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   05-JUN-2019, entry version 196.
DE   RecName: Full=Complement component C7;
DE   Flags: Precursor;
GN   Name=C7;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT
RP   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
RT   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT   project: 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
RT   and C9 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-
RT   mannosylated 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.,
RA   Moore R.J., 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.,
RA   Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA   Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT   "A strategy for precise and large scale identification of core
RT   fucosylated glycoproteins.";
RL   Mol. Cell. Proteomics 8:913-923(2009).
RN   [9]
RP   GLYCOSYLATION AT THR-696, STRUCTURE OF CARBOHYDRATES, AND
RP   IDENTIFICATION BY 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
RT   N-and 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.,
RA   Bramham J.;
RT   "Solution structure of factor I-like modules from complement C7
RT   reveals a pair of follistatin domains in compact pseudosymmetric
RT   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.,
RA   Platonov A.E., Vershinina I.V., Shipulin G.A., Lachmann P.J.,
RA   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.,
RA   Lin X., 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
CC       plays a key role in the innate and adaptive immune response by
CC       forming pores in the plasma membrane of target cells. C7 serves as
CC       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
CC       cleavage of C5 into C5a and C5b. C5b binds sequentially C6, C7, C8
CC       and multiple 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
CC       possibly 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
CC       rare 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
CC       associated with variations affecting the gene represented in this
CC       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/";
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   SMR; P10643; -.
DR   BioGrid; 107191; 4.
DR   IntAct; P10643; 3.
DR   MINT; P10643; -.
DR   STRING; 9606.ENSP00000322061; -.
DR   GlyConnect; 807; -.
DR   iPTMnet; P10643; -.
DR   PhosphoSitePlus; P10643; -.
DR   UniCarbKB; P10643; -.
DR   BioMuta; C7; -.
DR   DMDM; 61252057; -.
DR   jPOST; P10643; -.
DR   PaxDb; P10643; -.
DR   PeptideAtlas; P10643; -.
DR   PRIDE; P10643; -.
DR   ProteomicsDB; 52633; -.
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; HPA001465; -.
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   eggNOG; ENOG410IDXP; Eukaryota.
DR   eggNOG; ENOG410YJ70; LUCA.
DR   GeneTree; ENSGT00940000156804; -.
DR   HOGENOM; HOG000111868; -.
DR   InParanoid; P10643; -.
DR   KO; K03996; -.
DR   OMA; YNSSWSY; -.
DR   OrthoDB; 100680at2759; -.
DR   PhylomeDB; P10643; -.
DR   TreeFam; TF330498; -.
DR   Reactome; R-HSA-166665; Terminal pathway of complement.
DR   Reactome; R-HSA-977606; Regulation of Complement cascade.
DR   ChiTaRS; C7; human.
DR   EvolutionaryTrace; P10643; -.
DR   GenomeRNAi; 730; -.
DR   PRO; PR:P10643; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   Bgee; ENSG00000112936; Expressed in 195 organ(s), highest expression level in adrenal cortex.
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   GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
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;
KW   Complete proteome; Cytolysis; Direct protein sequencing;
KW   Disease mutation; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Immunity; Innate immunity; Membrane attack complex; Polymorphism;
KW   Reference proteome; Repeat; Secreted; Signal; Sushi.
FT   SIGNAL        1     22
FT   CHAIN        23    843       Complement component C7.
FT                                /FTId=PRO_0000023583.
FT   DOMAIN       27     80       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN       83    121       LDL-receptor class A.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      124    456       MACPF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00745}.
FT   DOMAIN      457    487       EGF-like.
FT   DOMAIN      500    549       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      569    628       Sushi 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      629    690       Sushi 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   REGION      545    615       CCP 1.
FT   REGION      616    693       CCP 2.
FT   REGION      695    770       Factor I module (FIM) 1.
FT   REGION      771    843       Factor I module (FIM) 2.
FT   CARBOHYD     36     36       C-linked (Man) tryptophan.
FT                                {ECO:0000269|PubMed:10551839}.
FT   CARBOHYD    202    202       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:14760718,
FT                                ECO:0000269|PubMed:16335952}.
FT   CARBOHYD    503    503       C-linked (Man) tryptophan; partial.
FT                                {ECO:0000269|PubMed:10551839}.
FT   CARBOHYD    506    506       C-linked (Man) tryptophan; partial.
FT                                {ECO:0000269|PubMed:10551839}.
FT   CARBOHYD    509    509       C-linked (Man) tryptophan; partial.
FT                                {ECO:0000269|PubMed:10551839}.
FT   CARBOHYD    696    696       O-linked (GalNAc...) threonine.
FT                                {ECO:0000269|PubMed:22171320}.
FT   CARBOHYD    754    754       N-linked (GlcNAc...) (complex)
FT                                asparagine. {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:19139490}.
FT   DISULFID     85     96       {ECO:0000250}.
FT   DISULFID     91    109       {ECO:0000250}.
FT   DISULFID    103    119       {ECO:0000250}.
