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Database: UniProt
Entry: P09871
LinkDB: P09871
Original site: P09871 
ID   C1S_HUMAN               Reviewed;         688 AA.
AC   P09871; D3DUT4; Q9UCU7; Q9UCU8; Q9UCU9; Q9UCV0; Q9UCV1; Q9UCV2;
AC   Q9UCV3; Q9UCV4; Q9UCV5; Q9UM14;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   26-NOV-2014, entry version 190.
DE   RecName: Full=Complement C1s subcomponent;
DE            EC=3.4.21.42;
DE   AltName: Full=C1 esterase;
DE   AltName: Full=Complement component 1 subcomponent s;
DE   Contains:
DE     RecName: Full=Complement C1s subcomponent heavy chain;
DE   Contains:
DE     RecName: Full=Complement C1s subcomponent light chain;
DE   Flags: Precursor;
GN   Name=C1S;
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].
RC   TISSUE=Liver;
RX   PubMed=3500856; DOI=10.1111/j.1432-1033.1987.tb13644.x;
RA   McKinnon C.M., Carter P.E., Smyth S.J., Dunbar B., Fothergill J.E.;
RT   "Molecular cloning of cDNA for human complement component C1s. The
RT   complete amino acid sequence.";
RL   Eur. J. Biochem. 169:547-553(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2831944; DOI=10.1021/bi00400a004;
RA   Tosi M., Duponchel C., Meo T., Julier C.;
RT   "Complete cDNA sequence of human complement Cls and close physical
RT   linkage of the homologous genes Cls and Clr.";
RL   Biochemistry 26:8516-8524(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2459702; DOI=10.1073/pnas.85.19.7307;
RA   Kusumoto H., Hirosawa S., Salier J.-P., Hagen F.S., Kurachi K.;
RT   "Human genes for complement components C1r and C1s in a close tail-to-
RT   tail arrangement.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:7307-7311(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-329.
RC   TISSUE=Peripheral blood leukocyte;
RX   PubMed=9794427;
RA   Endo Y., Takahashi M., Nakao M., Saiga H., Sekine H., Matsushita M.,
RA   Nonaka M., Fujita T.;
RT   "Two lineages of mannose-binding lectin-associated serine protease
RT   (MASP) in vertebrates.";
RL   J. Immunol. 161:4924-4930(1998).
RN   [7]
RP   NUCLEOTIDE SEQUENCE OF 291-688.
RX   PubMed=2553984; DOI=10.1016/0022-2836(89)90161-7;
RA   Tosi M., Duponchel C., Meo T., Couture-Tosi E.;
RT   "Complement genes C1r and C1s feature an intronless serine protease
RT   domain closely related to haptoglobin.";
RL   J. Mol. Biol. 208:709-714(1989).
RN   [8]
RP   PROTEIN SEQUENCE OF 16-61; 168-219; 287-334 AND 384-445.
RX   PubMed=3007145; DOI=10.1111/j.1432-1033.1986.tb09546.x;
RA   Spycher S.E., Nick H., Rickli E.E.;
RT   "Human complement component C1s. Partial sequence determination of the
RT   heavy chain and identification of the peptide bond cleaved during
RT   activation.";
RL   Eur. J. Biochem. 156:49-57(1986).
RN   [9]
RP   PROTEIN SEQUENCE OF 438-500; 503-534; 542-601; 617-623 AND 626-656.
RX   PubMed=6362661;
RA   Carter P.E., Dunbar B., Fothergill J.E.;
RT   "The serine proteinase chain of human complement component C1s.
RT   Cyanogen bromide cleavage and N-terminal sequences of the fragments.";
RL   Biochem. J. 215:565-571(1983).
RN   [10]
RP   PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-174, AND HYDROXYLATION
RP   AT ASN-149.
RX   PubMed=2141278; DOI=10.1021/bi00466a021;
RA   Thielens N.M., van Dorsselaer A., Gagnon J., Arlaud G.J.;
RT   "Chemical and functional characterization of a fragment of C1-s
RT   containing the epidermal growth factor homology region.";
RL   Biochemistry 29:3570-3578(1990).
RN   [11]
RP   PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Plasma;
RX   PubMed=1854725; DOI=10.1021/bi00243a014;
RA   Illy C., Thielens N.M., Gagnon J., Arlaud G.J.;
RT   "Effect of lactoperoxidase-catalyzed iodination on the Ca(2+)-
RT   dependent interactions of human C1s. Location of the iodination
RT   sites.";
RL   Biochemistry 30:7135-7141(1991).
