P27601 (GNA13_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanine nucleotide-binding protein subunit alpha-13
Short name=G alpha-13
Short name=G-protein subunit alpha-13

Gene names

Name:	Gna13
Synonyms:	Gna-13

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Subunit structure	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 By similarity.
Subcellular location	Membrane; Lipid-anchor. Melanosome By similarity.
Post-translational modification	Phosphorylation on Thr-203 destabilizes the heterotrimer of alpha, beta and gamma, and inhibits Rho activation By similarity.
Sequence similarities	Belongs to the G-alpha family. G(12) subfamily.

Ontologies

Keywords
Cellular component	Membrane
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transducer
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Rho protein signal transduction Inferred from direct assay PubMed 10037795. Source: MGI activation of phospholipase D activity Inferred from Biological aspect of Ancestor. Source: RefGenome adenylate cyclase-activating G-protein coupled receptor signaling pathway Inferred from genetic interaction PubMed 18541530. Source: MGI cell differentiation Inferred from direct assay PubMed 9305907. Source: MGI in utero embryonic development Inferred from genetic interaction PubMed 12077299. Source: MGI intracellular protein kinase cascade Inferred from direct assay PubMed 10037795. Source: MGI patterning of blood vessels Inferred from mutant phenotype PubMed 15919816. Source: MGI platelet activation Inferred from mutant phenotype PubMed 14528298. Source: MGI regulation of cell migration Inferred from mutant phenotype PubMed 12077299. Source: MGI regulation of cell shape Inferred from direct assay PubMed 10037795. Source: MGI
Cellular_component	brush border membrane Inferred from Biological aspect of Ancestor. Source: RefGenome heterotrimeric G-protein complex Inferred from sequence alignment Ref.4. Source: MGI melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	D5 dopamine receptor binding Inferred from Biological aspect of Ancestor. Source: RefGenome G-protein beta/gamma-subunit complex binding Inferred from Biological aspect of Ancestor. Source: RefGenome GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from sequence alignment Ref.4. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW signal transducer activity Inferred from Biological aspect of Ancestor. Source: RefGenome type 1 angiotensin receptor binding Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 377

377

Guanine nucleotide-binding protein subunit alpha-13

PRO_0000203774

Regions

Nucleotide binding

55 – 62

8

GTP By similarity

Nucleotide binding

197 – 203

7

GTP By similarity

Nucleotide binding

222 – 226

5

GTP By similarity

Nucleotide binding

291 – 294

4

GTP By similarity

Sites

Metal binding

62

1

Magnesium By similarity

Metal binding

203

1

Magnesium By similarity

Binding site

349

1

GTP; via amide nitrogen By similarity

Amino acid modifications

Modified residue

203

1

Phosphothreonine By similarity

Lipidation

14

1

S-palmitoyl cysteine By similarity

Lipidation

18

1

S-palmitoyl cysteine By similarity

Experimental info

Sequence conflict

52

1

L → P in AAH57665. Ref.2

Secondary structure

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377

Helix Strand Turn

Details...

