GenomeNet

Database: UniProt
Entry: P10643
LinkDB: P10643
Original site: P10643 
ID   CO7_HUMAN               Reviewed;         843 AA.
AC   P10643; A8K2T4; Q6P3T5; Q92489;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   29-SEP-2021, entry version 211.
DE   RecName: Full=Complement component C7;
DE   Flags: Precursor;
GN   Name=C7;
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], PARTIAL PROTEIN SEQUENCE, AND VARIANT PRO-587.
RX   PubMed=3335508;
RA   Discipio R.G., Chakravari D.N., Mueller-Eberhard H.J., Fey G.H.;
RT   "The structure of human complement component C7 and the C5b-7 complex.";
RL   J. Biol. Chem. 263:549-560(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-222.
RC   TISSUE=Tongue;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PNS;
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-822, AND VARIANT THR-389.
RX   PubMed=7730625;
RA   Hobart M.J., Fernie B.A., DiScipio R.G.;
RT   "Structure of the human C7 gene and comparison with the C6, C8A, C8B and C9
RT   genes.";
RL   J. Immunol. 154:5188-5194(1995).
RN   [5]
RP   GLYCOSYLATION AT TRP-36; TRP-503; TRP-506 AND TRP-509.
RX   PubMed=10551839; DOI=10.1074/jbc.274.46.32786;
RA   Hofsteenge J., Blommers M., Hess D., Furmanek A., Miroshnichenko O.;
RT   "The four terminal components of the complement system are C-mannosylated
RT   on multiple tryptophan residues.";
RL   J. Biol. Chem. 274:32786-32794(1999).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202.
RC   TISSUE=Plasma;
RX   PubMed=14760718; DOI=10.1002/pmic.200300556;
RA   Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT   "Screening for N-glycosylated proteins by liquid chromatography mass
RT   spectrometry.";
RL   Proteomics 4:454-465(2004).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202 AND ASN-754.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [8]
RP   GLYCOSYLATION AT ASN-754.
RX   PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA   Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA   Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA   Ying W.T., He S.M., Qian X.H.;
RT   "A strategy for precise and large scale identification of core fucosylated
RT   glycoproteins.";
RL   Mol. Cell. Proteomics 8:913-923(2009).
RN   [9]
RP   GLYCOSYLATION AT THR-696, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA   Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT   "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT   O-linked glycosylations by CID and ECD.";
RL   Mol. Cell. Proteomics 11:1-17(2012).
RN   [10]
RP   STRUCTURE BY NMR OF 693-843, AND DISULFIDE BONDS.
RX   PubMed=19419965; DOI=10.1074/jbc.m901993200;
RA   Phelan M.M., Thai C.-T., Soares D.C., Ogata R.T., Barlow P.N., Bramham J.;
RT   "Solution structure of factor I-like modules from complement C7 reveals a
RT   pair of follistatin domains in compact pseudosymmetric arrangement.";
RL   J. Biol. Chem. 284:19637-19649(2009).
RN   [11]
RP   VARIANT C7D SER-521.
RX   PubMed=8871666;
RA   Fernie B.A., Wurzner R., Orren A., Morgan B.P., Potter P.C., Platonov A.E.,
RA   Vershinina I.V., Shipulin G.A., Lachmann P.J., Hobart M.J.;
RT   "Molecular bases of combined subtotal deficiencies of C6 and C7: their
RT   effects in combination with other C6 and C7 deficiencies.";
RL   J. Immunol. 157:3648-3657(1996).
RN   [12]
RP   VARIANT C7D ARG-379.
RX   PubMed=9218625;
RA   Fernie B.A., Orren A., Sheehan G., Schlesinger M., Hobart M.J.;
RT   "Molecular bases of C7 deficiency: three different defects.";
RL   J. Immunol. 159:1019-1026(1997).
RN   [13]
RP   VARIANTS C7D GLN-220; GLN-682 AND HIS-687.
RX   PubMed=9856499; DOI=10.1007/s004390050859;
RA   Fernie B.A., Hobart M.J.;
RT   "Complement C7 deficiency: seven further molecular defects and their
RT   associated marker haplotypes.";
RL   Hum. Genet. 103:513-519(1998).
RN   [14]
RP   VARIANTS THR-389 AND PRO-587, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=22028381; DOI=10.1093/jmcb/mjr024;
RA   Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X.,
RA   Zeng R., Wu J.R.;
RT   "Quantitative detection of single amino acid polymorphisms by targeted
RT   proteomics.";
RL   J. Mol. Cell Biol. 3:309-315(2011).
