C1QC_RAT
ID C1QC_RAT Reviewed; 245 AA.
AC P31722; Q5RJZ8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Complement C1q subcomponent subunit C;
DE Flags: Precursor;
GN Name=C1qc; Synonyms=C1qg;
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=Ovary;
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 29-56.
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, C1r and
CC C1s 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 In addition to the major A:B and C:C dimer bands, rat, unlike human
CC C1q, contained minor dimer species.
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; BC086409; AAH86409.1; -; mRNA.
DR RefSeq; NP_001008524.1; NM_001008524.1.
DR AlphaFoldDB; P31722; -.
DR SMR; P31722; -.
DR BioGRID; 263599; 3.
DR IntAct; P31722; 2.
DR MINT; P31722; -.
DR STRING; 10116.ENSRNOP00000017065; -.
DR PaxDb; P31722; -.
DR PRIDE; P31722; -.
DR GeneID; 362634; -.
DR KEGG; rno:362634; -.
DR UCSC; RGD:1306828; rat.
DR CTD; 714; -.
DR RGD; 1306828; C1qc.
DR eggNOG; ENOG502RZM2; Eukaryota.
DR HOGENOM; CLU_001074_0_2_1; -.
DR InParanoid; P31722; -.
DR PhylomeDB; P31722; -.
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:P31722; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P31722; 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:0006958; P:complement activation, classical pathway; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0030853; P:negative regulation of granulocyte differentiation; ISO:RGD.
DR GO; GO:0045650; P:negative regulation of macrophage differentiation; ISO:RGD.
DR GO; GO:0098883; P:synapse pruning; ISO:RGD.
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; Direct protein sequencing; Disulfide bond;
KW Hydroxylation; Immunity; Innate immunity; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:8464426"
FT CHAIN 29..245
FT /note="Complement C1q subcomponent subunit C"
FT /id="PRO_0000003526"
FT DOMAIN 31..112
FT /note="Collagen-like"
FT DOMAIN 115..245
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 42..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 39
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 45
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 63
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 75
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 81
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 96
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 99
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 105
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT DISULFID 32
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 245 AA; 25686 MW; D3CB28932537B4E3 CRC64;
MVVGTSCQPQ HGLYLLLLLL ALPLRSQANA GCYGIPGMPG LPGTPGKDGH DGLQGPKGEP
GIPAIPGTQG PKGQKGEPGM PGHRGKNGPM GTSGSPGDPG PRGPPGEPGE EGRYKQKHQS
VFTVTRQTAQ YPAANGLVKF NSAITNPQGD YNTNTGKFTC KVPGLYYFVH HTSQTANLCV
QLLLNNAKVT SFCDHMSNSK QVSSGGVLLR LQRGDEVWLA VNDYNGMVGT EGSDSVFSGF
LLFPD