RN   [12]
RP   DISULFIDE BONDS.
RX   PubMed=2007122; DOI=10.1021/bi00225a014;
RA   Hess D., Schaller J., Rickli E.E.;
RT   "Identification of the disulfide bonds of human complement C1s.";
RL   Biochemistry 30:2827-2833(1991).
RN   [13]
RP   PARTIAL PROTEIN SEQUENCE, AND 3D-STRUCTURE MODELING OF CATALYTIC
RP   DOMAIN.
RX   PubMed=7779774; DOI=10.1021/bi00022a004;
RA   Rossi V., Gaboriaud C., Lacroix M., Ulrich J., Fontecilla-Camps J.-C.,
RA   Gagnon J., Arlaud G.J.;
RT   "Structure of the catalytic region of human complement protease C1s:
RT   study by chemical cross-linking and three-dimensional homology
RT   modeling.";
RL   Biochemistry 34:7311-7321(1995).
RN   [14]
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME
RP   REGULATION.
RX   PubMed=11527969; DOI=10.1074/jbc.M105934200;
RA   Rossi V., Cseh S., Bally I., Thielens N.M., Jensenius J.C.,
RA   Arlaud G.J.;
RT   "Substrate specificities of recombinant mannan-binding lectin-
RT   associated serine proteases-1 and -2.";
RL   J. Biol. Chem. 276:40880-40887(2001).
RN   [15]
RP   INVOLVEMENT IN COMPLEMENT COMPONENT C1S DEFICIENCY.
RX   PubMed=11390518; DOI=10.4049/jimmunol.166.12.7612;
RA   Dragon-Durey M.-A., Quartier P., Fremeaux-Bacchi V., Blouin J.,
RA   de Barace C., Prieur A.-M., Weiss L., Fridman W.-H.;
RT   "Molecular basis of a selective C1s deficiency associated with early
RT   onset multiple autoimmune diseases.";
RL   J. Immunol. 166:7612-7616(2001).
RN   [16]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406.
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   [17]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-174 AND ASN-406.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of
RT   multiple enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 358-688.
RX   PubMed=10775260; DOI=10.1093/emboj/19.8.1755;
RA   Gaboriaud C., Rossi V., Bally I., Arlaud G.J., Fontecilla-Camps J.-C.;
RT   "Crystal structure of the catalytic domain of human complement c1s: a
RT   serine protease with a handle.";
RL   EMBO J. 19:1755-1765(2000).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 16-174, CALCIUM-BINDING
RP   SITES, AND GLYCOSYLATION AT ASN-406.
RX   PubMed=12788922; DOI=10.1074/jbc.M305175200;
RA   Gregory L.A., Thielens N.M., Arlaud G.J., Fontecilla-Camps J.-C.,
RA   Gaboriaud C.;
RT   "X-ray structure of the Ca2+-binding interaction domain of C1s.
RT   Insights into the assembly of the C1 complex of complement.";
RL   J. Biol. Chem. 278:32157-32164(2003).
CC   -!- FUNCTION: C1s B chain is a serine protease that combines with C1q
CC       and C1r to form C1, the first component of the classical pathway
CC       of the complement system. C1r activates C1s so that it can, in
CC       turn, activate C2 and C4.
CC   -!- CATALYTIC ACTIVITY: Cleavage of Arg-|-Ala bond in complement
CC       component C4 to form C4a and C4b, and Lys(or Arg)-|-Lys bond in
CC       complement component C2 to form C2a and C2b: the 'classical'
CC       pathway C3 convertase. {ECO:0000269|PubMed:11527969}.
CC   -!- ENZYME REGULATION: Inhibited by SERPING1.
CC       {ECO:0000269|PubMed:11527969}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=12.3 uM for complement component C2 (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:11527969};
CC         KM=1.9 uM for complement component C4 (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:11527969};
CC         Note=Less efficient than MASP2 in C4 cleavage.;
CC   -!- SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q,
CC       C1r and C1s in the molar ration of 1:2:2. Activated C1s is an
CC       disulfide-linked heterodimer of a heavy chain and a light chain.
CC       {ECO:0000269|PubMed:2007122}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-2810045, EBI-2810045;
CC       P00736:C1R; NbExp=3; IntAct=EBI-2810045, EBI-3926504;
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000269|PubMed:2141278}.
