCKTCTPRNE TRVPCSTVPV TTEVSYAGCT KTVLMNHCSG SCGTFVMYSA
KAQALDHSCS CCKEEKTSQR EVVLSCPNGG SLTHTYTHIE SCQCQDTVCG LPTGTSRRAR
RSPRHLGSG
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