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A5A779

- PGTA_PIG

UniProt

A5A779 - PGTA_PIG

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Protein
Geranylgeranyl transferase type-2 subunit alpha
Gene
RABGGTA
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A By similarity.

Catalytic activityi

Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.

Enzyme regulationi

The enzymatic reaction requires the aid of a Rab escort protein (also called component A), such as CHM By similarity.

GO - Molecular functioni

  1. Rab GTPase binding Source: UniProtKB
  2. Rab geranylgeranyltransferase activity Source: UniProtKB
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. protein geranylgeranylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Geranylgeranyl transferase type-2 subunit alpha (EC:2.5.1.60)
Alternative name(s):
Geranylgeranyl transferase type II subunit alpha
Rab geranyl-geranyltransferase subunit alpha
Short name:
Rab GG transferase alpha
Short name:
Rab GGTase alpha
Rab geranylgeranyltransferase subunit alpha
Gene namesi
Name:RABGGTA
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Chromosome 7

Subcellular locationi

GO - Cellular componenti

  1. Rab-protein geranylgeranyltransferase complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 567567Geranylgeranyl transferase type-2 subunit alpha
PRO_0000331286Add
BLAST

Proteomic databases

PaxDbiA5A779.

Interactioni

Subunit structurei

Heterotrimer composed of RABGGTA, RABGGTB and CHM; within this trimer, RABGGTA and RABGGTB form the catalytic component B, while CHM (component A) mediates peptide substrate binding. The Rab GGTase dimer (RGGT) interacts with CHM (component A) prior to Rab protein binding; the association is stabilized by geranylgeranyl pyrophosphate (GGpp). The CHM:RGGT:Rab complex is destabilized by GGpp By similarity.

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000002178.

Structurei

3D structure databases

ProteinModelPortaliA5A779.
SMRiA5A779. Positions 2-567.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati44 – 7835PFTA 1
Add
BLAST
Repeati88 – 12235PFTA 2
Add
BLAST
Repeati124 – 15835PFTA 3
Add
BLAST
Repeati159 – 19335PFTA 4
Add
BLAST
Repeati207 – 24135PFTA 5
Add
BLAST
Repeati363 – 39735PFTA 6
Add
BLAST
Repeati442 – 46322LRR 1
Add
BLAST
Repeati464 – 48623LRR 2
Add
BLAST
Repeati487 – 50822LRR 3
Add
BLAST
Repeati509 – 53022LRR 4
Add
BLAST
Repeati534 – 55522LRR 5
Add
BLAST

Sequence similaritiesi

Contains 6 PFTA repeats.

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiCOG5536.
GeneTreeiENSGT00550000075121.
HOGENOMiHOG000007845.
HOVERGENiHBG002171.
KOiK14050.
OMAiWNCRREV.
OrthoDBiEOG7PP56C.
TreeFamiTF315057.

Family and domain databases

Gene3Di2.60.40.1130. 1 hit.
InterProiIPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR002088. Prenyl_trans_a.
IPR009087. RabGGT_asu_insert-domain.
[Graphical view]
PfamiPF00560. LRR_1. 1 hit.
PF12799. LRR_4. 1 hit.
PF01239. PPTA. 5 hits.
PF07711. RabGGT_insert. 1 hit.
[Graphical view]
ProDomiPD331837. RabGG_trans_A. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF49594. SSF49594. 1 hit.
PROSITEiPS51147. PFTA. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A5A779-1 [UniParc]FASTAAdd to Basket

« Hide

MHGRLKVKTS EEQAEAKRLE REQKLKLYQT ATQTVFQKRQ AGELDESVLE    50
LTSQILGANP DFATLWNCRR EVLQRLEVQK SPEELAALVK AELGFLESCL 100
RVNPKSYGTW HHRCWLLGRL PEPNWARELE LCARFLEVDE RNFHCWDYRR 150
FVASQAAVPP AEELAFTDSL ITRNFSNYSS WHYRSCLLPQ LHPQPDSGPQ 200
GRLPEDVLLK ELELVQNAFF TDPNDQSAWF YHRWLLGRAD PQDALRCLHV 250
SRDEACLTVS FSRPLLVGPS TETLLLMVNE SPLSVEWRTP DGRNRPSHVW 300
LCDLPAASLN DHLPQHTFRV IWTAGNAQKE CVLLKGRQEG WCRDSATDEQ 350
LFRCELSVEK STVLQSELES CKELQELEPE NKWCLLTIIL LMRALDPLLY 400
EKETLQYFQT LKAVDPMRAA YLDDLRSKFL LENSVLKMEY ADVRVLHLGH 450
KDLTVLCHLE QLLLVTHLDL SHNRLRALPP ALAALRCLEV LQANDNAIES 500
LDGVTNLPRL QELSLCNNRL QQPAVLQPLA SCPRLVLLNL QDNPLCQAVG 550
ISEHLAELLP SVSSILT 567
Length:567
Mass (Da):64,901
Last modified:June 12, 2007 - v1
Checksum:i79BFCA2DD50C4F97
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB271949 mRNA. Translation: BAF62324.1.
RefSeqiNP_001092063.1. NM_001098593.1.
XP_005666280.1. XM_005666223.1.
UniGeneiSsc.45681.

Genome annotation databases

EnsembliENSSSCT00000002230; ENSSSCP00000002178; ENSSSCG00000001992.
GeneIDi100049679.
KEGGissc:100049679.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB271949 mRNA. Translation: BAF62324.1 .
RefSeqi NP_001092063.1. NM_001098593.1.
XP_005666280.1. XM_005666223.1.
UniGenei Ssc.45681.

3D structure databases

ProteinModelPortali A5A779.
SMRi A5A779. Positions 2-567.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9823.ENSSSCP00000002178.

Proteomic databases

PaxDbi A5A779.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSSSCT00000002230 ; ENSSSCP00000002178 ; ENSSSCG00000001992 .
GeneIDi 100049679.
KEGGi ssc:100049679.

Organism-specific databases

CTDi 5875.

Phylogenomic databases

eggNOGi COG5536.
GeneTreei ENSGT00550000075121.
HOGENOMi HOG000007845.
HOVERGENi HBG002171.
KOi K14050.
OMAi WNCRREV.
OrthoDBi EOG7PP56C.
TreeFami TF315057.

Family and domain databases

Gene3Di 2.60.40.1130. 1 hit.
InterProi IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR002088. Prenyl_trans_a.
IPR009087. RabGGT_asu_insert-domain.
[Graphical view ]
Pfami PF00560. LRR_1. 1 hit.
PF12799. LRR_4. 1 hit.
PF01239. PPTA. 5 hits.
PF07711. RabGGT_insert. 1 hit.
[Graphical view ]
ProDomi PD331837. RabGG_trans_A. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF49594. SSF49594. 1 hit.
PROSITEi PS51147. PFTA. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Sequences and genetic variations of fourty-four porcine coat color related genes."
    Okumura N., Matsumoto T., Hamasima N., Uenishi H., Ogawa T., Komatsuda A., Fukudome N., Ide H., Suzuki A., Kojima C., Awata T.
    Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiPGTA_PIG
AccessioniPrimary (citable) accession number: A5A779
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 51 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

External Data

Dasty 3

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