FT   DISULFID    128    165       {ECO:0000250}.
FT   DISULFID    337    353       {ECO:0000269|PubMed:19419965}.
FT   DISULFID    571    613       {ECO:0000250}.
FT   DISULFID    599    626       {ECO:0000250}.
FT   DISULFID    631    673       {ECO:0000250}.
FT   DISULFID    659    688       {ECO:0000250}.
FT   DISULFID    702    713       {ECO:0000269|PubMed:19419965}.
FT   DISULFID    715    750       {ECO:0000269|PubMed:19419965}.
FT   DISULFID    721    743       {ECO:0000269|PubMed:19419965}.
FT   DISULFID    728    763       {ECO:0000269|PubMed:19419965}.
FT   DISULFID    773    782       {ECO:0000269|PubMed:19419965}.
FT   DISULFID    776    789       {ECO:0000269|PubMed:19419965}.
FT   DISULFID    791    825       {ECO:0000269|PubMed:19419965}.
FT   DISULFID    797    818       {ECO:0000269|PubMed:19419965}.
FT   DISULFID    805    838       {ECO:0000269|PubMed:19419965}.
FT   VARIANT     128    128       C -> R (in dbSNP:rs2271708).
FT                                /FTId=VAR_050480.
FT   VARIANT     220    220       R -> Q (in C7D; dbSNP:rs369349760).
FT                                {ECO:0000269|PubMed:9856499}.
FT                                /FTId=VAR_012643.
FT   VARIANT     222    222       R -> H (in dbSNP:rs75345202).
FT                                {ECO:0000269|PubMed:14702039}.
FT                                /FTId=VAR_081726.
FT   VARIANT     379    379       G -> R (in C7D; dbSNP:rs121964921).
FT                                {ECO:0000269|PubMed:9218625}.
FT                                /FTId=VAR_012644.
FT   VARIANT     389    389       S -> T (polymorphism; confirmed at
FT                                protein level; dbSNP:rs1063499).
FT                                {ECO:0000269|PubMed:22028381,
FT                                ECO:0000269|PubMed:7730625}.
FT                                /FTId=VAR_033798.
FT   VARIANT     420    420       K -> Q (in dbSNP:rs3792646).
FT                                /FTId=VAR_022023.
FT   VARIANT     521    521       R -> S (in C7D; dbSNP:rs121964920).
FT                                {ECO:0000269|PubMed:8871666}.
FT                                /FTId=VAR_012645.
FT   VARIANT     587    587       T -> P (polymorphism; confirmed at
FT                                protein level; dbSNP:rs13157656).
FT                                {ECO:0000269|PubMed:22028381,
FT                                ECO:0000269|PubMed:3335508}.
FT                                /FTId=VAR_033799.
FT   VARIANT     682    682       E -> Q (in C7D; dbSNP:rs541873000).
FT                                {ECO:0000269|PubMed:9856499}.
FT                                /FTId=VAR_012646.
FT   VARIANT     687    687       R -> H (in C7D; dbSNP:rs113187203).
FT                                {ECO:0000269|PubMed:9856499}.
FT                                /FTId=VAR_012647.
FT   CONFLICT     18     18       S -> G (in Ref. 2; BAF83038).
FT                                {ECO:0000305}.
FT   CONFLICT    123    123       E -> G (in Ref. 2; BAF83038).
FT                                {ECO:0000305}.
FT   CONFLICT    152    152       R -> V (in Ref. 4; CAA60121).
FT                                {ECO:0000305}.
FT   CONFLICT    212    212       S -> P (in Ref. 2; BAF83038).
FT                                {ECO:0000305}.
FT   CONFLICT    821    822       GA -> AL (in Ref. 4; CAA60121).
FT                                {ECO:0000305}.
FT   STRAND      706    709       {ECO:0000244|PDB:2WCY}.
FT   STRAND      712    715       {ECO:0000244|PDB:2WCY}.
FT   HELIX       718    720       {ECO:0000244|PDB:2WCY}.
FT   STRAND      726    731       {ECO:0000244|PDB:2WCY}.
FT   TURN        732    734       {ECO:0000244|PDB:2WCY}.
FT   STRAND      737    741       {ECO:0000244|PDB:2WCY}.
FT   HELIX       742    750       {ECO:0000244|PDB:2WCY}.
FT   STRAND      755    757       {ECO:0000244|PDB:2WCY}.
FT   STRAND      766    769       {ECO:0000244|PDB:2WCY}.
FT   STRAND      778    782       {ECO:0000244|PDB:2WCY}.
FT   STRAND      784    791       {ECO:0000244|PDB:2WCY}.
FT   HELIX       794    796       {ECO:0000244|PDB:2WCY}.
FT   STRAND      803    808       {ECO:0000244|PDB:2WCY}.
FT   STRAND      811    816       {ECO:0000244|PDB:2WCY}.
FT   HELIX       817    826       {ECO:0000244|PDB:2WCY}.
FT   STRAND      831    836       {ECO:0000244|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
//
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