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Protein

Guanine nucleotide-binding protein G(t) subunit alpha-1

Gene

GNAT1

Organism
Bos taurus (Bovine)
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. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 438GTP
Nucleotide bindingi196 – 2005GTP
Nucleotide bindingi265 – 2684GTP

GO - Molecular functioni

  • acyl binding Source: UniProtKB
  • GDP binding Source: UniProtKB
  • G-protein beta/gamma-subunit complex binding Source: GO_Central
  • G-protein coupled receptor binding Source: GO_Central
  • GTPase activity Source: GO_Central
  • GTP binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • signal transducer activity Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-112043. PLC beta mediated events.
R-BTA-202040. G-protein activation.
R-BTA-2485179. Activation of the phototransduction cascade.
R-BTA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-BTA-418594. G alpha (i) signalling events.
R-BTA-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(t) subunit alpha-1
Alternative name(s):
Transducin alpha-1 chain
Gene namesi
Name:GNAT1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 22

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 350349Guanine nucleotide-binding protein G(t) subunit alpha-1PRO_0000203735Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei142 – 1421PhosphotyrosineBy similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiP04695.
PRIDEiP04695.

PTM databases

iPTMnetiP04695.

Expressioni

Tissue specificityi

Rod.

Interactioni

Subunit structurei

Interacts (when myristoylated) with UNC119; interaction is required for localization in sensory neurons (By similarity). G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CNGB1Q281814EBI-7052221,EBI-6979031

GO - Molecular functioni

Protein-protein interaction databases

BioGridi159108. 1 interaction.
DIPiDIP-29226N.
IntActiP04695. 5 interactions.
STRINGi9913.ENSBTAP00000023990.

Structurei

Secondary structure

1
350
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2721Combined sources
Beta strandi28 – 358Combined sources
Helixi42 – 5312Combined sources
Helixi59 – 8628Combined sources
Helixi96 – 10914Combined sources
Helixi117 – 12812Combined sources
Helixi130 – 1378Combined sources
Helixi138 – 1414Combined sources
Helixi148 – 1525Combined sources
Helixi155 – 1584Combined sources
Beta strandi160 – 1623Combined sources
Helixi167 – 1726Combined sources
Beta strandi181 – 1877Combined sources
Beta strandi190 – 1967Combined sources
Helixi201 – 2044Combined sources
Helixi205 – 2106Combined sources
Beta strandi215 – 2228Combined sources
Helixi223 – 2275Combined sources
Helixi238 – 25013Combined sources
Helixi253 – 2553Combined sources
Beta strandi258 – 2658Combined sources
Helixi267 – 2737Combined sources
Turni274 – 2763Combined sources
Helixi279 – 2813Combined sources
Helixi292 – 30413Combined sources
Turni308 – 3125Combined sources
Beta strandi316 – 3194Combined sources
Helixi325 – 34117Combined sources
Helixi342 – 3454Combined sources
Turni346 – 3483Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQGNMR-A340-350[»]
1FQJX-ray2.02A/D26-215[»]
A/D295-350[»]
1FQKX-ray2.30A/C26-215[»]
A/C295-350[»]
1GOTX-ray2.00A1-350[»]
1LVZNMR-A340-350[»]
1TADX-ray1.70A/B/C27-350[»]
1TAGX-ray1.80A27-350[»]
1TNDX-ray2.20A/B/C27-350[»]
2X72X-ray3.00B340-350[»]
3DQBX-ray3.20B340-350[»]
3PQRX-ray2.85B340-350[»]
3V00X-ray2.90A/B/C1-215[»]
A/B/C295-350[»]
4BEYX-ray2.90B340-350[»]
4J4QX-ray2.65B340-350[»]
DisProtiDP00273.
ProteinModelPortaliP04695.
SMRiP04695. Positions 27-349.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04695.

Family & Domainsi

Phylogenomic databases

eggNOGiKOG0082. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiP04695.
KOiK04631.
OMAiCYERASE.
OrthoDBiEOG72C50B.
TreeFamiTF300673.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001408. Gprotein_alpha_I.
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.
PR00441. GPROTEINAI.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04695-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAGASAEEK HSRELEKKLK EDAEKDARTV KLLLLGAGES GKSTIVKQMK
60 70 80 90 100
IIHQDGYSLE ECLEFIAIIY GNTLQSILAI VRAMTTLNIQ YGDSARQDDA
110 120 130 140 150
RKLMHMADTI EEGTMPKEMS DIIQRLWKDS GIQACFDRAS EYQLNDSAGY
160 170 180 190 200
YLSDLERLVT PGYVPTEQDV LRSRVKTTGI IETQFSFKDL NFRMFDVGGQ
210 220 230 240 250
RSERKKWIHC FEGVTCIIFI AALSAYDMVL VEDDEVNRMH ESLHLFNSIC
260 270 280 290 300
NHRYFATTSI VLFLNKKDVF SEKIKKAHLS ICFPDYNGPN TYEDAGNYIK
310 320 330 340 350
VQFLELNMRR DVKEIYSHMT CATDTQNVKF VFDAVTDIII KENLKDCGLF
Length:350
Mass (Da):39,966
Last modified:January 23, 2007 - v3
Checksum:i36F0B4630EFBD7DF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03253 mRNA. Translation: AAA30787.1.
K03254 mRNA. Translation: AAA30791.1.
X02440 mRNA. Translation: CAA26285.1.
PIRiA22244. RGBOT1.
RefSeqiNP_851365.1. NM_181022.2.
XP_010815966.1. XM_010817664.2.
UniGeneiBt.4774.

