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   24-JAN-2024, entry version 167.
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   GlyCosmos; Q8CG16; 3 sites, No reported glycans.
DR   GlyGen; Q8CG16; 3 sites.
DR   iPTMnet; Q8CG16; -.
DR   PhosphoSitePlus; Q8CG16; -.
DR   MaxQB; Q8CG16; -.
DR   PaxDb; 10090-ENSMUSP00000063707; -.
DR   PeptideAtlas; Q8CG16; -.
DR   ProteomicsDB; 265402; -.
DR   Pumba; Q8CG16; -.
DR   DNASU; 50909; -.
DR   Ensembl; ENSMUST00000068593.9; ENSMUSP00000063707.8; ENSMUSG00000055172.11.
DR   GeneID; 50909; -.
DR   KEGG; mmu:50909; -.
DR   UCSC; uc009dra.2; mouse.
DR   AGR; MGI:1355313; -.
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; RIPACLP; -.
DR   OrthoDB; 5394076at2759; -.
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 77 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 cell types or tissues.
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:0140313; F:molecular sequestering activity; ISO:MGI.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
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:0031638; P:zymogen activation; ISO:MGI.
DR   CDD; cd00033; CCP; 2.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 2.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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; IPR024175; Pept_S1A_C1r/C1S/mannan-bd.
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; COMPLEMENT C1R SUBCOMPONENT; 1.
DR   PANTHER; PTHR24255; COMPLEMENT COMPONENT 1, S SUBCOMPONENT-RELATED; 1.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF14670; FXa_inhibition; 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; SM00181; EGF; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
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.
DR   Genevisible; Q8CG16; MM.
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
//