CC   -!- DISEASE: Complement component C1s deficiency (C1SD) [MIM:613783]:
CC       A rare defect resulting in C1 deficiency and impaired activation
CC       of the complement classical pathway. C1 deficiency generally leads
CC       to severe immune complex disease with features of systemic lupus
CC       erythematosus and glomerulonephritis.
CC       {ECO:0000269|PubMed:11390518}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- SIMILARITY: Contains 2 CUB domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00059}.
CC   -!- SIMILARITY: Contains 1 EGF-like domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   -!- SIMILARITY: Contains 2 Sushi (CCP/SCR) domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00302}.
CC   -!- WEB RESOURCE: Name=C1Sbase; Note=C1S mutation db;
CC       URL="http://bioinf.uta.fi/C1Sbase/";
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DR   EMBL; X06596; CAA29817.1; -; mRNA.
DR   EMBL; M18767; AAA51853.1; -; mRNA.
DR   EMBL; J04080; AAA51852.1; -; mRNA.
DR   EMBL; CH471116; EAW88689.1; -; Genomic_DNA.
DR   EMBL; CH471116; EAW88690.1; -; Genomic_DNA.
DR   EMBL; BC056903; AAH56903.1; -; mRNA.
DR   EMBL; AB009076; BAA86864.1; -; Genomic_DNA.
DR   CCDS; CCDS31735.1; -.
DR   PIR; A40496; C1HUS.
DR   RefSeq; NP_001725.1; NM_001734.3.
DR   RefSeq; NP_958850.1; NM_201442.2.
DR   RefSeq; XP_005253817.1; XM_005253760.1.
DR   UniGene; Hs.458355; -.
DR   PDB; 1ELV; X-ray; 1.70 A; A=356-688.
DR   PDB; 1NZI; X-ray; 1.50 A; A/B=16-174.
DR   PDB; 4J1Y; X-ray; 2.66 A; A/B=292-688.
DR   PDB; 4LMF; X-ray; 2.92 A; A/B/C/D=17-292.
DR   PDB; 4LOR; X-ray; 2.50 A; A=17-292.
DR   PDB; 4LOS; X-ray; 2.00 A; A=172-358.
DR   PDB; 4LOT; X-ray; 2.92 A; A=175-423.
DR   PDBsum; 1ELV; -.
DR   PDBsum; 1NZI; -.
DR   PDBsum; 4J1Y; -.
DR   PDBsum; 4LMF; -.
DR   PDBsum; 4LOR; -.
DR   PDBsum; 4LOS; -.
DR   PDBsum; 4LOT; -.
DR   ProteinModelPortal; P09871; -.
DR   SMR; P09871; 17-684.
DR   BioGrid; 107177; 7.
DR   IntAct; P09871; 8.
DR   MINT; MINT-4655918; -.
DR   BindingDB; P09871; -.
DR   ChEMBL; CHEMBL3913; -.
DR   DrugBank; DB00054; Abciximab.
DR   DrugBank; DB00051; Adalimumab.
DR   DrugBank; DB00074; Basiliximab.
DR   DrugBank; DB00002; Cetuximab.
DR   DrugBank; DB00005; Etanercept.
DR   DrugBank; DB00056; Gemtuzumab ozogamicin.
DR   DrugBank; DB00078; Ibritumomab.
DR   DrugBank; DB00075; Muromonab.
DR   DrugBank; DB00073; Rituximab.
DR   DrugBank; DB00072; Trastuzumab.
DR   MEROPS; S01.193; -.
DR   PhosphoSite; P09871; -.
DR   DMDM; 115205; -.
DR   SWISS-2DPAGE; P09871; -.
DR   MaxQB; P09871; -.
DR   PaxDb; P09871; -.
DR   PeptideAtlas; P09871; -.
DR   PRIDE; P09871; -.
DR   Ensembl; ENST00000328916; ENSP00000328173; ENSG00000182326.
DR   Ensembl; ENST00000360817; ENSP00000354057; ENSG00000182326.
DR   Ensembl; ENST00000406697; ENSP00000385035; ENSG00000182326.
DR   GeneID; 716; -.
DR   KEGG; hsa:716; -.
DR   UCSC; uc001qsj.3; human.
DR   CTD; 716; -.
DR   GeneCards; GC12P007096; -.
DR   HGNC; HGNC:1247; C1S.
DR   HPA; CAB016722; -.
DR   HPA; HPA018852; -.
