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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.1 Publication

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-RNO-416482. G alpha (12/13) signalling events.
R-RNO-428930. 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi1310221. Gna13.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi226 – 2261Q → L: Constitutively active. Interacts with PPP5C, activates its phosphatase activity and translocates PPP5C to the plasma membrane. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 377377Guanine nucleotide-binding protein subunit alpha-13PRO_0000424080Add
BLAST

Amino acid modifications

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

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.

Expressioni

Gene expression databases

ExpressionAtlasiQ6Q7Y5. baseline and differential.
GenevisibleiQ6Q7Y5. RN.

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.1 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 interaction.
STRINGi10116.ENSRNOP00000051938.

Structurei

3D structure databases

ProteinModelPortaliQ6Q7Y5.
SMRiQ6Q7Y5. Positions 47-372.
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.
PhylomeDBiQ6Q7Y5.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR000469. Gprotein_alpha_12/13.
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.

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ6Q7Y5.
SMRiQ6Q7Y5. Positions 47-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6Q7Y5. 1 interaction.
STRINGi10116.ENSRNOP00000051938.

PTM databases

iPTMnetiQ6Q7Y5.

Proteomic databases

PaxDbiQ6Q7Y5.
PRIDEiQ6Q7Y5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10672.
RGDi1310221. Gna13.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiR-RNO-416482. G alpha (12/13) signalling events.
R-RNO-428930. Thromboxane signalling through TP receptor.

Miscellaneous databases

PROiQ6Q7Y5.

Gene expression databases

ExpressionAtlasiQ6Q7Y5. baseline and differential.
GenevisibleiQ6Q7Y5. RN.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR000469. Gprotein_alpha_12/13.
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. "Genetic similarity between spontaneously hypertensive rats and wistar-kyoto rats in the coding regions of signal transduction proteins."
    Jackson E.K., Zhu C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: SHR and Wistar Kyoto.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "Galpha(12) and Galpha(13) interact with Ser/Thr protein phosphatase type 5 and stimulate its phosphatase activity."
    Yamaguchi Y., Katoh H., Mori K., Negishi M.
    Curr. Biol. 12:1353-1358(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PPP5C, SUBCELLULAR LOCATION, MUTAGENESIS OF GLN-226.

Entry informationi

Entry nameiGNA13_RAT
AccessioniPrimary (citable) accession number: Q6Q7Y5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 102 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

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.