Reviewed, UniProtKB/Swiss-Prot O35394 (PRAF1_RAT)

Names and origin

Protein names

Recommended name:
    Prenylated Rab acceptor protein 1
Alternative name(s):
    PRA1 family protein 1

Gene names

Name:	Rabac1
Synonyms:	Pra1, Praf1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	185 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
Subcellular location	Cell membrane; Multi-pass membrane protein. Cytoplasm. Golgi apparatus. Cytoplasmic vesicle › secretory vesicle › synaptic 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.5 Ref.6
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.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cytoplasm Cytoplasmic vesicle Golgi apparatus Membrane Synapse
Domain	Transmembrane
Gene Ontology (GO)
Biological process	vesicle-mediated transport Ref.1 Non-traceable author statement. Source: RGD
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell cell junction Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell synaptic vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding, bridging Ref.1 Non-traceable author statement. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Rab3a	P63012	1	EBI-2028510,EBI-440126
Vamp2	P63045	1	EBI-2028510,EBI-520880

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 185	185	Prenylated Rab acceptor protein 1		PRO_0000220880
Regions
	Topological domain	1 – 78	78	Cytoplasmic By similarity
	Transmembrane	79 – 94	16	By similarity
	Transmembrane	95 – 112	18	By similarity
	Topological domain	113 – 131	19	Cytoplasmic By similarity
	Transmembrane	132 – 148	17	By similarity
	Transmembrane	149 – 165	17	By similarity
	Topological domain	166 – 185	20	Cytoplasmic By similarity
	Region	30 – 54	25	Required for interaction with prenylated RAB3A and VAMP2
	Region	165 – 185	21	Required for interaction with GDI1
	Region	175 – 185	11	Homodimerization By similarity
	Region	175 – 185	11	Required for interaction with prenylated RAB3A and VAMP2
Experimental info
	Mutagenesis	70	1	N → T: Retained in endoplasmic reticulum, no interaction with RAB3A or VAMP2. Ref.4
	Mutagenesis	73	1	Y → A: Retained in endoplasmic reticulum, Golgi and tubular structures, no interaction with RAB3A. Ref.4
	Mutagenesis	76	1	S → A or V: Increased interaction with RAB3A or VAMP2, Golgi condensation. Ref.4
	Mutagenesis	77	1	N → A: No effect. Ref.4
	Mutagenesis	78	1	Y → A: Retained in endoplasmic reticulum, no interaction with RAB3A or VAMP2. Ref.4
	Mutagenesis	154	1	W → A: No effect. Ref.4
	Mutagenesis	161	1	V → A: Increased interaction with RAB3A or VAMP2, Golgi condensation. Ref.4
	Mutagenesis	166	1	H → A: Retained in endoplasmic reticulum, Golgi and tubular structures, no interaction with RAB3A. Ref.4
	Mutagenesis	176	1	D → A: Retained in endoplasmic reticulum. Ref.5
	Mutagenesis	178	1	E → A: Retained in endoplasmic reticulum. Ref.5
	Mutagenesis	179	1	E → A: Retained in endoplasmic reticulum. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	O35394-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: DA6341AE66F5C2F0	FASTA	185	20,643
	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

References

	« Hide 'large scale' referencesShow '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
EMBLGenBankDDBJ	AF025506 mRNA. Translation: AAB81721.1. BC086387 mRNA. Translation: AAH86387.1.
IPI	IPI00208565.
RefSeq	NP_113962.1.
UniGene	Rn.25604
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O35394. 4 interactions.
STRING	O35394.
Proteomic databases
PRIDE	O35394.
Genome annotation databases
Ensembl	ENSRNOT00000027435; ENSRNOP00000027435; ENSRNOG00000020233; Rattus norvegicus. [Genome view]
GeneID	83583.
KEGG	rno:83583.
UCSC	NM_031774. rat.
Organism-specific databases
CTD	83583.
RGD	621002. Rabac1.
Phylogenomic databases
HOVERGEN	O35394.
OMA	AGGISFP.
Gene expression databases
ArrayExpress	O35394.
Genevestigator	O35394.
GermOnline	ENSRNOG00000020233. Rattus norvegicus.
Family and domain databases
InterPro	IPR004895. Prenylated_rab_accept_PRA1. [Graphical view]
Pfam	PF03208. PRA1. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	616119.

Entry information

Entry name

PRAF1_RAT

Accession

Primary (citable) accession number: O35394

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)