DR   MIM; 120580; gene.
DR   MIM; 613783; phenotype.
DR   neXtProt; NX_P09871; -.
DR   Orphanet; 169147; Immunodeficiency due to an early component of complement deficiency.
DR   PharmGKB; PA25636; -.
DR   eggNOG; COG5640; -.
DR   GeneTree; ENSGT00760000118890; -.
DR   HOVERGEN; HBG000559; -.
DR   InParanoid; P09871; -.
DR   KO; K01331; -.
DR   OMA; PTMYGEI; -.
DR   PhylomeDB; P09871; -.
DR   TreeFam; TF330373; -.
DR   Reactome; REACT_7956; Classical antibody-mediated complement activation.
DR   Reactome; REACT_8024; Initial triggering of complement.
DR   SABIO-RK; P09871; -.
DR   ChiTaRS; C1S; human.
DR   EvolutionaryTrace; P09871; -.
DR   GeneWiki; C1S; -.
DR   GenomeRNAi; 716; -.
DR   NextBio; 2912; -.
DR   PMAP-CutDB; P09871; -.
DR   PRO; PR:P09871; -.
DR   Bgee; P09871; -.
DR   ExpressionAtlas; P09871; baseline and differential.
DR   Genevestigator; P09871; -.
DR   GO; GO:0072562; C:blood microparticle; IDA:UniProt.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0006956; P:complement activation; TAS:Reactome.
DR   GO; GO:0006958; P:complement activation, classical pathway; TAS:Reactome.
DR   GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR   Gene3D; 2.60.120.290; -; 2.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024175; Pept_S1A_C1r/C1S/mannan-bd.
DR   InterPro; IPR001254; Peptidase_S1.
DR   InterPro; IPR018114; Peptidase_S1_AS.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR000436; Sushi_SCR_CCP.
DR   InterPro; IPR009003; Trypsin-like_Pept_dom.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF00084; Sushi; 2.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001155; C1r_C1s_MASP; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00032; CCP; 2.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF49854; SSF49854; 2.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57535; SSF57535; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50923; SUSHI; 2.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Complement pathway; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Hydrolase; Hydroxylation; Immunity; Innate immunity;
KW   Metal-binding; Polymorphism; Protease; Reference proteome; Repeat;
KW   Serine protease; Signal; Sushi.
FT   SIGNAL        1     15       {ECO:0000269|PubMed:3007145}.
FT   CHAIN        16    688       Complement C1s subcomponent.
FT                                /FTId=PRO_0000027586.
FT   CHAIN        16    437       Complement C1s subcomponent heavy chain.
FT                                /FTId=PRO_0000027587.
FT   CHAIN       438    688       Complement C1s subcomponent light chain.
FT                                /FTId=PRO_0000027588.
FT   DOMAIN       16    130       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      131    172       EGF-like; calcium-binding.
FT   DOMAIN      175    290       CUB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      292    356       Sushi 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      357    423       Sushi 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      438    680       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    475    475       Charge relay system.
FT   ACT_SITE    529    529       Charge relay system.
FT   ACT_SITE    632    632       Charge relay system.
FT   METAL        60     60       Calcium.
FT   METAL        68     68       Calcium.
FT   METAL       113    113       Calcium.
FT   METAL       131    131       Calcium.
FT   METAL       132    132       Calcium; via carbonyl oxygen.
FT   METAL       134    134       Calcium.
FT   METAL       149    149       Calcium.
FT   METAL       150    150       Calcium; via carbonyl oxygen.
FT   METAL       153    153       Calcium; via carbonyl oxygen.
FT   MOD_RES     149    149       (3R)-3-hydroxyasparagine.
FT                                {ECO:0000269|PubMed:2141278}.
FT   CARBOHYD    174    174       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:19159218,
FT                                ECO:0000269|PubMed:2141278}.
FT   CARBOHYD    406    406       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:12788922,
FT                                ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:19159218}.
FT   DISULFID     65     83       {ECO:0000269|PubMed:2007122}.
FT   DISULFID    135    147       {ECO:0000269|PubMed:2007122}.
FT   DISULFID    143    156       {ECO:0000269|PubMed:2007122}.
FT   DISULFID    158    171       {ECO:0000269|PubMed:2007122}.
FT   DISULFID    175    202       {ECO:0000269|PubMed:2007122}.
FT   DISULFID    234    251       {ECO:0000269|PubMed:2007122}.
