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Protein

Complement C1q subcomponent subunit A

Gene

C1qa

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 - Biological processi

  • complement activation, classical pathway Source: MGI
  • innate immune response Source: UniProtKB-KW
  • response to iron ion Source: Ensembl
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 A
Gene namesi
Name:C1qa
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:88223. C1qa.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222By similarityAdd
BLAST
Chaini23 – 245223Complement C1q subcomponent subunit APRO_0000003518Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 – 26Interchain (with C-29 in B chain)By similarity
Modified residuei39 – 3914-hydroxyprolineBy similarity
Modified residuei45 – 4514-hydroxyprolineBy similarity
Modified residuei48 – 4815-hydroxylysine; alternateBy similarity
Glycosylationi48 – 481O-linked (Gal...); alternateBy similarity
Modified residuei54 – 5414-hydroxyprolineBy similarity
Modified residuei67 – 6715-hydroxylysine; alternateBy similarity
Glycosylationi67 – 671O-linked (Gal...); alternateBy similarity
Modified residuei79 – 7914-hydroxyprolineBy similarity
Modified residuei85 – 8514-hydroxyprolineBy similarity
Modified residuei100 – 10015-hydroxylysine; alternateBy similarity
Glycosylationi100 – 1001O-linked (Gal...); alternateBy similarity
Glycosylationi146 – 1461N-linked (GlcNAc...)1 Publication

Post-translational modificationi

O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.By similarity
Hydroxylation on proline residues within the sequence motif, GXPG, is most likely 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP98086.
PRIDEiP98086.

PTM databases

PhosphoSiteiP98086.

Expressioni

Gene expression databases

GenevisibleiP98086. 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.

Binary interactionsi

WithEntry#Exp.IntActNotes
FZD8Q9H4613EBI-299840,EBI-6254212From a different organism.

Protein-protein interaction databases

BioGridi198412. 1 interaction.
IntActiP98086. 6 interactions.
STRINGi10090.ENSMUSP00000048836.

Structurei

3D structure databases

ProteinModelPortaliP98086.
SMRiP98086. Positions 67-92, 112-244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 10979Collagen-likeAdd
BLAST
Domaini110 – 245136C1qPROSITE-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

eggNOGiENOG410IK45. Eukaryota.
ENOG410YJJD. LUCA.
GeneTreeiENSGT00760000118830.
HOGENOMiHOG000085653.
HOVERGENiHBG108220.
InParanoidiP98086.
KOiK03986.
OMAiYYYFTFQ.
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. 1 hit.
[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.

P98086-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METSQGWLVA CVLTMTLVWT VAEDVCRAPN GKDGAPGNPG RPGRPGLKGE
60 70 80 90 100
RGEPGAAGIR TGIRGFKGDP GESGPPGKPG NVGLPGPSGP LGDSGPQGLK
110 120 130 140 150
GVKGNPGNIR DQPRPAFSAI RQNPMTLGNV VIFDKVLTNQ ESPYQNHTGR
160 170 180 190 200
FICAVPGFYY FNFQVISKWD LCLFIKSSSG GQPRDSLSFS NTNNKGLFQV
210 220 230 240
LAGGTVLQLR RGDEVWIEKD PAKGRIYQGT EADSIFSGFL IFPSA
Length:245
Mass (Da):25,974
Last modified:October 3, 2012 - v2
Checksum:i41C2066D49592020
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161T → I in CAA41664 (PubMed:1940381).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58861 mRNA. Translation: CAA41664.1.
AK002655 mRNA. Translation: BAB22262.1.
AK136737 mRNA. Translation: BAE23115.1.
AK159210 mRNA. Translation: BAE34901.1.
AL627214 Genomic DNA. Translation: CAM46146.1.
CH466552 Genomic DNA. Translation: EDL29926.1.
BC002086 mRNA. Translation: AAH02086.1.
CCDSiCCDS18812.1.
PIRiS19018.
RefSeqiNP_031598.2. NM_007572.2.
UniGeneiMm.439957.

Genome annotation databases

EnsembliENSMUST00000046285; ENSMUSP00000048836; ENSMUSG00000036887.
GeneIDi12259.
KEGGimmu:12259.
UCSCiuc008vir.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58861 mRNA. Translation: CAA41664.1.
AK002655 mRNA. Translation: BAB22262.1.
AK136737 mRNA. Translation: BAE23115.1.
AK159210 mRNA. Translation: BAE34901.1.
AL627214 Genomic DNA. Translation: CAM46146.1.
CH466552 Genomic DNA. Translation: EDL29926.1.
BC002086 mRNA. Translation: AAH02086.1.
CCDSiCCDS18812.1.
PIRiS19018.
RefSeqiNP_031598.2. NM_007572.2.
UniGeneiMm.439957.

3D structure databases

ProteinModelPortaliP98086.
SMRiP98086. Positions 67-92, 112-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198412. 1 interaction.
IntActiP98086. 6 interactions.
STRINGi10090.ENSMUSP00000048836.

PTM databases

PhosphoSiteiP98086.

Proteomic databases

PaxDbiP98086.
PRIDEiP98086.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000046285; ENSMUSP00000048836; ENSMUSG00000036887.
GeneIDi12259.
KEGGimmu:12259.
UCSCiuc008vir.1. mouse.

Organism-specific databases

CTDi712.
MGIiMGI:88223. C1qa.

Phylogenomic databases

eggNOGiENOG410IK45. Eukaryota.
ENOG410YJJD. LUCA.
GeneTreeiENSGT00760000118830.
HOGENOMiHOG000085653.
HOVERGENiHBG108220.
InParanoidiP98086.
KOiK03986.
OMAiYYYFTFQ.
OrthoDBiEOG70ZZPW.
TreeFamiTF329591.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiC1qa. mouse.
NextBioi280690.
PROiP98086.
SOURCEiSearch...

Gene expression databases

GenevisibleiP98086. 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. 1 hit.
[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. "Gene expression of the A- and B-chain of mouse C1q in different tissues and the characterization of the recombinant A-chain."
    Petry F., Reid K.B.M., Loos M.
    J. Immunol. 147:3988-3993(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ICR.
    Tissue: Macrophage.
  2. "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 [MRNA].
    Strain: 129.
    Tissue: Liver.
  3. "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: Epididymis and Kidney.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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: Czech II.
    Tissue: Mammary tumor.
  7. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
    Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
    J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-146.
    Strain: C57BL/6J.
    Tissue: Plasma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue and Spleen.

Entry informationi

Entry nameiC1QA_MOUSE
AccessioniPrimary (citable) accession number: P98086
Secondary accession number(s): Q9DCM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 3, 2012
Last modified: February 17, 2016
This is version 125 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.