CO7_HUMAN
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 03-AUG-2022, entry version 214.
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; DOI=10.1016/s0021-9258(19)57427-0;
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/";
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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 PDB; 7NYC; EM; 3.50 A; C=23-843.
DR PDB; 7NYD; EM; 3.30 A; C=23-843.
DR PDBsum; 2WCY; -.
DR PDBsum; 6H03; -.
DR PDBsum; 6H04; -.
DR PDBsum; 7NYC; -.
DR PDBsum; 7NYD; -.
DR AlphaFoldDB; P10643; -.
DR BMRB; P10643; -.
DR SMR; P10643; -.
DR BioGRID; 107191; 6.
DR ComplexPortal; CPX-6159; Membrane attack complex.
DR IntAct; P10643; 4.
DR MINT; P10643; -.
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; 323 antibodies from 36 providers.
DR DNASU; 730; -.
DR Ensembl; ENST00000313164.10; ENSP00000322061.9; ENSG00000112936.19.
DR GeneID; 730; -.
DR KEGG; hsa:730; -.
DR MANE-Select; ENST00000313164.10; ENSP00000322061.9; NM_000587.4; NP_000578.2.
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 SignaLink; P10643; -.
DR SIGNOR; P10643; -.
DR BioGRID-ORCS; 730; 8 hits in 1071 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 right ovary and 167 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:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005579; C:membrane attack complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0006956; P:complement activation; IBA:GO_Central.
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 GO; GO:0050778; P:positive regulation of immune response; IC:ComplexPortal.
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 TURN 41..44
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:7NYD"
FT TURN 99..103
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:7NYD"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:7NYD"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:7NYD"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:7NYD"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:7NYC"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:7NYC"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 191..221
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 227..263
FT /evidence="ECO:0007829|PDB:7NYD"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:7NYD"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:7NYD"
FT HELIX 289..299
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 301..339
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 352..373
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:7NYD"
FT HELIX 382..388
FT /evidence="ECO:0007829|PDB:7NYD"
FT HELIX 400..409
FT /evidence="ECO:0007829|PDB:7NYD"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 415..423
FT /evidence="ECO:0007829|PDB:7NYD"
FT HELIX 424..427
FT /evidence="ECO:0007829|PDB:7NYD"
FT HELIX 434..452
FT /evidence="ECO:0007829|PDB:7NYD"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 470..476
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:7NYD"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 516..520
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 539..544
FT /evidence="ECO:0007829|PDB:7NYD"
FT HELIX 547..556
FT /evidence="ECO:0007829|PDB:7NYD"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 580..584
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 594..599
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 603..607
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 610..613
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 617..620
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 625..631
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 641..644
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 654..658
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 669..673
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 675..677
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 706..709
FT /evidence="ECO:0007829|PDB:2WCY"
FT STRAND 712..715
FT /evidence="ECO:0007829|PDB:2WCY"
FT TURN 718..723
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 726..730
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 732..735
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 737..741
FT /evidence="ECO:0007829|PDB:7NYD"
FT HELIX 742..750
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 755..757
FT /evidence="ECO:0007829|PDB:2WCY"
FT STRAND 766..769
FT /evidence="ECO:0007829|PDB:2WCY"
FT STRAND 780..782
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 787..791
FT /evidence="ECO:0007829|PDB:7NYD"
FT HELIX 794..796
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 803..808
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 811..816
FT /evidence="ECO:0007829|PDB:7NYD"
FT HELIX 817..825
FT /evidence="ECO:0007829|PDB:7NYD"
FT STRAND 830..836
FT /evidence="ECO:0007829|PDB:7NYD"
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