Beta strand

49 – 54

6

Helix

61 – 72

12

Helix

78 – 82

5

Helix

85 – 105

21

Helix

113 – 115

3

Helix

116 – 123

8

Beta strand

127 – 129

3

Helix

130 – 133

4

Helix

139 – 154

16

Helix

156 – 163

8

Helix

164 – 167

4

Helix

174 – 178

5

Helix

181 – 184

4

Beta strand

185 – 188

4

Helix

193 – 198

6

Beta strand

204 – 213

10

Beta strand

216 – 223

8

Helix

227 – 236

10

Beta strand

242 – 248

7

Helix

251 – 253

3

Beta strand

259 – 263

5

Helix

264 – 276

13

Helix

279 – 281

3

Beta strand

284 – 291

8

Helix

293 – 299

7

Turn

300 – 302

3

Helix

305 – 307

3

Helix

319 – 331

13

Beta strand

343 – 346

4

Helix

352 – 371

20

Sequences

	Sequence		Length	Mass (Da)
	P27601 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 45A6A6DB47C707BB	FASTA	377	44,055
	10 20 30 40 50 60 MADFLPSRSV LSVCFPGCVL TNGEAEQQRK SKEIDKCLSR EKTYVKRLVK ILLLGAGESG 70 80 90 100 110 120 KSTFLKQMRI IHGQDFDQRA REEFRPTIYS NVIKGMRVLV DAREKLHIPW GDNKNQLHGD 130 140 150 160 170 180 KLMAFDTRAP MAAQGMVETR VFLQYLPAIR ALWEDSGIQN AYDRRREFQL GESVKYFLDN 190 200 210 220 230 240 LDKLGVPDYI PSQQDILLAR RPTKGIHEYD FEIKNVPFKM VDVGGQRSER KRWFECFDSV 250 260 270 280 290 300 TSILFLVSSS EFDQVLMEDR QTNRLTESLN IFETIVNNRV FSNVSIILFL NKTDLLEEKV 310 320 330 340 350 360 QVVSIKDYFL EFEGDPHCLR DVQKFLVECF RGKRRDQQQR PLYHHFTTAI NTENIRLVFR 370 DVKDTILHDN LKQLMLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M63660 mRNA. Translation: AAA37649.1.
BC057665 mRNA. Translation: AAH57665.1.
M57620 mRNA. Translation: AAA63303.1.

IPI

IPI00118569.

PIR

B41095.

RefSeq

NP_034433.3. NM_010303.3.

UniGene

Mm.193925.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SHZ	X-ray	2.85	A/D	49-299	[»]
1ZCB	X-ray	2.00	A	47-377	[»]
3AB3	X-ray	2.40	A/C	47-377	[»]
3CX6	X-ray	2.50	A	41-377	[»]
3CX7	X-ray	2.25	A	41-377	[»]
3CX8	X-ray	2.00	A	41-377	[»]

ProteinModelPortal

P27601.

SMR

P27601. Positions 47-369.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46241N.

IntAct

P27601. 1 interaction.

PTM databases

PhosphoSite

P27601.

Proteomic databases

PaxDb

P27601.

PRIDE

P27601.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000020930; ENSMUSP00000020930; ENSMUSG00000020611.

GeneID

14674.

KEGG

mmu:14674.

Organism-specific databases

CTD

10672.

MGI

MGI:95768. Gna13.

Phylogenomic databases

eggNOG

NOG279688.

GeneTree

ENSGT00690000101672.

HOGENOM

HOG000038729.

HOVERGEN

HBG063184.

InParanoid

P27601.

KO

K04639.

OMA

CFPGCVL.

OrthoDB

EOG444KKJ.

Enzyme and pathway databases

Reactome

REACT_89750. Hemostasis.

Gene expression databases

ArrayExpress

P27601.

Bgee

P27601.

CleanEx

MM_GNA13.

Genevestigator

P27601.

GermOnline

ENSMUSG00000020611. Mus musculus.

Family and domain databases

Gene3D

1.10.400.10. 1 hit.

InterPro

IPR000469. Gprotein_alpha_12.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
[Graphical view]

PANTHER

PTHR10218. PTHR10218. 1 hit.

Pfam

PF00503. G-alpha. 1 hit.
[Graphical view]

PRINTS

PR00318. GPROTEINA.
PR00440. GPROTEINA12.

SMART

SM00275. G_alpha. 1 hit.
[Graphical view]

SUPFAM

SSF47895. Transducn_insert. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

GNA13. mouse.

EvolutionaryTrace

P27601.

NextBio

286562.

SOURCE

Search...

Entry information

Entry name

GNA13_MOUSE

Accession

Primary (citable) accession number: P27601
Secondary accession number(s): Q6PF99

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	April 3, 2013
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program