ID LOXL4_HUMAN Reviewed; 756 AA.
AC Q96JB6; Q5W0B3; Q96DY1; Q96PC0; Q9H6T5;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 186.
DE RecName: Full=Lysyl oxidase homolog 4;
DE EC=1.4.3.13 {ECO:0000269|PubMed:14551188};
DE AltName: Full=Lysyl oxidase-like protein 4;
DE AltName: Full=Lysyl oxidase-related protein C;
DE Flags: Precursor;
GN Name=LOXL4; Synonyms=LOXC;
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].
RC TISSUE=Testis;
RX PubMed=11292829; DOI=10.1074/jbc.m100861200;
RA Ito H., Akiyama H., Iguchi H., Iyama K., Miyamoto M., Ohsawa K.,
RA Nakamura T.;
RT "Molecular cloning and biological activity of a novel lysyl oxidase-related
RT gene expressed in cartilage.";
RL J. Biol. Chem. 276:24023-24029(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11691589; DOI=10.1016/s0945-053x(01)00157-3;
RA Maeki J.M., Tikkanen H., Kivirikko K.I.;
RT "Cloning and characterization of a fifth human lysyl oxidase isoenzyme: the
RT third member of the lysyl oxidase-related subfamily with four scavenger
RT receptor cysteine-rich domains.";
RL Matrix Biol. 20:493-496(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=11691588; DOI=10.1016/s0945-053x(01)00161-5;
RA Asuncion L., Fogelgren B., Fong K.S.K., Fong S.F.T., Kim Y., Csiszar K.;
RT "A novel human lysyl oxidase-like gene (LOXL4) on chromosome 10q24 has an
RT altered scavenger receptor cysteine rich domain.";
RL Matrix Biol. 20:487-491(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-405.
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=14551188; DOI=10.1074/jbc.m308856200;
RA Kim M.S., Kim S.S., Jung S.T., Park J.Y., Yoo H.W., Ko J., Csiszar K.,
RA Choi S.Y., Kim Y.;
RT "Expression and purification of enzymatically active forms of the human
RT lysyl oxidase-like protein 4.";
RL J. Biol. Chem. 278:52071-52074(2003).
CC -!- FUNCTION: Catalyzes the oxidative deamination of lysine and
CC hydroxylysine residues in collagen and elastin, resulting in the
CC formation of covalent cross-linkages, and the stabilization of collagen
CC and elastin fibers. {ECO:0000269|PubMed:14551188}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-
CC [protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:131803; EC=1.4.3.13;
CC Evidence={ECO:0000269|PubMed:14551188};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P16636};
CC -!- COFACTOR:
CC Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489;
CC Evidence={ECO:0000250|UniProtKB:P33072};
CC Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072};
CC -!- ACTIVITY REGULATION: Inhibited by beta-aminopropionitrile (BAPN).
CC {ECO:0000269|PubMed:14551188}.
CC -!- INTERACTION:
CC Q96JB6; Q86V38: ATN1; NbExp=3; IntAct=EBI-749562, EBI-11954292;
CC Q96JB6; P55212: CASP6; NbExp=3; IntAct=EBI-749562, EBI-718729;
CC Q96JB6; P02489: CRYAA; NbExp=3; IntAct=EBI-749562, EBI-6875961;
CC Q96JB6; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-749562, EBI-12593112;
CC Q96JB6; P22607: FGFR3; NbExp=3; IntAct=EBI-749562, EBI-348399;
CC Q96JB6; Q14957: GRIN2C; NbExp=3; IntAct=EBI-749562, EBI-8285963;
CC Q96JB6; P28799: GRN; NbExp=3; IntAct=EBI-749562, EBI-747754;
CC Q96JB6; P06396: GSN; NbExp=3; IntAct=EBI-749562, EBI-351506;
CC Q96JB6; P04792: HSPB1; NbExp=3; IntAct=EBI-749562, EBI-352682;
CC Q96JB6; O60341: KDM1A; NbExp=2; IntAct=EBI-749562, EBI-710124;
CC Q96JB6; O60333-2: KIF1B; NbExp=3; IntAct=EBI-749562, EBI-10975473;
CC Q96JB6; O14901: KLF11; NbExp=3; IntAct=EBI-749562, EBI-948266;
CC Q96JB6; Q92876: KLK6; NbExp=3; IntAct=EBI-749562, EBI-2432309;
CC Q96JB6; P13473-2: LAMP2; NbExp=3; IntAct=EBI-749562, EBI-21591415;
CC Q96JB6; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-749562, EBI-912440;
CC Q96JB6; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-749562, EBI-396669;
CC Q96JB6; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-749562, EBI-5235340;
CC Q96JB6; Q15645: TRIP13; NbExp=6; IntAct=EBI-749562, EBI-358993;
CC Q96JB6; O76024: WFS1; NbExp=3; IntAct=EBI-749562, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in many tissues, the highest levels among
CC the tissues studied being in the skeletal muscle, testis and pancreas.
