C1QA_RAT
ID C1QA_RAT Reviewed; 245 AA.
AC P31720; Q5RJK1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Complement C1q subcomponent subunit A;
DE Flags: Precursor;
GN Name=C1qa;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [2]
RP PROTEIN SEQUENCE OF 23-37.
RX PubMed=8464426; DOI=10.1016/0161-5890(93)90111-n;
RA Wing M.G., Seilly D.J., Bridgman D.J., Harrison R.A.;
RT "Rapid isolation and biochemical characterization of rat C1 and C1q.";
RL Mol. Immunol. 30:433-440(1993).
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 -!- 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; BC086605; AAH86605.1; -; mRNA.
DR RefSeq; NP_001008515.1; NM_001008515.1.
DR AlphaFoldDB; P31720; -.
DR SMR; P31720; -.
DR BioGRID; 255938; 1.
DR IntAct; P31720; 1.
DR MINT; P31720; -.
DR STRING; 10116.ENSRNOP00000017385; -.
DR GlyGen; P31720; 4 sites.
DR jPOST; P31720; -.
DR PaxDb; P31720; -.
DR PRIDE; P31720; -.
DR Ensembl; ENSRNOT00000017385; ENSRNOP00000017385; ENSRNOG00000012807.
DR GeneID; 298566; -.
DR KEGG; rno:298566; -.
DR CTD; 712; -.
DR RGD; 1306716; C1qa.
DR eggNOG; ENOG502RZM2; Eukaryota.
DR GeneTree; ENSGT00940000162143; -.
DR HOGENOM; CLU_001074_0_2_1; -.
DR InParanoid; P31720; -.
DR OMA; DMVITNQ; -.
DR OrthoDB; 1258047at2759; -.
DR PhylomeDB; P31720; -.
DR TreeFam; TF329591; -.
DR Reactome; R-RNO-166663; Initial triggering of complement.
DR Reactome; R-RNO-173623; Classical antibody-mediated complement activation.
DR Reactome; R-RNO-977606; Regulation of Complement cascade.
DR PRO; PR:P31720; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000012807; Expressed in spleen and 20 other tissues.
DR Genevisible; P31720; RN.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062167; C:complement component C1q complex; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:ARUK-UCL.
DR GO; GO:0007568; P:aging; ISO:RGD.
DR GO; GO:0048143; P:astrocyte activation; ISO:RGD.
DR GO; GO:0006958; P:complement activation, classical pathway; ISO:RGD.
DR GO; GO:0150062; P:complement-mediated synapse pruning; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0001774; P:microglial cell activation; ISO:RGD.
DR GO; GO:0016322; P:neuron remodeling; ISO:RGD.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:RGD.
DR GO; GO:0010039; P:response to iron ion; IEP:RGD.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
DR GO; GO:0098883; P:synapse pruning; ISO:RGD.
DR GO; GO:0150064; P:vertebrate eye-specific patterning; ISO:RGD.
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; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydroxylation; Immunity; Innate immunity; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:8464426"
FT CHAIN 23..245
FT /note="Complement C1q subcomponent subunit A"
FT /id="PRO_0000003520"
FT DOMAIN 31..109
FT /note="Collagen-like"
FT DOMAIN 110..245
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 35..111
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"
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"
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"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT CARBOHYD 48
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT CARBOHYD 67
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT CARBOHYD 100
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26
FT /note="Interchain (with C-29 in B chain)"
SQ SEQUENCE 245 AA; 25917 MW; 5AFD351C2278E09A CRC64;
METSQGWLVA CVLAVTLVWT VAEDVCRAPN GKDGVAGIPG RPGRPGLKGE RGEPGAAGIR
TGIRGLKGDM GESGPPGKPG NVGFPGPTGP LGNSGPQGLK GVKGNPGNIR DQPRPAFSAI
RQNPPTYGNV VVFDKVLTNQ ENPYQNRTGH FICAVPGFYY FTFQVISKWD LCLSIVSSSR
GQPRNSLGFC DTNSKGLFQV LAGGTVLQLQ RGDEVWIEKD PAKGRIYQGT EADSIFSGFL
IFPSA