CC   -!- FUNCTION: Constituent of the membrane attack complex (MAC) that plays a
CC       key role in the innate and adaptive immune response by forming pores in
CC       the plasma membrane of target cells. C7 serves as a membrane anchor.
CC   -!- SUBUNIT: Monomer or dimer; as a C5b-7 complex it can also form
CC       multimeric rosettes. MAC assembly is initiated by proteolytic cleavage
CC       of C5 into C5a and C5b. C5b binds sequentially C6, C7, C8 and multiple
CC       copies of the pore-forming subunit C9.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: C7 has 28 disulfide bridges.
CC   -!- PTM: C-, N- and O-glycosylated. O-glycosylated with core 1 or possibly
CC       core 8 glycans. {ECO:0000269|PubMed:10551839,
CC       ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952,
CC       ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:22171320}.
CC   -!- DISEASE: Complement component 7 deficiency (C7D) [MIM:610102]: A rare
CC       defect of the complement classical pathway associated with
CC       susceptibility to severe recurrent infections, predominantly by
CC       Neisseria gonorrhoeae or Neisseria meningitidis.
CC       {ECO:0000269|PubMed:8871666, ECO:0000269|PubMed:9218625,
CC       ECO:0000269|PubMed:9856499}. Note=Disease susceptibility is associated
CC       with variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=C7base; Note=C7 mutation db;
CC       URL="http://structure.bmc.lu.se/idbase/C7base/";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J03507; AAA51861.1; -; mRNA.
DR   EMBL; AK290349; BAF83038.1; -; mRNA.
DR   EMBL; BC063851; AAH63851.1; -; mRNA.
DR   EMBL; X86328; CAA60121.1; -; Genomic_DNA.
DR   EMBL; X86329; CAA60121.1; JOINED; Genomic_DNA.
DR   EMBL; X86330; CAA60121.1; JOINED; Genomic_DNA.
DR   EMBL; X86331; CAA60121.1; JOINED; Genomic_DNA.
DR   EMBL; X86332; CAA60121.1; JOINED; Genomic_DNA.
DR   EMBL; X86333; CAA60121.1; JOINED; Genomic_DNA.
DR   EMBL; X86334; CAA60121.1; JOINED; Genomic_DNA.
DR   EMBL; X86335; CAA60121.1; JOINED; Genomic_DNA.
DR   EMBL; X86336; CAA60121.1; JOINED; Genomic_DNA.
DR   EMBL; X86337; CAA60121.1; JOINED; Genomic_DNA.
DR   EMBL; X86338; CAA60121.1; JOINED; Genomic_DNA.
DR   EMBL; X86339; CAA60121.1; JOINED; Genomic_DNA.
DR   EMBL; X86340; CAA60121.1; JOINED; Genomic_DNA.
DR   EMBL; X86341; CAA60121.1; JOINED; Genomic_DNA.
DR   EMBL; X86342; CAA60121.1; JOINED; Genomic_DNA.
DR   EMBL; X86343; CAA60121.1; JOINED; Genomic_DNA.
DR   EMBL; X86344; CAA60121.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS47201.1; -.
DR   PIR; A27340; A27340.
DR   RefSeq; NP_000578.2; NM_000587.3.
DR   PDB; 2WCY; NMR; -; A=693-843.
DR   PDB; 6H03; EM; 5.60 A; D=23-843.
DR   PDB; 6H04; EM; 5.60 A; D=23-843.
DR   PDBsum; 2WCY; -.
DR   PDBsum; 6H03; -.
DR   PDBsum; 6H04; -.
DR   BMRB; P10643; -.
DR   SMR; P10643; -.
DR   BioGRID; 107191; 4.
DR   ComplexPortal; CPX-6159; Membrane attack complex.
DR   IntAct; P10643; 4.
DR   STRING; 9606.ENSP00000322061; -.
DR   GlyConnect; 807; 2 N-Linked glycans (2 sites), 1 O-Linked glycan (1 site).
DR   GlyGen; P10643; 7 sites, 3 N-linked glycans (2 sites), 2 O-linked glycans (1 site).
DR   iPTMnet; P10643; -.
DR   PhosphoSitePlus; P10643; -.
DR   BioMuta; C7; -.
DR   DMDM; 61252057; -.
DR   CPTAC; non-CPTAC-2655; -.
DR   jPOST; P10643; -.
DR   MassIVE; P10643; -.
DR   PaxDb; P10643; -.
