C1QA_BOVIN
ID C1QA_BOVIN Reviewed; 244 AA.
AC Q5E9E3; Q56JV0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Complement C1q subcomponent subunit A;
DE Flags: Precursor;
GN Name=C1QA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymphoid epithelium;
RA Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.;
RT "Analysis of sequences obtained from constructed full-length bovine cDNA
RT libraries.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; BT020977; AAX08994.1; -; mRNA.
DR EMBL; AY911382; AAW82145.1; -; mRNA.
DR EMBL; BC105345; AAI05346.1; -; mRNA.
DR RefSeq; NP_001014945.1; NM_001014945.2.
DR RefSeq; XP_005203271.1; XM_005203214.3.
DR AlphaFoldDB; Q5E9E3; -.
DR SMR; Q5E9E3; -.
DR STRING; 9913.ENSBTAP00000009415; -.
DR PaxDb; Q5E9E3; -.
DR PRIDE; Q5E9E3; -.
DR Ensembl; ENSBTAT00000009415; ENSBTAP00000009415; ENSBTAG00000007153.
DR Ensembl; ENSBTAT00000040146; ENSBTAP00000039925; ENSBTAG00000007153.
DR GeneID; 534961; -.
DR KEGG; bta:534961; -.
DR CTD; 712; -.
DR VEuPathDB; HostDB:ENSBTAG00000007153; -.
DR VGNC; VGNC:26616; C1QA.
DR eggNOG; ENOG502RZM2; Eukaryota.
DR GeneTree; ENSGT00940000162143; -.
DR HOGENOM; CLU_001074_0_2_1; -.
DR InParanoid; Q5E9E3; -.
DR OMA; DMVITNQ; -.
DR OrthoDB; 1258047at2759; -.
DR TreeFam; TF329591; -.
DR Reactome; R-BTA-166663; Initial triggering of complement.
DR Reactome; R-BTA-173623; Classical antibody-mediated complement activation.
DR Reactome; R-BTA-977606; Regulation of Complement cascade.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000007153; Expressed in lung and 107 other tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062167; C:complement component C1q complex; IEA:Ensembl.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0048143; P:astrocyte activation; IEA:Ensembl.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0150062; P:complement-mediated synapse pruning; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
DR GO; GO:0016322; P:neuron remodeling; IEA:Ensembl.
DR GO; GO:1901216; P:positive regulation of neuron death; IEA:Ensembl.
DR GO; GO:0150064; P:vertebrate eye-specific patterning; IEA:Ensembl.
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 2: Evidence at transcript 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:0000255"
FT CHAIN 23..244
FT /note="Complement C1q subcomponent subunit A"
FT /id="PRO_0000003516"
FT DOMAIN 31..109
FT /note="Collagen-like"
FT DOMAIN 110..244
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 28..94
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 57
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 73
FT /note="4-hydroxyproline"
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-26 in B chain)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 244 AA; 25802 MW; C7D5B699E501D00D CRC64;
MEAPRGWLVI SVLAISLASS VTEDVCRAPD GTHGSAGIPG RPGRPGLKGE RGEPGAPAIQ
TGIRGLKGDQ GDPGPPGNPG RMGYPGPSGP MGPAGLPGLK GTKGSPGNIK DQPRPAFSAV
GPNSVSRDNV VVFGKVITNQ ENVYQNNTGR FRCSVPGYYY FTFQVVSNWD ICLSIRSSRR
DQIQPLGFCD FNSKGFFQVV SGGTVLHLQQ GDQVWIEKDP SKGRIYHGSE ADSIFSGFLI
FPSA