CC Expressed in cartilage.
CC -!- PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by
CC condensation of the epsilon-amino group of a lysine with a topaquinone
CC produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:P33072}.
CC -!- PTM: May be proteolytically cleaved by BMP1.
CC {ECO:0000305|PubMed:14551188}.
CC -!- SIMILARITY: Belongs to the lysyl oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07522.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/41193/LOXL4";
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DR EMBL; AF338441; AAK71934.1; -; mRNA.
DR EMBL; AY036093; AAK64186.1; -; mRNA.
DR EMBL; AF395336; AAL27543.1; -; mRNA.
DR EMBL; AK025542; BAB15167.1; -; mRNA.
DR EMBL; AK172781; BAD18762.1; -; mRNA.
DR EMBL; AL139241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49886.1; -; Genomic_DNA.
DR EMBL; BC007522; AAH07522.1; ALT_INIT; mRNA.
DR EMBL; BC013153; AAH13153.1; -; mRNA.
DR CCDS; CCDS7473.1; -.
DR RefSeq; NP_115587.6; NM_032211.6.
DR AlphaFoldDB; Q96JB6; -.
DR SMR; Q96JB6; -.
DR BioGRID; 123925; 123.
DR IntAct; Q96JB6; 33.
DR MINT; Q96JB6; -.
DR STRING; 9606.ENSP00000260702; -.
DR BindingDB; Q96JB6; -.
DR ChEMBL; CHEMBL4295926; -.
DR GlyConnect; 1482; 1 N-Linked glycan (1 site).
DR GlyCosmos; Q96JB6; 2 sites, No reported glycans.
DR GlyGen; Q96JB6; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q96JB6; -.
DR PhosphoSitePlus; Q96JB6; -.
DR BioMuta; LOXL4; -.
DR DMDM; 20177960; -.
DR EPD; Q96JB6; -.
DR jPOST; Q96JB6; -.
DR MassIVE; Q96JB6; -.
DR MaxQB; Q96JB6; -.
DR PaxDb; 9606-ENSP00000260702; -.
DR PeptideAtlas; Q96JB6; -.
DR ProteomicsDB; 76933; -.
DR Pumba; Q96JB6; -.
DR Antibodypedia; 31028; 253 antibodies from 23 providers.
DR DNASU; 84171; -.
DR Ensembl; ENST00000260702.4; ENSP00000260702.3; ENSG00000138131.4.
DR GeneID; 84171; -.
DR KEGG; hsa:84171; -.
DR MANE-Select; ENST00000260702.4; ENSP00000260702.3; NM_032211.7; NP_115587.6.
DR UCSC; uc001kpa.2; human.
DR AGR; HGNC:17171; -.
DR CTD; 84171; -.
DR DisGeNET; 84171; -.
DR GeneCards; LOXL4; -.
DR HGNC; HGNC:17171; LOXL4.
DR HPA; ENSG00000138131; Low tissue specificity.
DR MIM; 607318; gene.
DR neXtProt; NX_Q96JB6; -.
DR OpenTargets; ENSG00000138131; -.
DR PharmGKB; PA30431; -.
DR VEuPathDB; HostDB:ENSG00000138131; -.
DR eggNOG; ENOG502QSX8; Eukaryota.
DR GeneTree; ENSGT00940000157042; -.
DR HOGENOM; CLU_002555_3_0_1; -.
DR InParanoid; Q96JB6; -.
DR OMA; HMSEVRC; -.
DR OrthoDB; 3035117at2759; -.
DR PhylomeDB; Q96JB6; -.
DR TreeFam; TF326061; -.
DR PathwayCommons; Q96JB6; -.
DR Reactome; R-HSA-1566948; Elastic fibre formation.
DR Reactome; R-HSA-2243919; Crosslinking of collagen fibrils.
DR SignaLink; Q96JB6; -.
DR BioGRID-ORCS; 84171; 9 hits in 1145 CRISPR screens.
DR ChiTaRS; LOXL4; human.
DR GeneWiki; LOXL4; -.
DR GenomeRNAi; 84171; -.
DR Pharos; Q96JB6; Tchem.
