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Protein

Complement C1q subcomponent subunit A

Gene

C1QA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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

Keywordsi

Biological processComplement pathway, Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiR-BTA-166663. Initial triggering of complement.
R-BTA-173623. Classical antibody-mediated complement activation.
R-BTA-977606. Regulation of Complement cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement C1q subcomponent subunit A
Gene namesi
Name:C1QA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000000351623 – 244Complement C1q subcomponent subunit AAdd BLAST222

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi26Interchain (with C-26 in B chain)By similarity
Modified residuei394-hydroxyprolineBy similarity1
Modified residuei454-hydroxyprolineBy similarity1
Modified residuei485-hydroxylysineBy similarity1
Glycosylationi48O-linked (Gal...) hydroxylysineBy similarity1
Modified residuei544-hydroxyprolineBy similarity1
Modified residuei574-hydroxyprolineBy similarity1
Modified residuei675-hydroxylysineBy similarity1
Glycosylationi67O-linked (Gal...) hydroxylysineBy similarity1
Modified residuei734-hydroxyprolineBy similarity1
Modified residuei794-hydroxyprolineBy similarity1
Modified residuei854-hydroxyprolineBy similarity1
Modified residuei1005-hydroxylysineBy similarity1
Glycosylationi100O-linked (Gal...) hydroxylysineBy similarity1
Glycosylationi146N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

O-linked glycans are Glc-Gal disaccharides typically found as secondary modifications of hydroxylated lysines in collagen-like domains.By similarity
Proline residues in the collagen-like domain motif, GXPG, are typically 4-hydroxylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiQ5E9E3.
PRIDEiQ5E9E3.

Expressioni

Gene expression databases

BgeeiENSBTAG00000007153.

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.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009415.

Structurei

3D structure databases

ProteinModelPortaliQ5E9E3.
SMRiQ5E9E3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 109Collagen-likeAdd BLAST79
Domaini110 – 244C1qPROSITE-ProRule annotationAdd BLAST135

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IK45. Eukaryota.
ENOG410YJJD. LUCA.
GeneTreeiENSGT00760000118830.
HOGENOMiHOG000085653.
HOVERGENiHBG108220.
InParanoidiQ5E9E3.
KOiK03986.
OMAiYYYFTFQ.
OrthoDBiEOG091G0L3Y.
TreeFamiTF329591.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiView protein in InterPro
IPR001073. C1q_dom.
IPR008160. Collagen.
IPR008983. Tumour_necrosis_fac-like_dom.
PfamiView protein in Pfam
PF00386. C1q. 1 hit.
PF01391. Collagen. 1 hit.
PRINTSiPR00007. COMPLEMNTC1Q.
SMARTiView protein in SMART
SM00110. C1Q. 1 hit.
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiView protein in PROSITE
PS50871. C1Q. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5E9E3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAPRGWLVI SVLAISLASS VTEDVCRAPD GTHGSAGIPG RPGRPGLKGE
60 70 80 90 100
RGEPGAPAIQ TGIRGLKGDQ GDPGPPGNPG RMGYPGPSGP MGPAGLPGLK
110 120 130 140 150
GTKGSPGNIK DQPRPAFSAV GPNSVSRDNV VVFGKVITNQ ENVYQNNTGR
160 170 180 190 200
FRCSVPGYYY FTFQVVSNWD ICLSIRSSRR DQIQPLGFCD FNSKGFFQVV
210 220 230 240
SGGTVLHLQQ GDQVWIEKDP SKGRIYHGSE ADSIFSGFLI FPSA
Length:244
Mass (Da):25,802
Last modified:March 15, 2005 - v1
Checksum:iC7D5B699E501D00D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020977 mRNA. Translation: AAX08994.1.
AY911382 mRNA. Translation: AAW82145.1.
BC105345 mRNA. Translation: AAI05346.1.
RefSeqiNP_001014945.1. NM_001014945.2.
XP_005203271.1. XM_005203214.3.
UniGeneiBt.1577.

Genome annotation databases

EnsembliENSBTAT00000009415; ENSBTAP00000009415; ENSBTAG00000007153.
ENSBTAT00000040146; ENSBTAP00000039925; ENSBTAG00000007153.
GeneIDi534961.
KEGGibta:534961.

Similar proteinsi

Entry informationi

Entry nameiC1QA_BOVIN
AccessioniPrimary (citable) accession number: Q5E9E3
Secondary accession number(s): Q56JV0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 15, 2005
Last modified: August 30, 2017
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome