C1QB_BOVIN
ID C1QB_BOVIN Reviewed; 247 AA.
AC Q2KIV9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Complement C1q subcomponent subunit B;
DE Flags: Precursor;
GN Name=C1QB;
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].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP GLYCOSYLATION ON HYDROXYLYSINES.
RX PubMed=6286235; DOI=10.1016/s0174-173x(81)80015-5;
RA Yonemasu K., Shinkai H., Sasaki T.;
RT "Comparable content of hydroxylysine-linked glycosides in subcomponents C1q
RT of the first component of human, bovine and mouse complement.";
RL Coll. Relat. Res. 1:385-390(1981).
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 (By similarity).
CC {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: Hydroxylated on lysine and proline residues. Hydroxylated lysine
CC residues can be glycosylated. Bovine C1Q contains up to 66.3
CC hydroxylysine-galactosylglucose residues. Total percentage
CC hydroxylysine residues glycosylated is 92.0%. Contains no
CC hydroxylysine-monosaccharides. {ECO:0000269|PubMed:6286235}.
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DR EMBL; BC112490; AAI12491.1; -; mRNA.
DR RefSeq; NP_001040064.1; NM_001046599.2.
DR RefSeq; XP_010800915.1; XM_010802613.1.
DR AlphaFoldDB; Q2KIV9; -.
DR SMR; Q2KIV9; -.
DR BioGRID; 545030; 1.
DR STRING; 9913.ENSBTAP00000014871; -.
DR PaxDb; Q2KIV9; -.
DR PRIDE; Q2KIV9; -.
DR Ensembl; ENSBTAT00000014871; ENSBTAP00000014871; ENSBTAG00000011196.
DR GeneID; 617435; -.
DR KEGG; bta:617435; -.
DR CTD; 713; -.
DR VEuPathDB; HostDB:ENSBTAG00000011196; -.
DR VGNC; VGNC:26617; C1QB.
DR eggNOG; ENOG502RYR2; Eukaryota.
DR GeneTree; ENSGT00940000161091; -.
DR HOGENOM; CLU_001074_0_2_1; -.
DR InParanoid; Q2KIV9; -.
DR OMA; VYNTFQV; -.
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; ENSBTAG00000011196; Expressed in lung and 107 other tissues.
DR ExpressionAtlas; Q2KIV9; baseline and differential.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0048839; P:inner ear development; IEA:Ensembl.
DR GO; GO:0098883; P:synapse pruning; IEA:Ensembl.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR037573; Complement_C1qB.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR PANTHER; PTHR15427:SF18; PTHR15427:SF18; 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; Pyrrolidone carboxylic acid; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..247
FT /note="Complement C1q subcomponent subunit B"
FT /id="PRO_0000286135"
FT DOMAIN 39..98
FT /note="Collagen-like"
FT DOMAIN 111..247
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 30..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P02746"
FT MOD_RES 29
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 32
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 35
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 47
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 50
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 53
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 56
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 59
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 71
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 77
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 80
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 86
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 92
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 95
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 98
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 104
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT DISULFID 26
FT /note="Interchain (with C-26 in chain A)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 247 AA; 26399 MW; 4C2CDCFF75A433B0 CRC64;
MKTPRGSVLV LLLLNLLRVS WAQSNCIRPS IPGIPGIPGK PGSDGKPGTP GTKGEKGLPG
LVSHLNENGE KGDPGFPGMP GKVGPKGPIG PKGVPGPPGV RGPKGESGDY KATQKIAFSA
SRTINHHQRQ GQPIRFDHVI TNANENYQAR SSKFTCKVPG LYFFTYHASS RGQLCVDLMR
GRAEPQKVVT FCDYVQNTFQ VTTGSIVLKL EKDETVFLQA TEKNALVGIE GANSIFSGFM
LFPDTEA