DR   PeptideAtlas; P10643; -.
DR   PRIDE; P10643; -.
DR   ProteomicsDB; 52633; -.
DR   Antibodypedia; 709; 312 antibodies.
DR   DNASU; 730; -.
DR   Ensembl; ENST00000313164; ENSP00000322061; ENSG00000112936.
DR   GeneID; 730; -.
DR   KEGG; hsa:730; -.
DR   UCSC; uc003jmh.5; human.
DR   CTD; 730; -.
DR   DisGeNET; 730; -.
DR   GeneCards; C7; -.
DR   HGNC; HGNC:1346; C7.
DR   HPA; ENSG00000112936; Tissue enhanced (ovary).
DR   MalaCards; C7; -.
DR   MIM; 217070; gene.
DR   MIM; 610102; phenotype.
DR   neXtProt; NX_P10643; -.
DR   OpenTargets; ENSG00000112936; -.
DR   Orphanet; 169150; Immunodeficiency due to a late component of complement deficiency.
DR   PharmGKB; PA25941; -.
DR   VEuPathDB; HostDB:ENSG00000112936; -.
DR   eggNOG; ENOG502QU3G; Eukaryota.
DR   GeneTree; ENSGT00940000156804; -.
DR   HOGENOM; CLU_014082_0_0_1; -.
DR   InParanoid; P10643; -.
DR   OMA; CKLHVLH; -.
DR   OrthoDB; 100680at2759; -.
DR   PhylomeDB; P10643; -.
DR   TreeFam; TF330498; -.
DR   PathwayCommons; P10643; -.
DR   Reactome; R-HSA-166665; Terminal pathway of complement.
DR   Reactome; R-HSA-977606; Regulation of Complement cascade.
DR   SIGNOR; P10643; -.
DR   BioGRID-ORCS; 730; 3 hits in 1013 CRISPR screens.
DR   ChiTaRS; C7; human.
DR   EvolutionaryTrace; P10643; -.
DR   GenomeRNAi; 730; -.
DR   Pharos; P10643; Tbio.
DR   PRO; PR:P10643; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; P10643; protein.
DR   Bgee; ENSG00000112936; Expressed in adrenal cortex and 207 other tissues.
DR   Genevisible; P10643; HS.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005579; C:membrane attack complex; IDA:UniProtKB.
DR   GO; GO:0006883; P:cellular sodium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0006956; P:complement activation; TAS:ProtInc.
DR   GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   CDD; cd00033; CCP; 2.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 2.20.100.10; -; 2.
DR   Gene3D; 4.10.400.10; -; 1.
DR   InterPro; IPR037564; Complement_C7.
DR   InterPro; IPR003884; FacI_MAC.
DR   InterPro; IPR040729; Kazal_3.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR001862; MAC_perforin.
DR   InterPro; IPR020864; MACPF.
DR   InterPro; IPR020863; MACPF_CS.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR45742:SF2; PTHR45742:SF2; 1.
DR   Pfam; PF18434; Kazal_3; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF01823; MACPF; 1.
DR   Pfam; PF00084; Sushi; 2.
DR   Pfam; PF00090; TSP_1; 2.
DR   PRINTS; PR00764; COMPLEMENTC9.
DR   SMART; SM00032; CCP; 2.
DR   SMART; SM00057; FIMAC; 2.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00457; MACPF; 1.
DR   SMART; SM00209; TSP1; 2.
DR   SUPFAM; SSF57535; SSF57535; 2.
DR   SUPFAM; SSF82895; SSF82895; 2.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS00279; MACPF_1; 1.
DR   PROSITE; PS51412; MACPF_2; 1.
DR   PROSITE; PS50923; SUSHI; 2.
DR   PROSITE; PS50092; TSP1; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Complement alternate pathway; Complement pathway; Cytolysis;
KW   Direct protein sequencing; Disease variant; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Immunity; Innate immunity;
KW   Membrane attack complex; Reference proteome; Repeat; Secreted; Signal;
KW   Sushi.
