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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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi62 – 621MagnesiumBy similarity
Metal bindingi203 – 2031MagnesiumBy similarity
Binding sitei349 – 3491GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi55 – 628GTPBy similarity
Nucleotide bindingi197 – 2037GTPBy similarity
Nucleotide bindingi222 – 2265GTPBy similarity
Nucleotide bindingi291 – 2944GTPBy similarity

GO - Molecular functioni

  1. D5 dopamine receptor binding Source: GO_Central
  2. G-protein beta/gamma-subunit complex binding Source: GO_Central
  3. GTPase activity Source: MGI
  4. GTP binding Source: UniProtKB-KW
  5. metal ion binding Source: UniProtKB-KW
  6. signal transducer activity Source: GO_Central
  7. type 1 angiotensin receptor binding Source: GO_Central

GO - Biological processi

  1. activation of phospholipase D activity Source: GO_Central
  2. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: MGI
  3. angiogenesis Source: MGI
  4. cell differentiation Source: MGI
  5. G-protein coupled receptor signaling pathway Source: MGI
  6. GTP catabolic process Source: InterPro
  7. intracellular signal transduction Source: MGI
  8. in utero embryonic development Source: MGI
  9. patterning of blood vessels Source: MGI
  10. platelet activation Source: MGI
  11. positive regulation of cytosolic calcium ion concentration Source: Ensembl
  12. regulation of cell migration Source: MGI
  13. regulation of cell shape Source: MGI
  14. Rho protein signal transduction Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_204733. G alpha (12/13) signalling events.
REACT_220322. Thrombin signalling through proteinase activated receptors (PARs).
REACT_233922. Thromboxane signalling through TP receptor.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:95768. Gna13.

Subcellular locationi

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

GO - Cellular componenti

  1. brush border membrane Source: GO_Central
  2. extracellular vesicular exosome Source: MGI
  3. focal adhesion Source: MGI
  4. heterotrimeric G-protein complex Source: MGI
  5. melanosome Source: UniProtKB-SubCell
  6. membrane Source: MGI
  7. nucleus Source: UniProtKB-SubCell
  8. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 377377Guanine nucleotide-binding protein subunit alpha-13PRO_0000203774Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi14 – 141S-palmitoyl cysteineBy similarity
Lipidationi18 – 181S-palmitoyl cysteineBy similarity
Modified residuei203 – 2031PhosphothreonineBy similarity

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

MaxQBiP27601.
PaxDbiP27601.
PRIDEiP27601.

PTM databases

PhosphoSiteiP27601.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP27601.
CleanExiMM_GNA13.
ExpressionAtlasiP27601. baseline and differential.
GenevestigatoriP27601.

Interactioni

Subunit structurei

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with UBXD5. Interacts with HAX1. Interacts (when active) with PPP5C (via TPR repeats); activates PPP5C phosphatase activity and translocates PPP5C to the cell membrane (By similarity). Interacts with RGS22 (By similarity).By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi199963. 2 interactions.
DIPiDIP-46241N.
IntActiP27601. 3 interactions.
MINTiMINT-4096246.

Structurei

Secondary structure

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi49 – 546Combined sources
Helixi61 – 7212Combined sources
Helixi78 – 825Combined sources
Helixi85 – 10521Combined sources
Helixi113 – 1153Combined sources
Helixi116 – 1238Combined sources
Beta strandi127 – 1293Combined sources
Helixi130 – 1334Combined sources
Helixi139 – 15416Combined sources
Helixi156 – 1638Combined sources
Helixi164 – 1674Combined sources
Helixi174 – 1785Combined sources
Helixi181 – 1844Combined sources
Beta strandi185 – 1884Combined sources
Helixi193 – 1986Combined sources
Beta strandi204 – 21310Combined sources
Beta strandi216 – 2238Combined sources
Helixi227 – 23610Combined sources
Beta strandi242 – 2487Combined sources
Helixi251 – 2533Combined sources
Beta strandi259 – 2635Combined sources
Helixi264 – 27613Combined sources
Helixi279 – 2813Combined sources
Beta strandi284 – 2918Combined sources
Helixi293 – 2997Combined sources
Turni300 – 3023Combined sources
Helixi305 – 3073Combined sources
Helixi319 – 33113Combined sources
Beta strandi343 – 3464Combined sources
Helixi352 – 37120Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 47-369.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27601.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG279688.
GeneTreeiENSGT00770000120503.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiP27601.
KOiK04639.
OMAiCFPGCVL.
OrthoDBiEOG7HF1JF.
PhylomeDBiP27601.
TreeFamiTF300673.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR000469. Gprotein_alpha_12.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00440. GPROTEINA12.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521L → P in AAH57665 (PubMed:15489334).Curated

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 47-369.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199963. 2 interactions.
DIPiDIP-46241N.
IntActiP27601. 3 interactions.
MINTiMINT-4096246.

PTM databases

PhosphoSiteiP27601.

Proteomic databases

MaxQBiP27601.
PaxDbiP27601.
PRIDEiP27601.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10672.
MGIiMGI:95768. Gna13.

Phylogenomic databases

eggNOGiNOG279688.
GeneTreeiENSGT00770000120503.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiP27601.
KOiK04639.
OMAiCFPGCVL.
OrthoDBiEOG7HF1JF.
PhylomeDBiP27601.
TreeFamiTF300673.

Enzyme and pathway databases

ReactomeiREACT_204733. G alpha (12/13) signalling events.
REACT_220322. Thrombin signalling through proteinase activated receptors (PARs).
REACT_233922. Thromboxane signalling through TP receptor.

Miscellaneous databases

ChiTaRSiGna13. mouse.
EvolutionaryTraceiP27601.
NextBioi286562.
PROiP27601.
SOURCEiSearch...

Gene expression databases

BgeeiP27601.
CleanExiMM_GNA13.
ExpressionAtlasiP27601. baseline and differential.
GenevestigatoriP27601.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR000469. Gprotein_alpha_12.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00440. GPROTEINA12.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "G alpha 12 and G alpha 13 subunits define a fourth class of G protein alpha subunits."
    Strathmann M.P., Simon M.I.
    Proc. Natl. Acad. Sci. U.S.A. 88:5582-5586(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "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: NMRI.
    Tissue: Mammary tumor.
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 51-61 AND 220-227, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  4. "Diversity of the G-protein family: sequences from five additional alpha subunits in the mouse."
    Strathmann M., Wilkie T.M., Simon M.I.
    Proc. Natl. Acad. Sci. U.S.A. 86:7407-7409(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 228-288.
  5. "RGS22, a novel testis-specific regulator of G-protein signaling involved in human and mouse spermiogenesis along with GNA12/13 subunits."
    Hu Y., Xing J., Chen L., Guo X., Du Y., Zhao C., Zhu Y., Lin M., Zhou Z., Sha J.
    Biol. Reprod. 79:1021-1029(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Testis.

Entry informationi

Entry nameiGNA13_MOUSE
AccessioniPrimary (citable) accession number: P27601
Secondary accession number(s): Q6PF99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: March 4, 2015
This is version 141 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

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

External Data

Dasty 3

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 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.