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Q5E9E3

- C1QA_BOVIN

UniProt

Q5E9E3 - C1QA_BOVIN

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Protein

Complement C1q subcomponent subunit A

Gene

C1QA

Organism
Bos taurus (Bovine)
Status
Reviewed - 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

  1. complement activation, classical pathway Source: UniProtKB-KW
  2. innate immune response Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Complement pathway, Immunity, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Complement C1q subcomponent subunit A
Gene namesi
Name:C1QA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 2

Subcellular locationi

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 244222Complement C1q subcomponent subunit APRO_0000003516Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 – 26Interchain (with C-26 in B chain)By similarity
Modified residuei39 – 3914-hydroxyprolineBy similarity
Modified residuei45 – 4514-hydroxyprolineBy similarity
Modified residuei48 – 4815-hydroxylysineBy similarity
Glycosylationi48 – 481O-linked (Gal...)By similarity
Modified residuei54 – 5414-hydroxyprolineBy similarity
Modified residuei57 – 5714-hydroxyprolineBy similarity
Modified residuei67 – 6715-hydroxylysineBy similarity
Glycosylationi67 – 671O-linked (Gal...)By similarity
Modified residuei73 – 7314-hydroxyprolineBy similarity
Modified residuei79 – 7914-hydroxyprolineBy similarity
Modified residuei85 – 8514-hydroxyprolineBy similarity
Modified residuei100 – 10015-hydroxylysineBy similarity
Glycosylationi100 – 1001O-linked (Gal...)By similarity
Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PRIDEiQ5E9E3.

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.

Structurei

3D structure databases

ProteinModelPortaliQ5E9E3.
SMRiQ5E9E3. Positions 112-243.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 10979Collagen-likeAdd
BLAST
Domaini110 – 244135C1qPROSITE-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

eggNOGiNOG126311.
GeneTreeiENSGT00760000118830.
HOGENOMiHOG000085653.
HOVERGENiHBG108220.
InParanoidiQ5E9E3.
KOiK03986.
OMAiYYYFTFQ.
OrthoDBiEOG70ZZPW.
TreeFamiTF329591.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR001073. C1q.
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.

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:
EMBL
GenBank
DDBJ
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_005203214.1.
UniGeneiBt.1577.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BT020977 mRNA. Translation: AAX08994.1 .
AY911382 mRNA. Translation: AAW82145.1 .
BC105345 mRNA. Translation: AAI05346.1 .
RefSeqi NP_001014945.1. NM_001014945.2.
XP_005203271.1. XM_005203214.1.
UniGenei Bt.1577.

3D structure databases

ProteinModelPortali Q5E9E3.
SMRi Q5E9E3. Positions 112-243.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q5E9E3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000009415 ; ENSBTAP00000009415 ; ENSBTAG00000007153 .
ENSBTAT00000040146 ; ENSBTAP00000039925 ; ENSBTAG00000007153 .
GeneIDi 534961.
KEGGi bta:534961.

Organism-specific databases

CTDi 712.

Phylogenomic databases

eggNOGi NOG126311.
GeneTreei ENSGT00760000118830.
HOGENOMi HOG000085653.
HOVERGENi HBG108220.
InParanoidi Q5E9E3.
KOi K03986.
OMAi YYYFTFQ.
OrthoDBi EOG70ZZPW.
TreeFami TF329591.

Miscellaneous databases

NextBioi 20876583.

Family and domain databases

Gene3Di 2.60.120.40. 1 hit.
InterProi IPR001073. C1q.
IPR008160. Collagen.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view ]
Pfami PF00386. C1q. 1 hit.
PF01391. Collagen. 1 hit.
[Graphical view ]
PRINTSi PR00007. COMPLEMNTC1Q.
SMARTi SM00110. C1Q. 1 hit.
[Graphical view ]
SUPFAMi SSF49842. SSF49842. 1 hit.
PROSITEi PS50871. C1Q. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "Analysis of sequences obtained from constructed full-length bovine cDNA libraries."
    Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lymphoid epithelium.
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.

Entry informationi

Entry nameiC1QA_BOVIN
AccessioniPrimary (citable) accession number: Q5E9E3
Secondary accession number(s): Q56JV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 15, 2005
Last modified: October 29, 2014
This is version 72 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3