C1RB_MOUSE
ID C1RB_MOUSE Reviewed; 706 AA.
AC Q8CFG9;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Complement C1r-B subcomponent;
DE EC=3.4.21.41;
DE AltName: Full=Complement component 1 subcomponent r-B;
DE Contains:
DE RecName: Full=Complement C1r-B subcomponent heavy chain;
DE Contains:
DE RecName: Full=Complement C1r-B subcomponent light chain;
DE Flags: Precursor;
GN Name=C1rb; Synonyms=C1r;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
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: differential
RT expression generates alternative isomorphs in the liver and in the male
RT reproductive system.";
RL Biochem. J. 371:631-640(2003).
CC -!- FUNCTION: C1r B chain is a serine protease that combines with C1q and
CC C1s to form C1, the first component of the classical pathway of the
CC complement system. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Lys(or Arg)-|-Ile bond in complement
CC subcomponent C1s to form the active form of C1s (EC 3.4.21.42).;
CC EC=3.4.21.41;
CC -!- SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q, C1r and
CC C1s in the molar ration of 1:2:2. C1r is a dimer of identical chains,
CC each of which is activated by cleavage into two chains, A and B,
CC connected by disulfide bonds (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 aspartate
CC and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AF459018; AAO15557.1; -; mRNA.
DR CCDS; CCDS71834.1; -.
DR RefSeq; NP_001106827.1; NM_001113356.1.
DR AlphaFoldDB; Q8CFG9; -.
DR SMR; Q8CFG9; -.
DR BioGRID; 579098; 2.
DR ComplexPortal; CPX-4985; Complement C1 complex, C1rb-C1sb variant.
DR STRING; 10090.ENSMUSP00000139376; -.
DR MEROPS; S01.209; -.
DR GlyGen; Q8CFG9; 3 sites.
DR PhosphoSitePlus; Q8CFG9; -.
DR CPTAC; non-CPTAC-3451; -.
DR MaxQB; Q8CFG9; -.
DR PeptideAtlas; Q8CFG9; -.
DR PRIDE; Q8CFG9; -.
DR ProteomicsDB; 273806; -.
DR Ensembl; ENSMUST00000184647; ENSMUSP00000139376; ENSMUSG00000098470.
DR GeneID; 667277; -.
DR KEGG; mmu:667277; -.
DR UCSC; uc009drd.1; mouse.
DR CTD; 667277; -.
DR MGI; MGI:3779804; C1rb.
DR VEuPathDB; HostDB:ENSMUSG00000098470; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000158621; -.
DR HOGENOM; CLU_006842_14_1_1; -.
DR InParanoid; Q8CFG9; -.
DR OMA; THEVKCP; -.
DR OrthoDB; 156878at2759; -.
DR PhylomeDB; Q8CFG9; -.
DR BioGRID-ORCS; 667277; 0 hits in 66 CRISPR screens.
DR ChiTaRS; C1rb; mouse.
DR PRO; PR:Q8CFG9; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8CFG9; protein.
DR Bgee; ENSMUSG00000098470; Expressed in white adipose tissue and 18 other tissues.
DR Genevisible; Q8CFG9; MM.
DR GO; GO:0072562; C:blood microparticle; IBA:GO_Central.
DR GO; GO:0005602; C:complement component C1 complex; IC:ComplexPortal.
DR GO; GO:0005576; C:extracellular region; IC:ComplexPortal.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0006958; P:complement activation, classical pathway; IC:ComplexPortal.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031638; P:zymogen activation; ISO:MGI.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 3.
DR Gene3D; 2.60.120.290; -; 2.
DR InterPro; IPR035707; Complement_C1r.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24255:SF25; PTHR24255:SF25; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00032; CCP; 2.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00181; EGF; 1.
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; PS01186; EGF_2; 1.
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 Complement pathway; Disulfide bond; EGF-like domain; Glycoprotein;
KW Hydrolase; Hydroxylation; Immunity; Innate immunity; Phosphoprotein;
KW Protease; Reference proteome; Repeat; Serine protease; Signal; Sushi.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT CHAIN 17..706
FT /note="Complement C1r-B subcomponent"
FT /id="PRO_0000042187"
FT CHAIN 17..462
FT /note="Complement C1r-B subcomponent heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042188"
FT CHAIN 463..706
FT /note="Complement C1r-B subcomponent light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042189"
FT DOMAIN 17..140
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 141..189
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000255"
FT DOMAIN 192..304
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 306..372
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 373..448
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 463..703
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 501
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 558
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 655
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 166
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000250"
FT MOD_RES 205
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P00736"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..88
FT /evidence="ECO:0000250"
FT DISULFID 145..164
FT /evidence="ECO:0000250"
FT DISULFID 160..173
FT /evidence="ECO:0000250"
FT DISULFID 175..188
FT /evidence="ECO:0000250"
FT DISULFID 192..219
FT /evidence="ECO:0000250"
FT DISULFID 249..267
FT /evidence="ECO:0000250"
FT DISULFID 308..357
FT /evidence="ECO:0000250"
FT DISULFID 337..370
FT /evidence="ECO:0000250"
FT DISULFID 375..428
FT /evidence="ECO:0000250"
FT DISULFID 405..446
FT /evidence="ECO:0000250"
FT DISULFID 450..578
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
FT ProRule:PRU00302"
FT DISULFID 621..640
FT /evidence="ECO:0000250"
FT DISULFID 651..681
FT /evidence="ECO:0000250"
SQ SEQUENCE 706 AA; 79936 MW; 092684922F41A64F CRC64;
MWLFALLVTL FYGVEGSIYL PQKLYGEVTS PLYPKPYPSD LETTTVITVP MGYRVKLVFW
QFDVEPSEGC LYDYVKISAD KQTLGRFCGQ LDSPLGNPPG SKEFMSQGNK MLLTFHTDFS
NEENGTIMFY KGFLAYYQAV DLDECASQPN SVEEGLQPRC QHLCHNYVGG YFCSCHPGYE
LQKDGQSCQA ECSSELYTEP SGYVSSLEYP QPYPPDLRCN YSIRVERGLT VHLKFLDPFE
IDDHQQVHCP YDQLQIYANG KNLGEFCGKQ RPPDLDTSSN AVDLLFFTDE SGDSRGWKLH
YTTETIKCPQ PKALDEFTII QDPQPQYQFR DYFTVTCKQG YQLMEGNQAL LSFTAVCQHD
GTWHRAMPRC KIKNCGQPQS LSNGDFRYIT TKGVTTYEAS IQYHCHEPYY KMLTRAGSSE
SMRGIYTCTA QGIWKNEEEG EKMPRCLPVC GKPVNPVTQK ERIIGGQPAR PGNFPWQAFT
TIYGPGGGAL LGDRWILTAA HTIYPKYPNK GKNTNPRTLV FLGHTNMEQI QKLGHHPVRR
VIIHPDYRQE EPDNFEGDIA LLELENSVTL GPELLPICLP DNETFYGQGL MGYVSGFGTT
GNRIPFHLRF VRLPVADREA CQRWLWTKKD TSPFSQNMFC SGDPAVQQDA CQGDSGGVFA
VRDRNRDIWV ATGIVSWGIG CGEGYGFYTK VLNYVDWIKK EMGDEN
