C1QA_PIG
ID C1QA_PIG Reviewed; 247 AA.
AC Q69DL0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Complement C1q subcomponent subunit A;
DE Flags: Precursor;
GN Name=C1QA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Trakooljul N., Ponsuksili S., Schellander K., Wimmers K.;
RT "Molecular analysis of soluble porcine complement component genes.";
RL Submitted (JUL-2003) 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; AY349424; AAR20892.1; -; mRNA.
DR RefSeq; NP_001003924.1; NM_001003924.1.
DR AlphaFoldDB; Q69DL0; -.
DR SMR; Q69DL0; -.
DR STRING; 9823.ENSSSCP00000003825; -.
DR PaxDb; Q69DL0; -.
DR PeptideAtlas; Q69DL0; -.
DR PRIDE; Q69DL0; -.
DR GeneID; 445461; -.
DR KEGG; ssc:445461; -.
DR CTD; 712; -.
DR eggNOG; ENOG502RZM2; Eukaryota.
DR InParanoid; Q69DL0; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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..24
FT /evidence="ECO:0000250"
FT CHAIN 25..247
FT /note="Complement C1q subcomponent subunit A"
FT /id="PRO_0000003519"
FT DOMAIN 33..111
FT /note="Collagen-like"
FT DOMAIN 112..247
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 26..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT MOD_RES 47
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT MOD_RES 50
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT MOD_RES 56
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT MOD_RES 59
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT MOD_RES 69
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT MOD_RES 81
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT MOD_RES 87
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT MOD_RES 102
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT CARBOHYD 50
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT CARBOHYD 69
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT CARBOHYD 102
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02745"
FT DISULFID 28
FT /note="Interchain (with C-29 in B chain)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 247 AA; 26483 MW; 16C79FB295955709 CRC64;
MEAPRGWLVI MISVLAVSLA SSAAQDTCRD LDGRDGAARK PGRPGRPGPK GERGEPGAPA
FQTGIRGLKG DQGESGSPGK PGRMGYPGPS GPPGLPGLPG LKGIKGNPGN IKDQRRPAFS
AVRQNPPTSG NVVIFDEVIT NQEGAYKSQL GQFICDVPGY YYFTFQVVSK WDLCLYIMSS
RRDQVQQSLG FCDFNSKGLF QVVSGGTVLQ LQRGDKVWIQ RDPNKGRIYQ GSEADSVFSG
FLIFPST