FT   SIGNAL          1..22
FT   CHAIN           23..843
FT                   /note="Complement component C7"
FT                   /id="PRO_0000023583"
FT   DOMAIN          27..80
FT                   /note="TSP type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          83..121
FT                   /note="LDL-receptor class A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          124..456
FT                   /note="MACPF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT   DOMAIN          457..487
FT                   /note="EGF-like"
FT   DOMAIN          500..549
FT                   /note="TSP type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          569..628
FT                   /note="Sushi 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          629..690
FT                   /note="Sushi 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   REGION          108..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..615
FT                   /note="CCP 1"
FT   REGION          616..693
FT                   /note="CCP 2"
FT   REGION          695..770
FT                   /note="Factor I module (FIM) 1"
FT   REGION          771..843
FT                   /note="Factor I module (FIM) 2"
FT   COMPBIAS        222..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        36
FT                   /note="C-linked (Man) tryptophan"
FT                   /evidence="ECO:0000269|PubMed:10551839"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14760718,
FT                   ECO:0000269|PubMed:16335952"
FT   CARBOHYD        503
FT                   /note="C-linked (Man) tryptophan; partial"
FT                   /evidence="ECO:0000269|PubMed:10551839"
FT   CARBOHYD        506
FT                   /note="C-linked (Man) tryptophan; partial"
FT                   /evidence="ECO:0000269|PubMed:10551839"
FT   CARBOHYD        509
FT                   /note="C-linked (Man) tryptophan; partial"
FT                   /evidence="ECO:0000269|PubMed:10551839"
FT   CARBOHYD        696
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:22171320"
FT   CARBOHYD        754
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19139490"
FT   DISULFID        85..96
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..109
FT                   /evidence="ECO:0000250"
FT   DISULFID        103..119
FT                   /evidence="ECO:0000250"
FT   DISULFID        128..165
FT                   /evidence="ECO:0000250"
FT   DISULFID        337..353
FT                   /evidence="ECO:0000269|PubMed:19419965"
FT   DISULFID        571..613
FT                   /evidence="ECO:0000250"
FT   DISULFID        599..626
FT                   /evidence="ECO:0000250"
FT   DISULFID        631..673
FT                   /evidence="ECO:0000250"
FT   DISULFID        659..688
FT                   /evidence="ECO:0000250"
FT   DISULFID        702..713
FT                   /evidence="ECO:0000269|PubMed:19419965"
FT   DISULFID        715..750
FT                   /evidence="ECO:0000269|PubMed:19419965"
FT   DISULFID        721..743
FT                   /evidence="ECO:0000269|PubMed:19419965"
FT   DISULFID        728..763
FT                   /evidence="ECO:0000269|PubMed:19419965"
FT   DISULFID        773..782
FT                   /evidence="ECO:0000269|PubMed:19419965"
FT   DISULFID        776..789
FT                   /evidence="ECO:0000269|PubMed:19419965"
FT   DISULFID        791..825
FT                   /evidence="ECO:0000269|PubMed:19419965"
FT   DISULFID        797..818
FT                   /evidence="ECO:0000269|PubMed:19419965"
FT   DISULFID        805..838
FT                   /evidence="ECO:0000269|PubMed:19419965"
FT   VARIANT         128
FT                   /note="C -> R (in dbSNP:rs2271708)"
FT                   /id="VAR_050480"
FT   VARIANT         220
FT                   /note="R -> Q (in C7D; dbSNP:rs369349760)"
FT                   /evidence="ECO:0000269|PubMed:9856499"
FT                   /id="VAR_012643"
FT   VARIANT         222
FT                   /note="R -> H (in dbSNP:rs75345202)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_081726"
FT   VARIANT         379
FT                   /note="G -> R (in C7D; dbSNP:rs121964921)"
FT                   /evidence="ECO:0000269|PubMed:9218625"