FT   DISULFID    294    341       {ECO:0000269|PubMed:2007122}.
FT   DISULFID    321    354       {ECO:0000269|PubMed:2007122}.
FT   DISULFID    359    403       {ECO:0000269|PubMed:2007122}.
FT   DISULFID    386    421       {ECO:0000269|PubMed:2007122}.
FT   DISULFID    425    549       Interchain (between heavy and light
FT                                chains). {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059, ECO:0000255|PROSITE-
FT                                ProRule:PRU00274, ECO:0000255|PROSITE-
FT                                ProRule:PRU00302,
FT                                ECO:0000269|PubMed:2007122}.
FT   DISULFID    595    618       {ECO:0000269|PubMed:2007122}.
FT   DISULFID    628    659       {ECO:0000269|PubMed:2007122}.
FT   VARIANT     119    119       R -> H (in dbSNP:rs12146727).
FT                                /FTId=VAR_033643.
FT   VARIANT     327    327       V -> L (in dbSNP:rs2239170).
FT                                /FTId=VAR_033644.
FT   VARIANT     383    383       R -> H (in dbSNP:rs20573).
FT                                /FTId=VAR_014565.
FT   CONFLICT    294    294       C -> K (in Ref. 8; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    513    513       G -> GG (in Ref. 7). {ECO:0000305}.
FT   CONFLICT    573    573       T -> A (in Ref. 9; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    645    646       TK -> GR (in Ref. 9; AA sequence).
FT                                {ECO:0000305}.
FT   STRAND       19     24       {ECO:0000244|PDB:1NZI}.
FT   TURN         26     29       {ECO:0000244|PDB:1NZI}.
FT   STRAND       34     43       {ECO:0000244|PDB:1NZI}.
FT   STRAND       48     58       {ECO:0000244|PDB:1NZI}.
FT   HELIX        63     65       {ECO:0000244|PDB:1NZI}.
FT   STRAND       67     73       {ECO:0000244|PDB:1NZI}.
FT   STRAND       80     82       {ECO:0000244|PDB:1NZI}.
FT   STRAND       84     86       {ECO:0000244|PDB:1NZI}.
FT   STRAND       96    112       {ECO:0000244|PDB:1NZI}.
FT   STRAND      122    131       {ECO:0000244|PDB:1NZI}.
FT   TURN        134    136       {ECO:0000244|PDB:1NZI}.
FT   STRAND      137    140       {ECO:0000244|PDB:4LOR}.
FT   STRAND      143    150       {ECO:0000244|PDB:1NZI}.
FT   STRAND      153    157       {ECO:0000244|PDB:1NZI}.
FT   STRAND      162    164       {ECO:0000244|PDB:4LOR}.
FT   STRAND      171    173       {ECO:0000244|PDB:4LOR}.
FT   STRAND      176    180       {ECO:0000244|PDB:4LOS}.
FT   STRAND      182    188       {ECO:0000244|PDB:4LOS}.
FT   TURN        190    193       {ECO:0000244|PDB:4LOS}.
FT   STRAND      201    207       {ECO:0000244|PDB:4LOS}.
FT   STRAND      212    217       {ECO:0000244|PDB:4LOS}.
FT   HELIX       220    222       {ECO:0000244|PDB:4LOS}.
FT   STRAND      223    225       {ECO:0000244|PDB:4LOS}.
FT   STRAND      235    242       {ECO:0000244|PDB:4LOS}.
FT   STRAND      245    250       {ECO:0000244|PDB:4LOS}.
FT   STRAND      252    254       {ECO:0000244|PDB:4LOS}.
FT   STRAND      259    262       {ECO:0000244|PDB:4LOS}.
FT   STRAND      265    273       {ECO:0000244|PDB:4LOS}.
FT   STRAND      282    291       {ECO:0000244|PDB:4LOS}.
FT   STRAND      300    306       {ECO:0000244|PDB:4LOS}.
FT   STRAND      309    312       {ECO:0000244|PDB:4J1Y}.
FT   STRAND      316    321       {ECO:0000244|PDB:4LOS}.
FT   STRAND      325    331       {ECO:0000244|PDB:4LOS}.
FT   STRAND      334    341       {ECO:0000244|PDB:4LOS}.
FT   TURN        348    351       {ECO:0000244|PDB:4LOS}.
FT   STRAND      353    356       {ECO:0000244|PDB:4LOS}.
FT   STRAND      368    370       {ECO:0000244|PDB:1ELV}.
