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Protein

Complement C1q subcomponent subunit B

Gene

C1qb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 Ca2+-dependent C1r2C1s2 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.

GO - Molecular functioni

  • protein homodimerization activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Complement pathway, Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiR-MMU-166663. Initial triggering of complement.
R-MMU-173623. Classical antibody-mediated complement activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement C1q subcomponent subunit B
Gene namesi
Name:C1qb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:88224. C1qb.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Add
BLAST
Chaini26 – 253228Complement C1q subcomponent subunit BPRO_0000003522Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261Pyrrolidone carboxylic acidBy similarity
Disulfide bondi29 – 29Interchain (with C-26 in chain A)By similarity
Modified residuei33 – 3314-hydroxyprolineBy similarity
Modified residuei36 – 3614-hydroxyprolineBy similarity
Modified residuei39 – 3914-hydroxyprolineBy similarity
Modified residuei51 – 5114-hydroxyprolineBy similarity
Modified residuei54 – 5414-hydroxyprolineBy similarity
Modified residuei57 – 5715-hydroxylysineBy similarity
Modified residuei60 – 6015-hydroxylysineBy similarity
Modified residuei63 – 6314-hydroxyprolineBy similarity
Modified residuei75 – 7515-hydroxylysineBy similarity
Modified residuei81 – 8114-hydroxyprolineBy similarity
Modified residuei84 – 8414-hydroxyprolineBy similarity
Modified residuei90 – 9015-hydroxylysineBy similarity
Modified residuei96 – 9615-hydroxylysineBy similarity
Modified residuei99 – 9914-hydroxyprolineBy similarity
Modified residuei108 – 10815-hydroxylysineBy similarity

Post-translational modificationi

Hydroxylated on lysine and proline residues. Hydroxylated lysine residues can be glycosylated. Mouse C1Q contains up to 64.0 hydroxylysine-galactosylglucose residues. Total percentage hydroxylysine residues glycosylated is 95.1%. Contains no hydroxylysine-monosaccharides.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Pyrrolidone carboxylic acid

Proteomic databases

EPDiP14106.
PaxDbiP14106.
PRIDEiP14106.

PTM databases

PhosphoSiteiP14106.
SwissPalmiP14106.

Expressioni

Tissue specificityi

Highest expression in thioglycolate-activated peritoneal macrophages. Also found in spleen, thymus and heart. Very weak expression liver, kidney, lung and intestine.1 Publication

Gene expression databases

GenevisibleiP14106. MM.

Interactioni

Subunit structurei

C1 is a calcium-dependent trimolecular complex of C1q, R and S 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.

GO - Molecular functioni

  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

IntActiP14106. 1 interaction.
STRINGi10090.ENSMUSP00000040246.

Structurei

3D structure databases

ProteinModelPortaliP14106.
SMRiP14106. Positions 117-250.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 11284Collagen-likeAdd
BLAST
Domaini115 – 253139C1qPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 C1q domain.PROSITE-ProRule annotation
Contains 1 collagen-like domain.Curated

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IWVM. Eukaryota.
ENOG4111MQB. LUCA.
GeneTreeiENSGT00760000118830.
HOGENOMiHOG000085653.
HOVERGENiHBG108220.
InParanoidiP14106.
KOiK03987.
OMAiFFTYHAS.
OrthoDBiEOG70ZZPW.
TreeFamiTF329591.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR001073. C1q_dom.
IPR008160. Collagen.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00386. C1q. 1 hit.
PF01391. Collagen. 2 hits.
[Graphical view]
PRINTSiPR00007. COMPLEMNTC1Q.
SMARTiSM00110. C1Q. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50871. C1Q. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14106-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTQWGEVWT HLLLLLLGFL HVSWAQSSCT GPPGIPGIPG VPGVPGSDGQ
60 70 80 90 100
PGTPGIKGEK GLPGLAGDLG EFGEKGDPGI PGTPGKVGPK GPVGPKGTPG
110 120 130 140 150
PSGPRGPKGD SGDYGATQKV AFSALRTINS PLRPNQVIRF EKVITNANEN
160 170 180 190 200
YEPRNGKFTC KVPGLYYFTY HASSRGNLCV NLVRGRDRDS MQKVVTFCDY
210 220 230 240 250
AQNTFQVTTG GVVLKLEQEE VVHLQATDKN SLLGIEGANS IFTGFLLFPD

