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-MAY-2013, entry version 84.
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).
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 (By similarity).
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).
CC -!- TISSUE SPECIFICITY: Specifically expressed in male reproductive
CC tissues.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC aspartate and asparagine is (R) stereospecific within EGF domains
CC (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC -!- SIMILARITY: Contains 2 CUB domains.
CC -!- SIMILARITY: Contains 1 EGF-like domain.
CC -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC -!- SIMILARITY: Contains 2 Sushi (CCP/SCR) domains.
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DR EMBL; AF459020; AAO15559.1; -; mRNA.
DR IPI; IPI00474340; -.
DR RefSeq; NP_776289.2; NM_173864.2.
DR UniGene; Mm.483270; -.
DR ProteinModelPortal; Q8CFG8; -.
DR SMR; Q8CFG8; 18-287, 292-683.
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 MGI; MGI:3644269; Gm5077.
DR eggNOG; COG5640; -.
DR HOGENOM; HOG000237311; -.
DR HOVERGEN; HBG000559; -.
DR InParanoid; Q8CFG8; -.
DR KO; K01331; -.
DR OrthoDB; EOG4H19VC; -.
DR NextBio; 394148; -.
DR ArrayExpress; Q8CFG8; -.
DR Bgee; Q8CFG8; -.
DR CleanEx; MM_C1S; -.
DR Genevestigator; Q8CFG8; -.
DR GermOnline; ENSMUSG00000038521; Mus musculus.
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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.290; -; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd.
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; PF07645; EGF_CA; 1.
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; SSF57535; Complement_control_module; 2.
DR SUPFAM; SSF49854; CUB; 2.
DR SUPFAM; SSF50494; Pept_Ser_Cys; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS00022; EGF_1; FALSE_NEG.
DR PROSITE; PS01186; EGF_2; FALSE_NEG.
DR PROSITE; PS50026; EGF_3; FALSE_NEG.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50923; SUSHI; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; FALSE_NEG.
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 By similarity.
FT CHAIN 16 688 Complement C1s-B subcomponent.
FT /FTId=PRO_0000042196.
FT CHAIN 16 437 Complement C1s-B subcomponent heavy chain
FT (By similarity).
FT /FTId=PRO_0000042197.
FT CHAIN 438 688 Complement C1s-B subcomponent light chain
FT (By similarity).
FT /FTId=PRO_0000042198.
FT DOMAIN 16 130 CUB 1.
FT DOMAIN 131 172 EGF-like; calcium-binding (Potential).
FT DOMAIN 175 290 CUB 2.
FT DOMAIN 292 356 Sushi 1.
FT DOMAIN 357 423 Sushi 2.
FT DOMAIN 438 680 Peptidase S1.
FT ACT_SITE 475 475 Charge relay system (By similarity).
FT ACT_SITE 529 529 Charge relay system (By similarity).
FT ACT_SITE 631 631 Charge relay system (By similarity).
FT METAL 60 60 Calcium (By similarity).
FT METAL 68 68 Calcium (By similarity).
FT METAL 113 113 Calcium (By similarity).
FT METAL 131 131 Calcium (By similarity).
FT METAL 132 132 Calcium; via carbonyl oxygen (By
FT similarity).
FT METAL 134 134 Calcium (By similarity).
FT METAL 149 149 Calcium (By similarity).
FT METAL 150 150 Calcium; via carbonyl oxygen (By
FT similarity).
FT METAL 153 153 Calcium; via carbonyl oxygen (By
FT similarity).
FT MOD_RES 149 149 (3R)-3-hydroxyasparagine (By similarity).
FT CARBOHYD 174 174 N-linked (GlcNAc...) (Potential).
FT DISULFID 65 83 By similarity.
FT DISULFID 135 147 By similarity.
FT DISULFID 143 156 By similarity.
FT DISULFID 158 171 By similarity.
FT DISULFID 175 202 By similarity.
FT DISULFID 234 251 By similarity.
FT DISULFID 294 341 By similarity.
FT DISULFID 321 354 By similarity.
FT DISULFID 359 403 By similarity.
FT DISULFID 386 421 By similarity.
FT DISULFID 425 549 Interchain (between heavy and light
FT chains) (By similarity).
FT DISULFID 595 618 By similarity.
FT DISULFID 627 659 By similarity.
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
//
