C1QB_RAT
ID C1QB_RAT Reviewed; 253 AA.
AC P31721;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Complement C1q subcomponent subunit B;
DE Flags: Precursor;
GN Name=C1qb;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Spleen;
RX PubMed=7594503;
RA Schwaeble W., Schaefer M.K.-H., Petry F., Fink T., Knebel D., Weihe E.,
RA Loos M.;
RT "Follicular dendritic cells, interdigitating cells, and cells of the
RT monocyte-macrophage lineage are the C1q-producing sources in the spleen.
RT Identification of specific cell types by in situ hybridization and
RT immunohistochemical analysis.";
RL J. Immunol. 155:4971-4978(1995).
RN [2]
RP PROTEIN SEQUENCE OF 71-79 AND 141-146.
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 -!- TISSUE SPECIFICITY: Highest levels in spleen, lung and brain. Weaker
CC expression in kidney and liver. In the spleen, localized mainly to the
CC red pulp, in cells mainly of monocyte-macrophage lineage. In white
CC pulp, localized in specific dendritic cells such as those from the
CC periarteriolar lymphatic sheath (PALS). {ECO:0000269|PubMed:7594503}.
CC -!- PTM: Hydroxylated on lysine and proline residues. Hydroxylated lysine
CC residues can be glycosylated.
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DR EMBL; X71127; CAA50440.1; -; mRNA.
DR PIR; S49158; S49158.
DR RefSeq; NP_062135.1; NM_019262.1.
DR AlphaFoldDB; P31721; -.
DR SMR; P31721; -.
DR BioGRID; 248307; 2.
DR IntAct; P31721; 1.
DR MINT; P31721; -.
DR STRING; 10116.ENSRNOP00000017060; -.
DR iPTMnet; P31721; -.
DR PhosphoSitePlus; P31721; -.
DR PaxDb; P31721; -.
DR PRIDE; P31721; -.
DR GeneID; 29687; -.
DR KEGG; rno:29687; -.
DR CTD; 713; -.
DR RGD; 2229; C1qb.
DR eggNOG; ENOG502RYR2; Eukaryota.
DR InParanoid; P31721; -.
DR OrthoDB; 1258047at2759; -.
DR PhylomeDB; P31721; -.
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:P31721; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005602; C:complement component C1 complex; IDA:RGD.
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:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0006958; P:complement activation, classical pathway; ISO:RGD.
DR GO; GO:0006955; P:immune response; TAS:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0048839; P:inner ear development; ISO:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP: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; 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; 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 Glycoprotein; Hydroxylation; Immunity; Innate immunity;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..253
FT /note="Complement C1q subcomponent subunit B"
FT /id="PRO_0000003523"
FT DOMAIN 29..112
FT /note="Collagen-like"
FT DOMAIN 115..253
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 29..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P02746"
FT MOD_RES 33
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
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 51
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 54
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 57
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 60
FT /note="5-hydroxylysine"
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 84
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 90
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 96
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 99
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 102
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 108
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT DISULFID 29
FT /note="Interchain (with C-26 in chain A)"
SQ SEQUENCE 253 AA; 26589 MW; 1CB40622571BFC9B CRC64;
MKTQWSEILT PLLLLLLGLL HVSWAQSSCT GSPGIPGVPG IPGVPGSDGK PGTPGIKGEK
GLPGLAGDHG ELGEKGDAGI PGIPGKVGPK GPVGPKGAPG PPGPRGPKGG SGDYKATQKV
AFSALRTVNS ALRPNQAIRF EKVITNVNDN YEPRSGKFTC KVPGLYYFTY HASSRGNLCV
NIVRGRDRDR MQKVLTFCDY AQNTFQVTTG GVVLKLEQEE VVHLQATDKN SLLGVEGANS
IFTGFLLFPD MDV
