C1QB_MOUSE
ID C1QB_MOUSE Reviewed; 253 AA.
AC P14106; Q3U793;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Complement C1q subcomponent subunit B;
DE Flags: Precursor;
GN Name=C1qb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=ICR; TISSUE=Macrophage;
RX PubMed=2591537; DOI=10.1016/0014-5793(89)81622-9;
RA Petry F., Reid K.B.M., Loos M.;
RT "Molecular cloning and characterization of the complementary DNA coding for
RT the B-chain of murine Clq.";
RL FEBS Lett. 258:89-93(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3258283; DOI=10.1016/0165-2478(88)90102-2;
RA Wood L., Pulaski S., Vogeli G.;
RT "cDNA clones coding for the complete murine B chain of complement Clq:
RT nucleotide and derived amino acid sequences.";
RL Immunol. Lett. 17:59-62(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8606057; DOI=10.1007/bf02199805;
RA Petry F., McClive P.J., Botto M., Morley B.J., Morahan G., Loos M.;
RT "The mouse C1q genes are clustered on chromosome 4 and show conservation of
RT gene organization.";
RL Immunogenetics 43:370-376(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
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).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Highest expression in thioglycolate-activated
CC peritoneal macrophages. Also found in spleen, thymus and heart. Very
CC weak expression liver, kidney, lung and intestine.
CC {ECO:0000269|PubMed:2591537}.
CC -!- PTM: Hydroxylated on lysine and proline residues. Hydroxylated lysine
CC residues can be glycosylated. Mouse C1Q contains up to 64.0
CC hydroxylysine-galactosylglucose residues. Total percentage
CC hydroxylysine residues glycosylated is 95.1%. Contains no
CC hydroxylysine-monosaccharides. {ECO:0000269|PubMed:6286235}.
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DR EMBL; X16874; CAA34757.1; -; mRNA.
DR EMBL; M36293; AAA37283.1; -; mRNA.
DR EMBL; M22531; AAA37335.1; -; mRNA.
DR EMBL; X92959; CAA63534.1; -; Genomic_DNA.
DR EMBL; AK152764; BAE31477.1; -; mRNA.
DR EMBL; AL627214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067001; AAH67001.1; -; mRNA.
DR CCDS; CCDS18810.1; -.
DR PIR; I49560; I49560.
DR RefSeq; NP_033907.1; NM_009777.2.
DR AlphaFoldDB; P14106; -.
DR SMR; P14106; -.
DR BioGRID; 198413; 6.
DR ComplexPortal; CPX-4981; Complement component C1q complex.
DR IntAct; P14106; 2.
DR MINT; P14106; -.
DR STRING; 10090.ENSMUSP00000040246; -.
DR PhosphoSitePlus; P14106; -.
DR SwissPalm; P14106; -.
DR CPTAC; non-CPTAC-5579; -.
DR PaxDb; P14106; -.
DR PeptideAtlas; P14106; -.
DR PRIDE; P14106; -.
DR ProteomicsDB; 265398; -.
DR Antibodypedia; 30104; 280 antibodies from 30 providers.
DR DNASU; 12260; -.
DR Ensembl; ENSMUST00000046384; ENSMUSP00000040246; ENSMUSG00000036905.
DR GeneID; 12260; -.
DR KEGG; mmu:12260; -.
DR UCSC; uc008vip.2; mouse.
DR CTD; 713; -.
DR MGI; MGI:88224; C1qb.
DR VEuPathDB; HostDB:ENSMUSG00000036905; -.
DR eggNOG; ENOG502RYR2; Eukaryota.
DR GeneTree; ENSGT00940000161091; -.
DR HOGENOM; CLU_001074_0_2_1; -.
DR InParanoid; P14106; -.
DR OMA; VYNTFQV; -.
DR OrthoDB; 1258047at2759; -.
DR PhylomeDB; P14106; -.
DR TreeFam; TF329591; -.
DR Reactome; R-MMU-166663; Initial triggering of complement.
DR Reactome; R-MMU-173623; Classical antibody-mediated complement activation.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 12260; 2 hits in 74 CRISPR screens.
DR ChiTaRS; C1qb; mouse.
DR PRO; PR:P14106; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P14106; protein.
DR Bgee; ENSMUSG00000036905; Expressed in stroma of bone marrow and 254 other tissues.
DR Genevisible; P14106; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005602; C:complement component C1 complex; ISO:MGI.
DR GO; GO:0062167; C:complement component C1q complex; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0098794; C:postsynapse; IGI:ARUK-UCL.
DR GO; GO:0045202; C:synapse; IDA:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0006958; P:complement activation, classical pathway; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0048839; P:inner ear development; IDA:MGI.
DR GO; GO:0098883; P:synapse pruning; IGI:ARUK-UCL.
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; Disulfide bond; Glycoprotein; Hydroxylation;
KW Immunity; Innate immunity; Pyrrolidone carboxylic acid; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT CHAIN 26..253
FT /note="Complement C1q subcomponent subunit B"
FT /id="PRO_0000003522"
FT DOMAIN 29..112
FT /note="Collagen-like"
FT DOMAIN 115..253
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 35..115
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 108
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT DISULFID 29
FT /note="Interchain (with C-26 in chain A)"
FT /evidence="ECO:0000250"
FT CONFLICT 115
FT /note="G -> R (in Ref. 1; CAA34757)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 253 AA; 26717 MW; 0F5C33EA2DE2E253 CRC64;
MKTQWGEVWT HLLLLLLGFL HVSWAQSSCT GPPGIPGIPG VPGVPGSDGQ PGTPGIKGEK
GLPGLAGDLG EFGEKGDPGI PGTPGKVGPK GPVGPKGTPG PSGPRGPKGD SGDYGATQKV
AFSALRTINS PLRPNQVIRF EKVITNANEN YEPRNGKFTC KVPGLYYFTY HASSRGNLCV
NLVRGRDRDS MQKVVTFCDY AQNTFQVTTG GVVLKLEQEE VVHLQATDKN SLLGIEGANS
IFTGFLLFPD MDA