MDA
Length:253
Mass (Da):26,717
Last modified:October 3, 2012 - v2
Checksum:i0F5C33EA2DE2E253
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151G → R in CAA34757 (PubMed:2591537).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16874 mRNA. Translation: CAA34757.1.
M36293 mRNA. Translation: AAA37283.1.
M22531 mRNA. Translation: AAA37335.1.
X92959 Genomic DNA. Translation: CAA63534.1.
AK152764 mRNA. Translation: BAE31477.1.
AL627214 Genomic DNA. Translation: CAM46144.1.
BC067001 mRNA. Translation: AAH67001.1.
CCDSiCCDS18810.1.
PIRiI49560.
RefSeqiNP_033907.1. NM_009777.2.
UniGeneiMm.2570.

Genome annotation databases

EnsembliENSMUST00000046384; ENSMUSP00000040246; ENSMUSG00000036905.
GeneIDi12260.
KEGGimmu:12260.
UCSCiuc008vip.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16874 mRNA. Translation: CAA34757.1.
M36293 mRNA. Translation: AAA37283.1.
M22531 mRNA. Translation: AAA37335.1.
X92959 Genomic DNA. Translation: CAA63534.1.
AK152764 mRNA. Translation: BAE31477.1.
AL627214 Genomic DNA. Translation: CAM46144.1.
BC067001 mRNA. Translation: AAH67001.1.
CCDSiCCDS18810.1.
PIRiI49560.
RefSeqiNP_033907.1. NM_009777.2.
UniGeneiMm.2570.

3D structure databases

ProteinModelPortaliP14106.
SMRiP14106. Positions 117-250.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP14106. 1 interaction.
STRINGi10090.ENSMUSP00000040246.

PTM databases

PhosphoSiteiP14106.
SwissPalmiP14106.

Proteomic databases

EPDiP14106.
PaxDbiP14106.
PRIDEiP14106.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000046384; ENSMUSP00000040246; ENSMUSG00000036905.
GeneIDi12260.
KEGGimmu:12260.
UCSCiuc008vip.2. mouse.

Organism-specific databases

CTDi713.
MGIiMGI:88224. C1qb.

Phylogenomic databases

eggNOGiENOG410IWVM. Eukaryota.
ENOG4111MQB. LUCA.
GeneTreeiENSGT00760000118830.
HOGENOMiHOG000085653.
HOVERGENiHBG108220.
InParanoidiP14106.
KOiK03987.
OMAiFFTYHAS.
OrthoDBiEOG70ZZPW.
TreeFamiTF329591.

Enzyme and pathway databases

ReactomeiR-MMU-166663. Initial triggering of complement.
R-MMU-173623. Classical antibody-mediated complement activation.

Miscellaneous databases

PROiP14106.
SOURCEiSearch...

Gene expression databases

GenevisibleiP14106. MM.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR001073. C1q_dom.
IPR008160. Collagen.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00386. C1q. 1 hit.
PF01391. Collagen. 2 hits.
[Graphical view]
PRINTSiPR00007. COMPLEMNTC1Q.
SMARTiSM00110. C1Q. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50871. C1Q. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of the complementary DNA coding for the B-chain of murine Clq."
    Petry F., Reid K.B.M., Loos M.
    FEBS Lett. 258:89-93(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: ICR.
    Tissue: Macrophage.
  2. "cDNA clones coding for the complete murine B chain of complement Clq: nucleotide and derived amino acid sequences."
    Wood L., Pulaski S., Vogeli G.
    Immunol. Lett. 17:59-62(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The mouse C1q genes are clustered on chromosome 4 and show conservation of gene organization."
    Petry F., McClive P.J., Botto M., Morley B.J., Morahan G., Loos M.
    Immunogenetics 43:370-376(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/cJ.
    Tissue: Liver.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  7. "Comparable content of hydroxylysine-linked glycosides in subcomponents C1q of the first component of human, bovine and mouse complement."
    Yonemasu K., Shinkai H., Sasaki T.
    Coll. Relat. Res. 1:385-390(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION ON HYDROXYLYSINES.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Liver and Spleen.

Entry informationi

Entry nameiC1QB_MOUSE
AccessioniPrimary (citable) accession number: P14106
Secondary accession number(s): Q3U793
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 3, 2012
Last modified: June 8, 2016
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.