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UniProtKB - P27601 (GNA13_MOUSE)

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Protein

Guanine nucleotide-binding protein subunit alpha-13

Gene

Gna13

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

Functioni

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems (PubMed:21212405, PubMed:19151758, PubMed:16388592). Activates effector molecule RhoA by binding and activating RhoGEFs (ARHGEF1/p115RhoGEF, ARHGEF11/PDZ-RhoGEF and ARHGEF12/LARG) (PubMed:16388592). GNA13-dependent Rho signaling subsequently regulates transcription factor AP-1 (activating protein-1) (PubMed:19151758, PubMed:21212405). Promotes tumor cell invasion and metastasis by activating Rho/ROCK signaling pathway (By similarity). Inhibits CDH1-mediated cell adhesion in process independent from Rho activation (By similarity).By similarity3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi62MagnesiumCombined sources1 Publication1
Binding sitei173GTPCombined sources1 Publication1
Metal bindingi203MagnesiumCombined sources1 Publication1
Metal bindingi222MagnesiumCombined sources1 Publication1
Binding sitei349GTP; via amide nitrogenCombined sources2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi58 – 63GTPCombined sources2 Publications6
Nucleotide bindingi197 – 200GTPCombined sources2 Publications4
Nucleotide bindingi291 – 294GTPCombined sources2 Publications4

GO - Molecular functioni

Complete GO annotation...

GO - Biological processi

  • activation of phospholipase D activity Source: GO_Central
  • adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: MGI
  • angiogenesis Source: MGI
  • branching involved in blood vessel morphogenesis Source: MGI
  • cell differentiation Source: MGI
  • G-protein coupled receptor signaling pathway Source: MGI
  • intracellular signal transduction Source: MGI
  • in utero embryonic development Source: MGI
  • platelet activation Source: MGI
  • positive regulation of cytosolic calcium ion concentration Source: Ensembl
  • regulation of cell migration Source: MGI
  • regulation of cell shape Source: MGI
  • Rho protein signal transduction Source: MGI
Complete GO annotation...

Keywordsi

Molecular functionTransducer
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-193648. NRAGE signals death through JNK.
R-MMU-194840. Rho GTPase cycle.
R-MMU-416482. G alpha (12/13) signalling events.
R-MMU-428930. Thromboxane signalling through TP receptor.
R-MMU-456926. Thrombin signalling through proteinase activated receptors (PARs).

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein subunit alpha-13
Short name:
G alpha-13
Short name:
G-protein subunit alpha-13
Gene namesi
Name:Gna13
Synonyms:Gna-13
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:95768. Gna13.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002037741 – 377Guanine nucleotide-binding protein subunit alpha-13Add BLAST377

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi14S-palmitoyl cysteineBy similarity1
Lipidationi18S-palmitoyl cysteineBy similarity1
Modified residuei203PhosphothreonineBy similarity1

Post-translational modificationi

Phosphorylation on Thr-203 destabilizes the heterotrimer of alpha, beta and gamma, and inhibits Rho activation.By similarity

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

EPDiP27601.
MaxQBiP27601.
PaxDbiP27601.
PeptideAtlasiP27601.
PRIDEiP27601.

PTM databases

iPTMnetiP27601.
PhosphoSitePlusiP27601.
SwissPalmiP27601.

Expressioni

Tissue specificityi

Expressed in brain and testis, as well as in kidney and sperm (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000020611.
CleanExiMM_GNA13.
ExpressionAtlasiP27601. baseline and differential.
GenevisibleiP27601. MM.

Interactioni

Subunit structurei

G proteins are composed of 3 units; alpha, beta and gamma (PubMed:16388592). The alpha chain contains the guanine nucleotide binding site (PubMed:16388592). Interacts with UBXD5 (By similarity). Interacts with HAX1 (By similarity). Interacts (in GTP-bound form) with PPP5C (via TPR repeats); activates PPP5C phosphatase activity and translocates PPP5C to the cell membrane (By similarity). Interacts with RGS22 (By similarity). Interacts (in GTP-bound form) with ARHGEF1 (PubMed:16388592). Interacts (in GTP-bound form) with ARHGEF11 (via RGS domain) (PubMed:18940608). Interacts (in GTP-bound form) with ARHGEF12 (via RGS domain) (PubMed:16388592). Interacts with CTNND1 (PubMed:15240885).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AipO089153EBI-2255627,EBI-6935014

GO - Molecular functioni

Complete GO annotation...

Protein-protein interaction databases

BioGridi199963. 2 interactors.
DIPiDIP-46241N.
IntActiP27601. 4 interactors.
MINTiMINT-4096246.
STRINGi10090.ENSMUSP00000020930.

