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Database: UniProt
Entry: Q8CFG8
LinkDB: Q8CFG8
Original site: Q8CFG8 
ID   CS1B_MOUSE              Reviewed;         688 AA.
AC   Q8CFG8;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   29-OCT-2014, entry version 97.
DE   RecName: Full=Complement C1s-B subcomponent;
DE            EC=3.4.21.42;
DE   AltName: Full=C1 esterase;
DE   AltName: Full=Complement component 1 subcomponent s-B;
DE   Contains:
DE     RecName: Full=Complement C1s-B subcomponent heavy chain;
DE   Contains:
DE     RecName: Full=Complement C1s-B subcomponent light chain;
DE   Flags: Precursor;
GN   Name=C1sb; Synonyms=C1s, Gm5077;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6;
RX   PubMed=12513694; DOI=10.1042/BJ20021555;
RA   Garnier G., Circolo A., Xu Y., Volanakis J.E.;
RT   "Complement C1r and C1s genes are duplicated in the mouse:
RT   differential expression generates alternative isomorphs in the liver
RT   and in the male reproductive system.";
RL   Biochem. J. 371:631-640(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 (By similarity). {ECO:0000250}.
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.
CC   -!- ENZYME REGULATION: Inhibited by SERPING1. {ECO:0000250}.
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       (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in male reproductive
CC       tissues. {ECO:0000269|PubMed:12513694}.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000250}.
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}.
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DR   EMBL; AF459020; AAO15559.1; -; mRNA.
DR   RefSeq; NP_776289.2; NM_173864.2.
DR   UniGene; Mm.483270; -.
DR   ProteinModelPortal; Q8CFG8; -.
DR   SMR; Q8CFG8; 17-683.
DR   STRING; 10090.ENSMUSP00000066999; -.
DR   MEROPS; S01.210; -.
DR   PhosphoSite; Q8CFG8; -.
DR   PaxDb; Q8CFG8; -.
DR   PRIDE; Q8CFG8; -.
DR   DNASU; 317677; -.
DR   GeneID; 317677; -.
DR   KEGG; mmu:317677; -.
DR   CTD; 317677; -.
DR   MGI; MGI:3644269; Gm5077.
DR   eggNOG; COG5640; -.
DR   HOGENOM; HOG000237311; -.
DR   HOVERGEN; HBG000559; -.
DR   InParanoid; Q8CFG8; -.
DR   KO; K01331; -.
DR   OrthoDB; EOG7W6WK4; -.
DR   PhylomeDB; Q8CFG8; -.
DR   Reactome; REACT_202834; Initial triggering of complement.
DR   Reactome; REACT_209334; Classical antibody-mediated complement activation.
DR   NextBio; 394148; -.
DR   PRO; PR:Q8CFG8; -.
DR   Bgee; Q8CFG8; -.
DR   CleanEx; MM_C1S; -.
DR   ExpressionAtlas; Q8CFG8; baseline and differential.
DR   Genevestigator; Q8CFG8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Calcium; Complement pathway; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Hydrolase; Hydroxylation; Immunity;
KW   Innate immunity; Metal-binding; Protease; Reference proteome; Repeat;
KW   Serine protease; Signal; Sushi.
FT   SIGNAL        1     15       {ECO:0000250}.
FT   CHAIN        16    688       Complement C1s-B subcomponent.
FT                                /FTId=PRO_0000042196.
FT   CHAIN        16    437       Complement C1s-B subcomponent heavy
FT                                chain. {ECO:0000250}.
FT                                /FTId=PRO_0000042197.
FT   CHAIN       438    688       Complement C1s-B subcomponent light
FT                                chain. {ECO:0000250}.
FT                                /FTId=PRO_0000042198.
FT   DOMAIN       16    130       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      131    172       EGF-like; calcium-binding. {ECO:0000255}.
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. {ECO:0000250}.
FT   ACT_SITE    529    529       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    631    631       Charge relay system. {ECO:0000250}.
FT   METAL        60     60       Calcium. {ECO:0000250}.
FT   METAL        68     68       Calcium. {ECO:0000250}.
FT   METAL       113    113       Calcium. {ECO:0000250}.
FT   METAL       131    131       Calcium. {ECO:0000250}.
FT   METAL       132    132       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       134    134       Calcium. {ECO:0000250}.
FT   METAL       149    149       Calcium. {ECO:0000250}.
FT   METAL       150    150       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       153    153       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   MOD_RES     149    149       (3R)-3-hydroxyasparagine. {ECO:0000250}.
FT   CARBOHYD    174    174       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     65     83       {ECO:0000250}.
FT   DISULFID    135    147       {ECO:0000250}.
FT   DISULFID    143    156       {ECO:0000250}.
FT   DISULFID    158    171       {ECO:0000250}.
FT   DISULFID    175    202       {ECO:0000250}.
FT   DISULFID    234    251       {ECO:0000250}.
FT   DISULFID    294    341       {ECO:0000250}.
FT   DISULFID    321    354       {ECO:0000250}.
FT   DISULFID    359    403       {ECO:0000250}.
FT   DISULFID    386    421       {ECO:0000250}.
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   DISULFID    595    618       {ECO:0000250}.
FT   DISULFID    627    659       {ECO:0000250}.
SQ   SEQUENCE   688 AA;  76700 MW;  F10A1DC565875A73 CRC64;
     MWYLVLFSLL ASFSAEPTMH GEILSPNYPQ AYPNDVVKSW DIEVPEGFGI HLYFTHVDIE
     PSESCAYDSV QIISGGIEEG RLCGQRTSKS PNSPIIEEFQ FPYNKLQVVF TSDFSIEEQF
     TGFAAYYTAI DVNECTDFTD VPCSHFCNNF IGGYFCSCPP EYFLHDDMRN CGVNCSGDVF
     TALIGEISSP NYPNPYPENS RCEYQIQLQE GFQVVVTMQR EDFDVEPADS EGNCPDSLTF
     AAKNQQFGPY CGDGFPGPLT IRTQSNTLGI VFQTDLMGQK KGWKLRYHGD PISCPKESTA
     NSNWEPDKAK YVFKDVVKIT CVDGFEVVEG HVSSTSYYST CQSDGQWSNS GLKCQPVYCG
     IPDPIANGKV EEPENSVFGT VIHYTCEEPY YYMEHEEGGE YRCAANGRWV NDQLGIELPR
     CIPVCGVPTE PFQVQQKIFG GQPAKIENFP WQVFFNHPTA GGALINEYWV LTAAHVVEKN
     SDPSMYAGIT ALRLADLENA QRLYTKRVII HPGWKEDDDL NPRTNFDNDI ALVQLKDPVK
     MGPKFSPICL PGTSSEYNLS PGDMGLISGW GRTEKRLHVI NLRGAKVPVT SLETCKQVKE
     ENPTARPEDY VITDNMICAG EKGVDSCKGD SGGAFAFQVP NVKAPKFYVA GLVSWGKKCG
     AYGVYTKVKN YVDWILKTMQ ENSGPRKD
//
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