FT   STRAND      381    386       {ECO:0000244|PDB:1ELV}.
FT   TURN        388    390       {ECO:0000244|PDB:1ELV}.
FT   STRAND      391    393       {ECO:0000244|PDB:1ELV}.
FT   STRAND      395    397       {ECO:0000244|PDB:4LOT}.
FT   STRAND      399    403       {ECO:0000244|PDB:1ELV}.
FT   TURN        405    407       {ECO:0000244|PDB:4LOT}.
FT   STRAND      409    411       {ECO:0000244|PDB:1ELV}.
FT   TURN        412    414       {ECO:0000244|PDB:1ELV}.
FT   STRAND      421    423       {ECO:0000244|PDB:1ELV}.
FT   HELIX       446    448       {ECO:0000244|PDB:1ELV}.
FT   STRAND      452    455       {ECO:0000244|PDB:1ELV}.
FT   TURN        456    459       {ECO:0000244|PDB:1ELV}.
FT   STRAND      460    466       {ECO:0000244|PDB:1ELV}.
FT   STRAND      469    472       {ECO:0000244|PDB:1ELV}.
FT   HELIX       474    477       {ECO:0000244|PDB:1ELV}.
FT   STRAND      490    492       {ECO:0000244|PDB:4J1Y}.
FT   HELIX       494    499       {ECO:0000244|PDB:4J1Y}.
FT   STRAND      505    510       {ECO:0000244|PDB:1ELV}.
FT   HELIX       520    522       {ECO:0000244|PDB:4J1Y}.
FT   STRAND      531    537       {ECO:0000244|PDB:1ELV}.
FT   HELIX       555    557       {ECO:0000244|PDB:1ELV}.
FT   STRAND      564    570       {ECO:0000244|PDB:1ELV}.
FT   STRAND      576    578       {ECO:0000244|PDB:4J1Y}.
FT   STRAND      583    590       {ECO:0000244|PDB:1ELV}.
FT   HELIX       592    596       {ECO:0000244|PDB:1ELV}.
FT   STRAND      616    620       {ECO:0000244|PDB:1ELV}.
FT   HELIX       627    629       {ECO:0000244|PDB:4J1Y}.
FT   STRAND      635    639       {ECO:0000244|PDB:1ELV}.
FT   STRAND      647    655       {ECO:0000244|PDB:1ELV}.
FT   STRAND      661    667       {ECO:0000244|PDB:1ELV}.
FT   HELIX       668    671       {ECO:0000244|PDB:1ELV}.
FT   HELIX       672    681       {ECO:0000244|PDB:1ELV}.
SQ   SEQUENCE   688 AA;  76684 MW;  85522647A4C47205 CRC64;
     MWCIVLFSLL AWVYAEPTMY GEILSPNYPQ AYPSEVEKSW DIEVPEGYGI HLYFTHLDIE
     LSENCAYDSV QIISGDTEEG RLCGQRSSNN PHSPIVEEFQ VPYNKLQVIF KSDFSNEERF
     TGFAAYYVAT DINECTDFVD VPCSHFCNNF IGGYFCSCPP EYFLHDDMKN CGVNCSGDVF
     TALIGEIASP NYPKPYPENS RCEYQIRLEK GFQVVVTLRR EDFDVEAADS AGNCLDSLVF
     VAGDRQFGPY CGHGFPGPLN IETKSNALDI IFQTDLTGQK KGWKLRYHGD PMPCPKEDTP
     NSVWEPAKAK YVFRDVVQIT CLDGFEVVEG RVGATSFYST CQSNGKWSNS KLKCQPVDCG
     IPESIENGKV EDPESTLFGS VIRYTCEEPY YYMENGGGGE YHCAGNGSWV NEVLGPELPK
     CVPVCGVPRE PFEEKQRIIG GSDADIKNFP WQVFFDNPWA GGALINEYWV LTAAHVVEGN
     REPTMYVGST SVQTSRLAKS KMLTPEHVFI HPGWKLLEVP EGRTNFDNDI ALVRLKDPVK
     MGPTVSPICL PGTSSDYNLM DGDLGLISGW GRTEKRDRAV RLKAARLPVA PLRKCKEVKV
     EKPTADAEAY VFTPNMICAG GEKGMDSCKG DSGGAFAVQD PNDKTKFYAA GLVSWGPQCG
     TYGLYTRVKN YVDWIMKTMQ ENSTPRED
//
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