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Reviewed, UniProtKB/Swiss-Prot O35394 (PRAF1_RAT)

Last modified January 19, 2010. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Prenylated Rab acceptor protein 1
Alternative name(s):
    PRA1 family protein 1
Gene names
Name: Rabac1
Synonyms: Pra1, Praf1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

General Rab protein regulator required for vesicle formation from the Golgi complex. May control vesicle docking and fusion by mediating the action of Rab GTPases to the SNARE complexes. In addition it inhibits the removal of Rab GTPases from the membrane by GDI1. Ref.1 Ref.3 Ref.4

Subunit structure

Homodimers By similarity. Interacts specifically with both prenylated Rab proteins (including RAB3A and RAB1), and VAMP2 (synaptobrevin-2), in an exclusive way. Interacts with free GDI1 in the absence of Rab proteins. Also interacts with PCLO. Ref.3 Ref.6

Subcellular location

Cell membrane; Multi-pass membrane protein. Cytoplasm. Golgi apparatus. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle. Note: According to some authors, it is an integral membrane protein, while others showed that it is cytoplasmic and membrane-associated to Golgi and synaptic vesicles. Ref.3 Ref.4 Ref.6 Ref.5

Tissue specificity

Ubiquitous. Ref.1

Sequence similarities

Belongs to the PRA1 family.

Caution

In contrast to the mouse ortholog, it does not interact with the Ras-like GTPases RAC1 and RHOA.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 185185Prenylated Rab acceptor protein 1
PRO_0000220880

Regions

Topological domain1 – 7878Cytoplasmic By similarity
Transmembrane79 – 9416 By similarity
Transmembrane95 – 11218 By similarity
Topological domain113 – 13119Cytoplasmic By similarity
Transmembrane132 – 14817 By similarity
Transmembrane149 – 16517 By similarity
Topological domain166 – 18520Cytoplasmic By similarity
Region30 – 5425Required for interaction with prenylated RAB3A and VAMP2
Region165 – 18521Required for interaction with GDI1
Region175 – 18511Homodimerization By similarity
Region175 – 18511Required for interaction with prenylated RAB3A and VAMP2

Experimental info

Mutagenesis701N → T: Retained in endoplasmic reticulum, no interaction with RAB3A or VAMP2. Ref.4
Mutagenesis731Y → A: Retained in endoplasmic reticulum, Golgi and tubular structures, no interaction with RAB3A. Ref.4
Mutagenesis761S → A or V: Increased interaction with RAB3A or VAMP2, Golgi condensation. Ref.4
Mutagenesis771N → A: No effect. Ref.4
Mutagenesis781Y → A: Retained in endoplasmic reticulum, no interaction with RAB3A or VAMP2. Ref.4
Mutagenesis1541W → A: No effect. Ref.4
Mutagenesis1611V → A: Increased interaction with RAB3A or VAMP2, Golgi condensation. Ref.4
Mutagenesis1661H → A: Retained in endoplasmic reticulum, Golgi and tubular structures, no interaction with RAB3A. Ref.4
Mutagenesis1761D → A: Retained in endoplasmic reticulum. Ref.5
Mutagenesis1781E → A: Retained in endoplasmic reticulum. Ref.5
Mutagenesis1791E → A: Retained in endoplasmic reticulum. Ref.5

Sequences

Sequence LengthMass (Da)Tools
O35394-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: DA6341AE66F5C2F0

FASTA18520,643
        10         20         30         40         50         60 
MAAQKDQQKD AEVEGLSATT LLPKLIPSGA GREWLERRRA TIRPWGTFVD QQRFSRPRNV 

        70         80         90        100        110        120 
GELCQRLVRN VEYYQSNYVF VFLGLILYCV VTSPMLLVAL AVFFGACYIL YLRTLQSKLV 

       130        140        150        160        170        180 
LFGREVSPAH QYALAGGVSF PFFWLAGAGS AVFWVLGATL VLIGSHAAFH QIEPADGEEL 


QMEPV 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of a dual prenylated Rab and VAMP2 receptor."
Martincic I., Peralta M.E., Ngsee J.K.
J. Biol. Chem. 272:26991-26998(1997) [PubMed: 9341137] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.
[3]"PRA1 inhibits the extraction of membrane-bound rab GTPase by GDI1."
Hutt D.M., da Silva L.F., Chang L.-H., Prosser D.C., Ngsee J.K.
J. Biol. Chem. 275:18511-18519(2000) [PubMed: 10751420] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GDI1.
[4]"Disruption of Golgi morphology and trafficking in cells expressing mutant prenylated rab acceptor-1."
Gougeon P.-Y., Prosser D.C., Da-Silva L.F., Ngsee J.K.
J. Biol. Chem. 277:36408-36414(2002) [PubMed: 12107180] [Abstract]
Cited for: MUTAGENESIS OF ASN-70; TYR-73; SER-76; ASN-77; TYR-78; TRP-154; VAL-161 AND HIS-166, FUNCTION, SUBCELLULAR LOCATION.
[5]"PRA isoforms are targeted to distinct membrane compartments."
Abdul-Ghani M., Gougeon P.-Y., Prosser D.C., Da-Silva L.F., Ngsee J.K.
J. Biol. Chem. 276:6225-6233(2001) [PubMed: 11096102] [Abstract]
Cited for: MUTAGENESIS OF ASP-176; GLU-178 AND GLU-179, SUBCELLULAR LOCATION.
[6]"Piccolo, a presynaptic zinc finger protein structurally related to bassoon."
Fenster S.D., Chung W.J., Zhai R., Cases-Langhoff C., Voss B., Garner A.M., Kaempf U., Kindler S., Gundelfinger E.D., Garner C.C.
Neuron 25:203-214(2000) [PubMed: 10707984] [Abstract]
Cited for: INTERACTION WITH PCLO, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF025506 mRNA. Translation: AAB81721.1.
BC086387 mRNA. Translation: AAH86387.1.
IPIIPI00208565.
RefSeqNP_113962.1.
UniGeneRn.25604

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActO35394. 6 interactions.
STRINGO35394.

Proteomic databases

PRIDEO35394.

Genome annotation databases

EnsemblENSRNOT00000027435; ENSRNOP00000027435; ENSRNOG00000020233; Rattus norvegicus. [Genome view]
GeneID83583.
KEGGrno:83583.
UCSCNM_031774. rat.

Organism-specific databases

CTD83583.
RGD621002. Rabac1.

Phylogenomic databases

eggNOGmaNOG18371.
HOVERGENO35394.
InParanoidO35394.
OMAAGGISFP.
OrthoDBEOG9DV85S.
PhylomeDBO35394.

Gene expression databases

ArrayExpressO35394.
GenevestigatorO35394.
GermOnlineENSRNOG00000020233. Rattus norvegicus.

Family and domain databases

InterProIPR004895. Prenylated_rab_accept_PRA1.
[Graphical view]
PfamPF03208. PRA1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio616119.

Entry information

Entry namePRAF1_RAT
AccessionPrimary (citable) accession number: O35394
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: January 1, 1998
Last modified: January 19, 2010
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents