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Complement C1q subcomponent subunit B

 C1QB_RAT                Reviewed;         253 AA.
P31721;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
23-MAY-2018, entry version 126.
RecName: Full=Complement C1q subcomponent subunit B;
Flags: Precursor;
Name=C1qb;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Spleen;
PubMed=7594503;
Schwaeble W., Schaefer M.K.-H., Petry F., Fink T., Knebel D.,
Weihe E., Loos M.;
"Follicular dendritic cells, interdigitating cells, and cells of the
monocyte-macrophage lineage are the C1q-producing sources in the
spleen. Identification of specific cell types by in situ hybridization
and immunohistochemical analysis.";
J. Immunol. 155:4971-4978(1995).
[2]
PROTEIN SEQUENCE OF 71-79 AND 141-146.
PubMed=8464426; DOI=10.1016/0161-5890(93)90111-N;
Wing M.G., Seilly D.J., Bridgman D.J., Harrison R.A.;
"Rapid isolation and biochemical characterization of rat C1 and C1q.";
Mol. Immunol. 30:433-440(1993).
-!- FUNCTION: C1q associates with the proenzymes C1r and C1s to yield
C1, the first component of the serum complement system. The
collagen-like regions of C1q interact with the Ca(2+)-dependent
C1r(2)C1s(2) proenzyme complex, and efficient activation of C1
takes place on interaction of the globular heads of C1q with the
Fc regions of IgG or IgM antibody present in immune complexes.
-!- SUBUNIT: C1 is a calcium-dependent trimolecular complex of C1q,
C1r and C1s in the molar ration of 1:2:2. C1q subcomponent is
composed of nine subunits, six of which are disulfide-linked
dimers of the a and B chains, and three of which are disulfide-
linked dimers of the C chain. In addition to the major A:B and C:C
dimer bands, rat, unlike human C1q, contained minor dimer species.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Highest levels in spleen, lung and brain.
Weaker expression in kidney and liver. In the spleen, localized
mainly to the red pulp, in cells mainly of monocyte-macrophage
lineage. In white pulp, localized in specific dendritic cells such
as those from the periarteriolar lymphatic sheath (PALS).
{ECO:0000269|PubMed:7594503}.
-!- PTM: Hydroxylated on lysine and proline residues. Hydroxylated
lysine residues can be glycosylated.
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EMBL; X71127; CAA50440.1; -; mRNA.
PIR; S49158; S49158.
RefSeq; NP_062135.1; NM_019262.1.
UniGene; Rn.6702; -.
ProteinModelPortal; P31721; -.
SMR; P31721; -.
BioGrid; 248307; 1.
STRING; 10116.ENSRNOP00000017060; -.
iPTMnet; P31721; -.
PhosphoSitePlus; P31721; -.
PaxDb; P31721; -.
PRIDE; P31721; -.
GeneID; 29687; -.
KEGG; rno:29687; -.
CTD; 713; -.
RGD; 2229; C1qb.
eggNOG; ENOG410IWVM; Eukaryota.
eggNOG; ENOG4111MQB; LUCA.
HOGENOM; HOG000085653; -.
HOVERGEN; HBG108220; -.
InParanoid; P31721; -.
KO; K03987; -.
PhylomeDB; P31721; -.
PRO; PR:P31721; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
GO; GO:0005602; C:complement component C1 complex; IDA:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0006955; P:immune response; TAS:RGD.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
Gene3D; 2.60.120.40; -; 1.
InterPro; IPR001073; C1q_dom.
InterPro; IPR008160; Collagen.
InterPro; IPR037573; Complement_C1qB.
InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
PANTHER; PTHR44403:SF2; PTHR44403:SF2; 1.
Pfam; PF00386; C1q; 1.
Pfam; PF01391; Collagen; 2.
PRINTS; PR00007; COMPLEMNTC1Q.
SMART; SM00110; C1Q; 1.
SUPFAM; SSF49842; SSF49842; 1.
PROSITE; PS50871; C1Q; 1.
1: Evidence at protein level;
Collagen; Complement pathway; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Hydroxylation; Immunity; Innate immunity; Pyrrolidone carboxylic acid;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 25 {ECO:0000250}.
CHAIN 26 253 Complement C1q subcomponent subunit B.
/FTId=PRO_0000003523.
DOMAIN 29 112 Collagen-like.
DOMAIN 115 253 C1q. {ECO:0000255|PROSITE-
ProRule:PRU00368}.
MOD_RES 26 26 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:P02746}.
MOD_RES 33 33 4-hydroxyproline. {ECO:0000250}.
MOD_RES 36 36 4-hydroxyproline. {ECO:0000250}.
MOD_RES 39 39 4-hydroxyproline. {ECO:0000250}.
MOD_RES 51 51 4-hydroxyproline. {ECO:0000250}.
MOD_RES 54 54 4-hydroxyproline. {ECO:0000250}.
MOD_RES 57 57 5-hydroxylysine. {ECO:0000250}.
MOD_RES 60 60 5-hydroxylysine. {ECO:0000250}.
MOD_RES 63 63 4-hydroxyproline. {ECO:0000250}.
MOD_RES 75 75 5-hydroxylysine. {ECO:0000250}.
MOD_RES 81 81 4-hydroxyproline. {ECO:0000250}.
MOD_RES 84 84 4-hydroxyproline. {ECO:0000250}.
MOD_RES 90 90 5-hydroxylysine. {ECO:0000250}.
MOD_RES 96 96 5-hydroxylysine. {ECO:0000250}.
MOD_RES 99 99 4-hydroxyproline. {ECO:0000250}.
MOD_RES 102 102 4-hydroxyproline. {ECO:0000250}.
MOD_RES 108 108 5-hydroxylysine. {ECO:0000250}.
DISULFID 29 29 Interchain (with C-26 in chain A).
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


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