C1RA_MOUSE
ID C1RA_MOUSE Reviewed; 707 AA.
AC Q8CG16; Q99KI6; Q9ET60;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Complement C1r-A subcomponent;
DE EC=3.4.21.41;
DE AltName: Full=Complement component 1 subcomponent r-A;
DE Contains:
DE RecName: Full=Complement C1r-A subcomponent heavy chain;
DE Contains:
DE RecName: Full=Complement C1r-A subcomponent light chain;
DE Flags: Precursor;
GN Name=C1ra; 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].
RC STRAIN=C57BL/6J;
RA Byun S.J., Hyun J.H., Hwang H.Y., Ryoo Z.Y., Kim T.Y.;
RT "Cloning and sequencing of a cDNA encoding a serine protease homologous to
RT human complement C1r precursor from an allografted mouse skin and its
RT expression in Escherichia coli.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-220.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
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.
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 -!- 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; AF148216; AAG01898.1; -; mRNA.
DR EMBL; AF459011; AAO15553.1; -; Genomic_DNA.
DR EMBL; AF459008; AAO15553.1; JOINED; Genomic_DNA.
DR EMBL; AF459009; AAO15553.1; JOINED; Genomic_DNA.
DR EMBL; AF459010; AAO15553.1; JOINED; Genomic_DNA.
DR EMBL; BC004637; AAH04637.1; -; mRNA.
DR CCDS; CCDS20521.1; -.
DR RefSeq; NP_075632.3; NM_023143.3.
DR AlphaFoldDB; Q8CG16; -.
DR SMR; Q8CG16; -.
DR ComplexPortal; CPX-4984; Complement C1 complex, C1ra-C1sa variant.
DR STRING; 10090.ENSMUSP00000063707; -.
DR MEROPS; S01.209; -.
DR GlyGen; Q8CG16; 3 sites.
DR iPTMnet; Q8CG16; -.
DR PhosphoSitePlus; Q8CG16; -.
DR MaxQB; Q8CG16; -.
DR PaxDb; Q8CG16; -.
DR PeptideAtlas; Q8CG16; -.
DR PRIDE; Q8CG16; -.
DR ProteomicsDB; 265402; -.
DR DNASU; 50909; -.
DR Ensembl; ENSMUST00000068593; ENSMUSP00000063707; ENSMUSG00000055172.
DR GeneID; 50909; -.
DR KEGG; mmu:50909; -.
DR UCSC; uc009dra.2; mouse.
DR CTD; 50909; -.
DR MGI; MGI:1355313; C1ra.
DR VEuPathDB; HostDB:ENSMUSG00000055172; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000158621; -.
DR HOGENOM; CLU_006842_14_1_1; -.
DR InParanoid; Q8CG16; -.
DR OMA; REKCQSW; -.
DR OrthoDB; 156878at2759; -.
DR PhylomeDB; Q8CG16; -.
DR TreeFam; TF330373; -.
DR Reactome; R-MMU-166663; Initial triggering of complement.
DR Reactome; R-MMU-173623; Classical antibody-mediated complement activation.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 50909; 2 hits in 72 CRISPR screens.
DR ChiTaRS; C1ra; mouse.
DR PRO; PR:Q8CG16; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8CG16; protein.
DR Bgee; ENSMUSG00000055172; Expressed in mesenteric lymph node and 97 other tissues.
DR Genevisible; Q8CG16; 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; -; 1.
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 1: Evidence at protein 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..707
FT /note="Complement C1r-A subcomponent"
FT /id="PRO_0000027580"
FT CHAIN 17..462
FT /note="Complement C1r-A subcomponent heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027581"
FT CHAIN 463..707
FT /note="Complement C1r-A subcomponent light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027582"
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..704
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 559
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 656
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:0000269|PubMed:17330941"
FT CARBOHYD 583
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..579
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 622..641
FT /evidence="ECO:0000250"
FT DISULFID 652..682
FT /evidence="ECO:0000250"
FT CONFLICT 101
FT /note="S -> R (in Ref. 1; AAG01898)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="N -> H (in Ref. 3; AAH04637)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 80073 MW; 29DAAEB3C047D8E8 CRC64;
MWLFALLVTL FYGVEGSIYL PQKLYGEVTS PLYPKPYPSD LETTTVITVP MGYRVKLVFW
QFDVEPSEGC FYDYVKISAD 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 DYFIVTCKQG YQLMEGNQAL LSFTAVCQND
GTWHRAMPRC KIKNCGQPQS LSNGDFRYIT TKGVTTYEAS IQYHCHEPYY KMLTRAGSSE
SMRGIYTCTA QGIWKNEEEG EKMPRCLPVC GKPVNPVTQK ERIIRGQPAR PGNFPWQAFT
TTHGRGGGAL LGDRWILTAA HTIYPKHHNK ENDNANPKML VFLGHTNVEQ IKKLGHHPVR
RVIIHPDYRQ DEPNNFEGDI ALLELENSVT LGPELLPICL PDNETFYGQG LMGYVSGFGI
TEDKLAFDLR FVRLPVADSE ACQRWLQTKK DTSPFSQNMF CSGDPAVQQD ACQGDSGGVF
AVRDRNRDIW VATGIVSWGI GCGEGYGFYT KVLNYVDWIK KEMGDEN
