C1QA_MOUSE
ID C1QA_MOUSE Reviewed; 245 AA.
AC P98086; Q9DCM6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Complement C1q subcomponent subunit A;
DE Flags: Precursor;
GN Name=C1qa;
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=1940381;
RA Petry F., Reid K.B.M., Loos M.;
RT "Gene expression of the A- and B-chain of mouse C1q in different tissues
RT and the characterization of the recombinant A-chain.";
RL J. Immunol. 147:3988-3993(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129; 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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Epididymis, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=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 [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-146.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Spleen;
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 Interacts (via C-terminus) with CD33; this interaction activates CD33
CC inhibitory motifs. {ECO:0000250|UniProtKB:P02745}.
CC -!- INTERACTION:
CC P98086; Q9H461: FZD8; Xeno; NbExp=3; IntAct=EBI-299840, EBI-6254212;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: O-linked glycans are Glc-Gal disaccharides typically found as
CC secondary modifications of hydroxylated lysines in collagen-like
CC domains. {ECO:0000250|UniProtKB:P02745}.
CC -!- PTM: Proline residues in the collagen-like domain motif, GXPG, are
CC typically 4-hydroxylated. {ECO:0000250|UniProtKB:P02745}.
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DR EMBL; X58861; CAA41664.1; -; mRNA.
DR EMBL; AK002655; BAB22262.1; -; mRNA.
DR EMBL; AK136737; BAE23115.1; -; mRNA.
DR EMBL; AK159210; BAE34901.1; -; mRNA.
DR EMBL; AL627214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466552; EDL29926.1; -; Genomic_DNA.
DR EMBL; BC002086; AAH02086.1; -; mRNA.
DR CCDS; CCDS18812.1; -.
DR PIR; S19018; S19018.
DR RefSeq; NP_031598.2; NM_007572.2.
DR AlphaFoldDB; P98086; -.
DR SMR; P98086; -.
DR BioGRID; 198412; 6.
DR ComplexPortal; CPX-4981; Complement component C1q complex.
DR IntAct; P98086; 7.
DR MINT; P98086; -.
DR STRING; 10090.ENSMUSP00000048836; -.
DR GlyConnect; 2223; 7 N-Linked glycans (1 site).
DR GlyGen; P98086; 4 sites, 7 N-linked glycans (1 site).
DR iPTMnet; P98086; -.
DR PhosphoSitePlus; P98086; -.
DR SwissPalm; P98086; -.
DR CPTAC; non-CPTAC-3638; -.
DR CPTAC; non-CPTAC-5581; -.
DR jPOST; P98086; -.
DR PaxDb; P98086; -.
DR PeptideAtlas; P98086; -.
DR PRIDE; P98086; -.
DR ProteomicsDB; 265397; -.
DR Antibodypedia; 707; 451 antibodies from 35 providers.
DR DNASU; 12259; -.
DR Ensembl; ENSMUST00000046285; ENSMUSP00000048836; ENSMUSG00000036887.
DR GeneID; 12259; -.
DR KEGG; mmu:12259; -.
DR UCSC; uc008vir.1; mouse.
DR CTD; 712; -.
DR MGI; MGI:88223; C1qa.
DR VEuPathDB; HostDB:ENSMUSG00000036887; -.
DR eggNOG; ENOG502RZM2; Eukaryota.
DR GeneTree; ENSGT00940000162143; -.
DR HOGENOM; CLU_001074_0_2_1; -.
DR InParanoid; P98086; -.
DR OMA; DMVITNQ; -.
DR OrthoDB; 1258047at2759; -.
DR PhylomeDB; P98086; -.
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; 12259; 0 hits in 72 CRISPR screens.
DR ChiTaRS; C1qa; mouse.
DR PRO; PR:P98086; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P98086; protein.
DR Bgee; ENSMUSG00000036887; Expressed in stroma of bone marrow and 215 other tissues.
DR ExpressionAtlas; P98086; baseline and differential.
DR Genevisible; P98086; 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:0007568; P:aging; IGI:ARUK-UCL.
DR GO; GO:0048143; P:astrocyte activation; IGI:ARUK-UCL.
DR GO; GO:0006958; P:complement activation, classical pathway; IMP:MGI.
DR GO; GO:0150062; P:complement-mediated synapse pruning; IMP:ARUK-UCL.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0001774; P:microglial cell activation; IGI:ARUK-UCL.
DR GO; GO:0016322; P:neuron remodeling; IMP:ARUK-UCL.
DR GO; GO:1901216; P:positive regulation of neuron death; IGI:ARUK-UCL.
DR GO; GO:0050808; P:synapse organization; IGI:ARUK-UCL.
DR GO; GO:0098883; P:synapse pruning; IGI:ARUK-UCL.
DR GO; GO:0150064; P:vertebrate eye-specific patterning; IMP:ARUK-UCL.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR037572; Complement_C1q_A.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR PANTHER; PTHR15427:SF26; PTHR15427:SF26; 1.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF01391; Collagen; 1.
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; Glycoprotein; Hydroxylation;
KW Immunity; Innate immunity; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..245
FT /note="Complement C1q subcomponent subunit A"
FT /id="PRO_0000003518"
FT DOMAIN 31..109
FT /note="Collagen-like"
FT DOMAIN 110..245
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 28..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT MOD_RES 45
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT MOD_RES 48
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT MOD_RES 54
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT MOD_RES 67
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT MOD_RES 79
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT MOD_RES 85
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT MOD_RES 100
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT CARBOHYD 48
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT CARBOHYD 67
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT CARBOHYD 100
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT DISULFID 26
FT /note="Interchain (with C-29 in B chain)"
FT /evidence="ECO:0000250"
FT CONFLICT 16
FT /note="T -> I (in Ref. 1; CAA41664)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 25974 MW; 41C2066D49592020 CRC64;
METSQGWLVA CVLTMTLVWT VAEDVCRAPN GKDGAPGNPG RPGRPGLKGE RGEPGAAGIR
TGIRGFKGDP GESGPPGKPG NVGLPGPSGP LGDSGPQGLK GVKGNPGNIR DQPRPAFSAI
RQNPMTLGNV VIFDKVLTNQ ESPYQNHTGR FICAVPGFYY FNFQVISKWD LCLFIKSSSG
GQPRDSLSFS NTNNKGLFQV LAGGTVLQLR RGDEVWIEKD PAKGRIYQGT EADSIFSGFL
IFPSA