FT                   /id="VAR_012644"
FT   VARIANT         389
FT                   /note="S -> T (confirmed at protein level;
FT                   dbSNP:rs1063499)"
FT                   /evidence="ECO:0000269|PubMed:22028381,
FT                   ECO:0000269|PubMed:7730625"
FT                   /id="VAR_033798"
FT   VARIANT         420
FT                   /note="K -> Q (in dbSNP:rs3792646)"
FT                   /id="VAR_022023"
FT   VARIANT         521
FT                   /note="R -> S (in C7D; dbSNP:rs121964920)"
FT                   /evidence="ECO:0000269|PubMed:8871666"
FT                   /id="VAR_012645"
FT   VARIANT         587
FT                   /note="T -> P (confirmed at protein level;
FT                   dbSNP:rs13157656)"
FT                   /evidence="ECO:0000269|PubMed:22028381,
FT                   ECO:0000269|PubMed:3335508"
FT                   /id="VAR_033799"
FT   VARIANT         682
FT                   /note="E -> Q (in C7D; dbSNP:rs541873000)"
FT                   /evidence="ECO:0000269|PubMed:9856499"
FT                   /id="VAR_012646"
FT   VARIANT         687
FT                   /note="R -> H (in C7D; dbSNP:rs113187203)"
FT                   /evidence="ECO:0000269|PubMed:9856499"
FT                   /id="VAR_012647"
FT   CONFLICT        18
FT                   /note="S -> G (in Ref. 2; BAF83038)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="E -> G (in Ref. 2; BAF83038)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152
FT                   /note="R -> V (in Ref. 4; CAA60121)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="S -> P (in Ref. 2; BAF83038)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        821..822
FT                   /note="GA -> AL (in Ref. 4; CAA60121)"
FT                   /evidence="ECO:0000305"
FT   STRAND          706..709
FT                   /evidence="ECO:0007829|PDB:2WCY"
FT   STRAND          712..715
FT                   /evidence="ECO:0007829|PDB:2WCY"
FT   HELIX           718..720
FT                   /evidence="ECO:0007829|PDB:2WCY"
FT   STRAND          726..731
FT                   /evidence="ECO:0007829|PDB:2WCY"
FT   TURN            732..734
FT                   /evidence="ECO:0007829|PDB:2WCY"
FT   STRAND          737..741
FT                   /evidence="ECO:0007829|PDB:2WCY"
FT   HELIX           742..750
FT                   /evidence="ECO:0007829|PDB:2WCY"
FT   STRAND          755..757
FT                   /evidence="ECO:0007829|PDB:2WCY"
FT   STRAND          766..769
FT                   /evidence="ECO:0007829|PDB:2WCY"
FT   STRAND          778..782
FT                   /evidence="ECO:0007829|PDB:2WCY"
FT   STRAND          784..791
FT                   /evidence="ECO:0007829|PDB:2WCY"
FT   HELIX           794..796
FT                   /evidence="ECO:0007829|PDB:2WCY"
FT   STRAND          803..808
FT                   /evidence="ECO:0007829|PDB:2WCY"
FT   STRAND          811..816
FT                   /evidence="ECO:0007829|PDB:2WCY"
FT   HELIX           817..826
FT                   /evidence="ECO:0007829|PDB:2WCY"
FT   STRAND          831..836
FT                   /evidence="ECO:0007829|PDB:2WCY"
SQ   SEQUENCE   843 AA;  93518 MW;  DBD5D7C92DF71FA5 CRC64;
     MKVISLFILV GFIGEFQSFS SASSPVNCQW DFYAPWSECN GCTKTQTRRR SVAVYGQYGG
     QPCVGNAFET QSCEPTRGCP TEEGCGERFR CFSGQCISKS LVCNGDSDCD EDSADEDRCE
     DSERRPSCDI DKPPPNIELT GNGYNELTGQ FRNRVINTKS FGGQCRKVFS GDGKDFYRLS
     GNVLSYTFQV KINNDFNYEF YNSTWSYVKH TSTEHTSSSR KRSFFRSSSS SSRSYTSHTN
     EIHKGKSYQL LVVENTVEVA QFINNNPEFL QLAEPFWKEL SHLPSLYDYS AYRRLIDQYG
     THYLQSGSLG GEYRVLFYVD SEKLKQNDFN SVEEKKCKSS GWHFVVKFSS HGCKELENAL
     KAASGTQNNV LRGEPFIRGG GAGFISGLSY LELDNPAGNK RRYSAWAESV TNLPQVIKQK
     LTPLYELVKE VPCASVKKLY LKWALEEYLD EFDPCHCRPC QNGGLATVEG THCLCHCKPY
     TFGAACEQGV LVGNQAGGVD GGWSCWSSWS PCVQGKKTRS RECNNPPPSG GGRSCVGETT
     ESTQCEDEEL EHLRLLEPHC FPLSLVPTEF CPSPPALKDG FVQDEGTMFP VGKNVVYTCN
     EGYSLIGNPV ARCGEDLRWL VGEMHCQKIA CVLPVLMDGI QSHPQKPFYT VGEKVTVSCS
     GGMSLEGPSA FLCGSSLKWS PEMKNARCVQ KENPLTQAVP KCQRWEKLQN SRCVCKMPYE
     CGPSLDVCAQ DERSKRILPL TVCKMHVLHC QGRNYTLTGR DSCTLPASAE KACGACPLWG
     KCDAESSKCV CREASECEEE GFSICVEVNG KEQTMSECEA GALRCRGQSI SVTSIRPCAA
     ETQ
//
DBGET integrated database retrieval system