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Protein

Guanine nucleotide-binding protein subunit alpha-13

Gene

Gna13

Organism
Rattus norvegicus (Rat)
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:12176367). Activates effector molecule RhoA by binding and activating RhoGEFs (ARHGEF1/p115RhoGEF, ARHGEF11/PDZ-RhoGEF and ARHGEF12/LARG) (By similarity). GNA13-dependent Rho signaling subsequently regulates transcription factor AP-1 (activating protein-1) (By similarity). Promotes tumor cell invasion and metastasis by activating RhoA/ROCK signaling pathway (By similarity). Inhibits CDH1-mediated cell adhesion in process independent from Rho activation (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi62MagnesiumBy similarity1
Binding sitei173GTPBy similarity1
Metal bindingi203MagnesiumBy similarity1
Metal bindingi222MagnesiumBy similarity1
Binding sitei349GTP; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi58 – 63GTPBy similarity6
Nucleotide bindingi197 – 200GTPBy similarity4
Nucleotide bindingi291 – 294GTPBy similarity4

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-RNO-193648. NRAGE signals death through JNK.
R-RNO-194840. Rho GTPase cycle.
R-RNO-416482. G alpha (12/13) signalling events.
R-RNO-428930. Thromboxane signalling through TP receptor.
R-RNO-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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi1310221. Gna13.

Subcellular locationi

  • Membrane 1 Publication; Lipid-anchor 1 Publication
  • Melanosome By similarity
  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Cytoplasmic in adult somatic cells, but mainly nuclear in spermatids in the testes. Translocates from the cytoplasm to the nucleus during spermatogenesis, hence predominantly observed in the cytoplasm of round spermatids but localized in the nuclei of elongating or elongated spermatids and testicular spermatozoa.By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi226Q → L: Constitutively active. Interacts with PPP5C, activates its phosphatase activity and translocates PPP5C to the plasma membrane. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004240801 – 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 residuei203Phosphothreonine; by PKABy similarity1

Post-translational modificationi

Palmitoylation is critical for proper membrane localization and signaling.By similarity
Phosphorylation on Thr-203 by PKA destabilizes the heterotrimer of alpha, beta and gamma, and inhibits Rho activation.

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiQ6Q7Y5.
PRIDEiQ6Q7Y5.

PTM databases

iPTMnetiQ6Q7Y5.
PhosphoSitePlusiQ6Q7Y5.

Expressioni

Gene expression databases

BgeeiENSRNOG00000036745.
GenevisibleiQ6Q7Y5. RN.

Interactioni

Subunit structurei

G proteins are composed of 3 units; alpha, beta and gamma (By similarity). The alpha chain contains the guanine nucleotide binding site (By similarity). 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 (PubMed:12176367). Interacts with RGS22 (By similarity). Interacts with ARHGEF1. Interacts (in GTP-bound form) with ARHGEF11 (via RGS domain) (By similarity). Interacts (in GTP-bound form) with ARHGEF12 (via RGS domain) (By similarity). Interacts (in GTP-bound form) with CTNND1 (By similarity).By similarity1 Publication

GO - Molecular functioni

  • D5 dopamine receptor binding Source: RGD
  • G-protein beta/gamma-subunit complex binding Source: GO_Central

Protein-protein interaction databases

IntActiQ6Q7Y5. 1 interactor.
STRINGi10116.ENSRNOP00000051938.

Structurei

3D structure databases

ProteinModelPortaliQ6Q7Y5.
SMRiQ6Q7Y5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0082. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00770000120503.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
KOiK04639.
OMAiCFPGCVL.
OrthoDBiEOG091G0NV2.
PhylomeDBiQ6Q7Y5.

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.

Q6Q7Y5-1 [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 GDNKNQVHGD KLMAFDTRAP MAAQGMVETR VFLQYLPAIR
160 170 180 190 200
ALWDDSGIQN AYDRRREFQL GESVKYFLDN LDKLGVPDYI PSQQDILLAR
210 220 230 240 250
RPTKGIHEYD FEIKNVPFKM VDVGGQRSER KRWFECFDSV TSILFLVSSS
260 270 280 290 300
EFDQVLMEDR LTNRLTESLN IFETIVNNRV FSNVSIILFL NKTDLLEEKV
310 320 330 340 350
QVVSIKDYFL EFEGDPHCLR DVQKFLVECF RGKRRDQQQR PLYHHFTTAI
360 370
NTENIRLVFR DVKDTILHDN LKQLMLQ
Length:377
Mass (Da):44,012
Last modified:July 5, 2004 - v1
Checksum:i076F9F65508E8416
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY553631 mRNA. Translation: AAS64389.1.
AY553632 mRNA. Translation: AAS64390.1.
DQ120481 mRNA. Translation: AAZ23820.1.
DQ120482 mRNA. Translation: AAZ23821.1.
RefSeqiNP_001013137.1. NM_001013119.1.
UniGeneiRn.163174.

Genome annotation databases

EnsembliENSRNOT00000055062; ENSRNOP00000051938; ENSRNOG00000036745.
GeneIDi303634.
KEGGirno:303634.

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_RAT
AccessioniPrimary (citable) accession number: Q6Q7Y5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: July 5, 2004
Last modified: July 5, 2017
This is version 112 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families