C1QC_MOUSE
ID C1QC_MOUSE Reviewed; 246 AA.
AC Q02105; Q6DI63;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Complement C1q subcomponent subunit C;
DE Flags: Precursor;
GN Name=C1qc; Synonyms=C1qg;
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=ICR; TISSUE=Macrophage;
RX PubMed=1396691; DOI=10.1111/j.1432-1033.1992.tb17269.x;
RA Petry F., Reid K.B.M., Loos M.;
RT "Isolation, sequence analysis and characterization of cDNA clones coding
RT for the C chain of mouse C1q. Sequence similarity of complement
RT subcomponent C1q, collagen type VIII and type X and precerebellin.";
RL Eur. J. Biochem. 209:129-134(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8606057; DOI=10.1007/bf02199805;
RA Petry F., McClive P.J., Botto M., Morley B.J., Morahan G., Loos M.;
RT "The mouse C1q genes are clustered on chromosome 4 and show conservation of
RT gene organization.";
RL Immunogenetics 43:370-376(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Colon, Kidney, and Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: C1q associates with the proenzymes C1r and C1s to yield C1,
CC the first component of the serum complement system. The collagen-like
CC regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2)
CC proenzyme complex, and efficient activation of C1 takes place on
CC interaction of the globular heads of C1q with the Fc regions of IgG or
CC IgM antibody present in immune complexes.
CC -!- SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q, R and S
CC in the molar ration of 1:2:2. C1q subcomponent is composed of nine
CC subunits, six of which are disulfide-linked dimers of the A and B
CC chains, and three of which are disulfide-linked dimers of the C chain.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Hydroxylation on proline residues within the sequence motif, GXPG,
CC is most likely to be 4-hydroxy as this fits the requirement for 4-
CC hydroxylation in vertebrates. {ECO:0000250}.
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DR EMBL; X66295; CAA46993.1; -; mRNA.
DR EMBL; X92960; CAA63535.1; -; Genomic_DNA.
DR EMBL; AL627214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC043945; AAH43945.1; -; mRNA.
DR EMBL; BC054443; AAH54443.1; -; mRNA.
DR EMBL; BC075724; AAH75724.1; -; mRNA.
DR CCDS; CCDS18811.1; -.
DR PIR; S29328; S29328.
DR RefSeq; NP_031600.2; NM_007574.2.
DR RefSeq; XP_017175416.1; XM_017319927.1.
DR AlphaFoldDB; Q02105; -.
DR SMR; Q02105; -.
DR BioGRID; 198415; 10.
DR ComplexPortal; CPX-4981; Complement component C1q complex.
DR IntAct; Q02105; 2.
DR MINT; Q02105; -.
DR STRING; 10090.ENSMUSP00000036747; -.
DR iPTMnet; Q02105; -.
DR PhosphoSitePlus; Q02105; -.
DR CPTAC; non-CPTAC-3302; -.
DR CPTAC; non-CPTAC-3357; -.
DR PaxDb; Q02105; -.
DR PeptideAtlas; Q02105; -.
DR PRIDE; Q02105; -.
DR ProteomicsDB; 273852; -.
DR Antibodypedia; 691; 315 antibodies from 34 providers.
DR DNASU; 12262; -.
DR Ensembl; ENSMUST00000046332; ENSMUSP00000036747; ENSMUSG00000036896.
DR GeneID; 12262; -.
DR KEGG; mmu:12262; -.
DR UCSC; uc008viq.1; mouse.
DR CTD; 714; -.
DR MGI; MGI:88225; C1qc.
DR VEuPathDB; HostDB:ENSMUSG00000036896; -.
DR eggNOG; ENOG502RZM2; Eukaryota.
DR GeneTree; ENSGT00940000161227; -.
DR HOGENOM; CLU_001074_0_2_1; -.
DR InParanoid; Q02105; -.
DR OMA; RGTNEYP; -.
DR OrthoDB; 1258047at2759; -.
DR PhylomeDB; Q02105; -.
DR TreeFam; TF329591; -.
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; 12262; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q02105; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q02105; protein.
DR Bgee; ENSMUSG00000036896; Expressed in stroma of bone marrow and 179 other tissues.
DR Genevisible; Q02105; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005602; C:complement component C1 complex; IC:ComplexPortal.
DR GO; GO:0062167; C:complement component C1q complex; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0098794; C:postsynapse; IGI:ARUK-UCL.
DR GO; GO:0045202; C:synapse; IDA:ARUK-UCL.
DR GO; GO:0006958; P:complement activation, classical pathway; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0030853; P:negative regulation of granulocyte differentiation; ISO:MGI.
DR GO; GO:0045650; P:negative regulation of macrophage differentiation; ISO:MGI.
DR GO; GO:0098883; P:synapse pruning; IGI:ARUK-UCL.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF01391; Collagen; 2.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 1: Evidence at protein level;
KW Collagen; Complement pathway; Disulfide bond; Hydroxylation; Immunity;
KW Innate immunity; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT CHAIN 30..246
FT /note="Complement C1q subcomponent subunit C"
FT /id="PRO_0000003525"
FT DOMAIN 32..113
FT /note="Collagen-like"
FT DOMAIN 116..246
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 44..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 40
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 43
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 64
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 76
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 82
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 97
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 100
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 106
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT DISULFID 33
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 10
FT /note="P -> Q (in Ref. 1; CAA46993, 2; CAA63535 and 4;
FT AAH43945/AAH54443)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="R -> Q (in Ref. 1; CAA46993 and 4; AAH43945/
FT AAH54443)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="V -> A (in Ref. 1; CAA46993 and 4; AAH43945/
FT AAH54443)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 25992 MW; D3D2EB5851359791 CRC64;
MVVGPSCQPP CGLCLLLLFL LALPLRSQAS AGCYGIPGMP GMPGAPGKDG HDGLQGPKGE
PGIPAVPGTR GPKGQKGEPG MPGHRGKNGP RGTSGLPGDP GPRGPPGEPG VEGRYKQKHQ
SVFTVTRQTT QYPEANALVR FNSVVTNPQG HYNPSTGKFT CEVPGLYYFV YYTSHTANLC
VHLNLNLARV ASFCDHMFNS KQVSSGGVLL RLQRGDEVWL SVNDYNGMVG IEGSNSVFSG
FLLFPD