Genome annotation databases

EnsembliENSBTAT00000023990; ENSBTAP00000023990; ENSBTAG00000018020.
GeneIDi281794.
KEGGibta:281794.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03253 mRNA. Translation: AAA30787.1.
K03254 mRNA. Translation: AAA30791.1.
X02440 mRNA. Translation: CAA26285.1.
PIRiA22244. RGBOT1.
RefSeqiNP_851365.1. NM_181022.2.
XP_010815966.1. XM_010817664.2.
UniGeneiBt.4774.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQGNMR-A340-350[»]
1FQJX-ray2.02A/D26-215[»]
A/D295-350[»]
1FQKX-ray2.30A/C26-215[»]
A/C295-350[»]
1GOTX-ray2.00A1-350[»]
1LVZNMR-A340-350[»]
1TADX-ray1.70A/B/C27-350[»]
1TAGX-ray1.80A27-350[»]
1TNDX-ray2.20A/B/C27-350[»]
2X72X-ray3.00B340-350[»]
3DQBX-ray3.20B340-350[»]
3PQRX-ray2.85B340-350[»]
3V00X-ray2.90A/B/C1-215[»]
A/B/C295-350[»]
4BEYX-ray2.90B340-350[»]
4J4QX-ray2.65B340-350[»]
DisProtiDP00273.
ProteinModelPortaliP04695.
SMRiP04695. Positions 27-349.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi159108. 1 interaction.
DIPiDIP-29226N.
IntActiP04695. 5 interactions.
STRINGi9913.ENSBTAP00000023990.

PTM databases

iPTMnetiP04695.

Proteomic databases

PaxDbiP04695.
PRIDEiP04695.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000023990; ENSBTAP00000023990; ENSBTAG00000018020.
GeneIDi281794.
KEGGibta:281794.

Organism-specific databases

CTDi2779.

Phylogenomic databases

eggNOGiKOG0082. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiP04695.
KOiK04631.
OMAiCYERASE.
OrthoDBiEOG72C50B.
TreeFamiTF300673.

Enzyme and pathway databases

ReactomeiR-BTA-112043. PLC beta mediated events.
R-BTA-202040. G-protein activation.
R-BTA-2485179. Activation of the phototransduction cascade.
R-BTA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-BTA-418594. G alpha (i) signalling events.
R-BTA-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Miscellaneous databases

EvolutionaryTraceiP04695.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001408. Gprotein_alpha_I.
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.
PR00441. GPROTEINAI.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "Amino acid sequence of the alpha subunit of transducin deduced from the cDNA sequence."
    Medynski D.C., Sullivan K., Smith D., van Dop C., Chang F.-H., Fung B.K.-K., Seeburg P.H., Bourne H.R.
    Proc. Natl. Acad. Sci. U.S.A. 82:4311-4315(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "GTPase of bovine rod outer segments: the amino acid sequence of the alpha subunit as derived from the cDNA sequence."
    Yatsunami K., Khorana H.G.
    Proc. Natl. Acad. Sci. U.S.A. 82:4316-4320(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Primary structure of the alpha-subunit of transducin and its relationship to ras proteins."
    Tanaba T., Nukada T., Nishikawa Y., Sugimoto K., Suzuki H., Takahashi H., Noda M., Haga T., Ichiyama A., Kangawa K., Minamino N., Matsuo H., Numa S.
    Nature 315:242-245(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Isolation and characteristics of cyanogen bromide peptides of transducin alpha and beta subunits."
    Lipkin V.M., Obukhov A.N., Bogachuk A.P., Telezhinskaya I.N., Shemyakin V.V.
    Bioorg. Khim. 11:1481-1492(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  5. "Lipid modification at the N-terminus of photoreceptor G-protein alpha-subunit."
    Kokame K., Fukada Y., Yoshizawa T., Takao T., Shimonishi Y.
    Nature 359:749-752(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2.
  6. "The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S."
    Noel J.P., Hamm H.E., Sigler P.B.
    Nature 366:654-663(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GTP ANALOG.
  7. "Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein."
    Lambright D.G., Noel J.P., Hamm H.E., Sigler P.B.
    Nature 369:621-628(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GDP.
  8. "GTPase mechanism of Gproteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4."
    Sondek J., Lambright D.G., Noel J.P., Hamm H.E., Sigler P.B.
    Nature 372:276-279(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH GTP ANALOG.
  9. "Light-activated rhodopsin induces structural binding motif in G protein alpha subunit."
    Kisselev O.G., Kao J., Ponder J.W., Fann Y.C., Gautam N., Marshall G.R.
    Proc. Natl. Acad. Sci. U.S.A. 95:4270-4275(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 340-350.
    Tissue: Retina.
  10. "Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A."
    Slep K.C., Kercher M.A., He W., Cowan C.W., Wensel T.G., Sigler P.B.
    Nature 409:1071-1077(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 26-350 IN COMPLEX WITH PDE6G AND GNAT1.

Entry informationi

Entry nameiGNAT1_BOVIN
AccessioniPrimary (citable) accession number: P04695
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 158 of the entry and version 3 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.