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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi36 – 43GTP8
Nucleotide bindingi196 – 200GTP5
Nucleotide bindingi265 – 268GTP4

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00002037352 – 350Guanine nucleotide-binding protein G(t) subunit alpha-1Add BLAST349

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1
Modified residuei142PhosphotyrosineBy similarity1

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiP04695.
PRIDEiP04695.

PTM databases

iPTMnetiP04695.

Expressioni

Tissue specificityi

Rod.

Gene expression databases

BgeeiENSBTAG00000018020.

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 interactor.
DIPiDIP-29226N.
IntActiP04695. 5 interactors.
STRINGi9913.ENSBTAP00000023990.

Structurei

Secondary structure

1350
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 27Combined sources21
Beta strandi28 – 35Combined sources8
Helixi42 – 53Combined sources12
Helixi59 – 86Combined sources28
Helixi96 – 109Combined sources14
Helixi117 – 128Combined sources12
Helixi130 – 137Combined sources8
Helixi138 – 141Combined sources4
Helixi148 – 152Combined sources5
Helixi155 – 158Combined sources4
Beta strandi160 – 162Combined sources3
Helixi167 – 172Combined sources6
Beta strandi181 – 187Combined sources7
Beta strandi190 – 196Combined sources7
Helixi201 – 204Combined sources4
Helixi205 – 210Combined sources6
Beta strandi215 – 222Combined sources8
Helixi223 – 227Combined sources5
Helixi238 – 250Combined sources13
Helixi253 – 255Combined sources3
Beta strandi258 – 265Combined sources8
Helixi267 – 273Combined sources7
Turni274 – 276Combined sources3
Helixi279 – 281Combined sources3
Helixi292 – 304Combined sources13
Turni308 – 312Combined sources5
Beta strandi316 – 319Combined sources4
Helixi325 – 341Combined sources17
Helixi342 – 345Combined sources4
Turni346 – 348Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04695.

Family & Domainsi

Phylogenomic databases

eggNOGiKOG0082. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiP04695.
KOiK04631.
OMAiCYERASE.
OrthoDBiEOG091G0VUT.
TreeFamiTF300673.

Family and domain databases

CDDicd00066. G-alpha. 1 hit.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi159108. 1 interactor.
DIPiDIP-29226N.
IntActiP04695. 5 interactors.
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.
OrthoDBiEOG091G0VUT.
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.

Gene expression databases

BgeeiENSBTAG00000018020.

Family and domain databases

CDDicd00066. G-alpha. 1 hit.
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...

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: November 30, 2016
This is version 162 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.