DR PRO; PR:Q96JB6; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q96JB6; Protein.
DR Bgee; ENSG00000138131; Expressed in tibia and 140 other cell types or tissues.
DR Genevisible; Q96JB6; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; IDA:UniProtKB.
DR GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR Gene3D; 3.10.250.10; SRCR-like domain; 4.
DR InterPro; IPR001695; Lysyl_oxidase.
DR InterPro; IPR019828; Lysyl_oxidase_CS.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR PANTHER; PTHR45817:SF5; LYSYL OXIDASE HOMOLOG 4; 1.
DR PANTHER; PTHR45817; LYSYL OXIDASE-LIKE-RELATED; 1.
DR Pfam; PF01186; Lysyl_oxidase; 1.
DR Pfam; PF00530; SRCR; 4.
DR PRINTS; PR00074; LYSYLOXIDASE.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 4.
DR SUPFAM; SSF56487; SRCR-like; 4.
DR PROSITE; PS00926; LYSYL_OXIDASE; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 4.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Disulfide bond; Glycoprotein; LTQ;
KW Metal-binding; Oxidoreductase; Reference proteome; Repeat; Secreted;
KW Signal; TPQ.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..756
FT /note="Lysyl oxidase homolog 4"
FT /id="PRO_0000018535"
FT DOMAIN 32..133
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 159..287
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 311..411
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 421..529
FT /note="SRCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT REGION 533..736
FT /note="Lysyl-oxidase like"
FT BINDING 611
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 613
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 615
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT SITE 569..570
FT /note="Cleavage; by BMP1"
FT /evidence="ECO:0000305|PubMed:14551188"
FT MOD_RES 674
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 71..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 102..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 191..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 204..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 251..261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 336..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 349..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 380..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 450..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 463..528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 497..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 558..564
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 610..658
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 642..648
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 670..680
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 717..731
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT CROSSLNK 638..674
FT /note="Lysine tyrosylquinone (Lys-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT VARIANT 154
FT /note="R -> Q (in dbSNP:rs33995374)"
FT /id="VAR_050012"
FT VARIANT 372
FT /note="P -> T (in dbSNP:rs11189525)"
FT /id="VAR_059431"
FT VARIANT 405
FT /note="D -> A (in dbSNP:rs1983864)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_050013"
FT CONFLICT 3
FT /note="W -> R (in Ref. 7; AAH13153)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="R -> Q (in Ref. 7; AAH13153)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="S -> G (in Ref. 3; AAL27543)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="A -> T (in Ref. 3; AAL27543)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="V -> A (in Ref. 3; AAL27543)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="Y -> H (in Ref. 3; AAL27543)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 756 AA; 84483 MW; 13051ACADB922BBC CRC64;
MAWSPPATLF LFLLLLGQPP PSRPQSLGTT KLRLVGPESK PEEGRLEVLH QGQWGTVCDD
NFAIQEATVA CRQLGFEAAL TWAHSAKYGQ GEGPIWLDNV RCVGTESSLD QCGSNGWGVS
DCSHSEDVGV ICHPRRHRGY LSETVSNALG PQGRRLEEVR LKPILASAKQ HSPVTEGAVE
VKYEGHWRQV CDQGWTMNNS RVVCGMLGFP SEVPVDSHYY RKVWDLKMRD PKSRLKSLTN
KNSFWIHQVT CLGTEPHMAN CQVQVAPARG KLRPACPGGM HAVVSCVAGP HFRPPKTKPQ
RKGSWAEEPR VRLRSGAQVG EGRVEVLMNR QWGTVCDHRW NLISASVVCR QLGFGSAREA
LFGARLGQGL GPIHLSEVRC RGYERTLSDC PALEGSQNGC QHENDAAVRC NVPNMGFQNQ
VRLAGGRIPE EGLLEVQVEV NGVPRWGSVC SENWGLTEAM VACRQLGLGF AIHAYKETWF
WSGTPRAQEV VMSGVRCSGT ELALQQCQRH GPVHCSHGGG RFLAGVSCMD SAPDLVMNAQ
LVQETAYLED RPLSQLYCAH EENCLSKSAD HMDWPYGYRR LLRFSTQIYN LGRTDFRPKT
GRDSWVWHQC HRHYHSIEVF THYDLLTLNG SKVAEGHKAS FCLEDTNCPT GLQRRYACAN
FGEQGVTVGC WDTYRHDIDC QWVDITDVGP GNYIFQVIVN PHYEVAESDF SNNMLQCRCK
YDGHRVWLHN CHTGNSYPAN AELSLEQEQR LRNNLI
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