Structurei

Secondary structure

1377
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi49 – 54Combined sources6
Helixi61 – 72Combined sources12
Helixi78 – 82Combined sources5
Helixi85 – 105Combined sources21
Helixi113 – 115Combined sources3
Helixi116 – 123Combined sources8
Beta strandi127 – 129Combined sources3
Helixi130 – 133Combined sources4
Helixi139 – 154Combined sources16
Helixi156 – 163Combined sources8
Helixi164 – 167Combined sources4
Helixi174 – 178Combined sources5
Helixi181 – 184Combined sources4
Beta strandi185 – 188Combined sources4
Helixi193 – 198Combined sources6
Beta strandi204 – 213Combined sources10
Beta strandi216 – 223Combined sources8
Helixi227 – 236Combined sources10
Beta strandi242 – 248Combined sources7
Helixi251 – 253Combined sources3
Beta strandi259 – 263Combined sources5
Helixi264 – 276Combined sources13
Helixi279 – 281Combined sources3
Beta strandi284 – 291Combined sources8
Helixi293 – 299Combined sources7
Turni300 – 302Combined sources3
Helixi305 – 307Combined sources3
Helixi319 – 331Combined sources13
Beta strandi343 – 346Combined sources4
Helixi352 – 371Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SHZX-ray2.85A/D52-159[»]
A/D333-376[»]
1ZCBX-ray2.00A47-377[»]
3AB3X-ray2.40A/C47-377[»]
3CX6X-ray2.50A41-377[»]
3CX7X-ray2.25A41-377[»]
3CX8X-ray2.00A41-377[»]
ProteinModelPortaliP27601.
SMRiP27601.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27601.

Family & Domainsi

Sequence similaritiesi

Belongs to the G-alpha family. G(12) subfamily.Curated

Phylogenomic databases

eggNOGiKOG0082. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00770000120503.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiP27601.
KOiK04639.
OMAiCFPGCVL.
OrthoDBiEOG091G0NV2.
PhylomeDBiP27601.
TreeFamiTF300673.

Family and domain databases

CDDicd00066. G-alpha. 1 hit.
Gene3Di1.10.400.10. 1 hit.
InterProiView protein in InterPro
IPR000469. Gprotein_alpha_12/13.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiView protein in Pfam
PF00503. G-alpha. 1 hit.
PRINTSiPR00318. GPROTEINA.
PR00440. GPROTEINA12.
SMARTiView protein in SMART
SM00275. G_alpha. 1 hit.
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

P27601-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADFLPSRSV LSVCFPGCVL TNGEAEQQRK SKEIDKCLSR EKTYVKRLVK 
        60         70         80         90        100
ILLLGAGESG KSTFLKQMRI IHGQDFDQRA REEFRPTIYS NVIKGMRVLV 
       110        120        130        140        150
DAREKLHIPW GDNKNQLHGD KLMAFDTRAP MAAQGMVETR VFLQYLPAIR 
       160        170        180        190        200
ALWEDSGIQN AYDRRREFQL GESVKYFLDN LDKLGVPDYI PSQQDILLAR 
       210        220        230        240        250
RPTKGIHEYD FEIKNVPFKM VDVGGQRSER KRWFECFDSV TSILFLVSSS 
       260        270        280        290        300
EFDQVLMEDR QTNRLTESLN IFETIVNNRV FSNVSIILFL NKTDLLEEKV 
       310        320        330        340        350
QVVSIKDYFL EFEGDPHCLR DVQKFLVECF RGKRRDQQQR PLYHHFTTAI 
       360        370 
NTENIRLVFR DVKDTILHDN LKQLMLQ
Length:377
Mass (Da):44,055
Last modified:August 1, 1992 - v1
Checksum:i45A6A6DB47C707BB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti52L → P in AAH57665 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63660 mRNA. Translation: AAA37649.1.
BC057665 mRNA. Translation: AAH57665.1.
M57620 mRNA. Translation: AAA63303.1.
CCDSiCCDS25577.1.
PIRiB41095.
RefSeqiNP_034433.3. NM_010303.3.
UniGeneiMm.193925.

Genome annotation databases

EnsembliENSMUST00000020930; ENSMUSP00000020930; ENSMUSG00000020611.
GeneIDi14674.
KEGGimmu:14674.
UCSCiuc007mce.1. mouse.

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.

Entry informationi

Entry nameiGNA13_MOUSE
AccessioniPrimary (citable) accession number: P27601
Secondary accession number(s): Q6PF99
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 7, 2017
This is version 162 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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