PRAF1_RAT
ID PRAF1_RAT Reviewed; 185 AA.
AC O35394;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Prenylated Rab acceptor protein 1;
DE AltName: Full=PRA1 family protein 1;
GN Name=Rabac1; Synonyms=Pra1, Praf1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9341137; DOI=10.1074/jbc.272.43.26991;
RA Martincic I., Peralta M.E., Ngsee J.K.;
RT "Isolation and characterization of a dual prenylated Rab and VAMP2
RT receptor.";
RL J. Biol. Chem. 272:26991-26998(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GDI1.
RX PubMed=10751420; DOI=10.1074/jbc.m909309199;
RA Hutt D.M., da Silva L.F., Chang L.-H., Prosser D.C., Ngsee J.K.;
RT "PRA1 inhibits the extraction of membrane-bound rab GTPase by GDI1.";
RL J. Biol. Chem. 275:18511-18519(2000).
RN [4]
RP MUTAGENESIS OF ASN-70; TYR-73; SER-76; ASN-77; TYR-78; TRP-154; VAL-161 AND
RP HIS-166, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12107180; DOI=10.1074/jbc.m205026200;
RA Gougeon P.-Y., Prosser D.C., Da-Silva L.F., Ngsee J.K.;
RT "Disruption of Golgi morphology and trafficking in cells expressing mutant
RT prenylated rab acceptor-1.";
RL J. Biol. Chem. 277:36408-36414(2002).
RN [5]
RP MUTAGENESIS OF ASP-176; GLU-178 AND GLU-179, AND SUBCELLULAR LOCATION.
RX PubMed=11096102; DOI=10.1074/jbc.m009073200;
RA Abdul-Ghani M., Gougeon P.-Y., Prosser D.C., Da-Silva L.F., Ngsee J.K.;
RT "PRA isoforms are targeted to distinct membrane compartments.";
RL J. Biol. Chem. 276:6225-6233(2001).
RN [6]
RP INTERACTION WITH PCLO, AND SUBCELLULAR LOCATION.
RX PubMed=10707984; DOI=10.1016/s0896-6273(00)80883-1;
RA Fenster S.D., Chung W.J., Zhai R., Cases-Langhoff C., Voss B., Garner A.M.,
RA Kaempf U., Kindler S., Gundelfinger E.D., Garner C.C.;
RT "Piccolo, a presynaptic zinc finger protein structurally related to
RT bassoon.";
RL Neuron 25:203-214(2000).
CC -!- FUNCTION: General Rab protein regulator required for vesicle formation
CC from the Golgi complex. May control vesicle docking and fusion by
CC mediating the action of Rab GTPases to the SNARE complexes. In addition
CC it inhibits the removal of Rab GTPases from the membrane by GDI1.
CC {ECO:0000269|PubMed:10751420, ECO:0000269|PubMed:12107180,
CC ECO:0000269|PubMed:9341137}.
CC -!- SUBUNIT: Homodimers (By similarity). Interacts specifically with both
CC prenylated Rab proteins (including RAB3A and RAB1), and VAMP2
CC (synaptobrevin-2), in an exclusive way. Interacts with NDRG1 (By
CC similarity). Interacts with free GDI1 in the absence of Rab proteins.
CC Also interacts with PCLO. {ECO:0000250, ECO:0000269|PubMed:10707984,
CC ECO:0000269|PubMed:10751420}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10751420};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000269|PubMed:10751420}. Golgi apparatus
CC {ECO:0000269|PubMed:10751420, ECO:0000269|PubMed:11096102,
CC ECO:0000269|PubMed:12107180}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle {ECO:0000269|PubMed:10707984}. Note=According to some
CC authors, it is an integral membrane protein, while others showed that
CC it is cytoplasmic and membrane-associated to Golgi (PubMed:10751420,
CC PubMed:12107180, PubMed:11096102) and synaptic vesicles
CC (PubMed:10707984). {ECO:0000269|PubMed:10707984,
CC ECO:0000269|PubMed:10751420, ECO:0000269|PubMed:11096102,
CC ECO:0000269|PubMed:12107180}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9341137}.
CC -!- SIMILARITY: Belongs to the PRA1 family. {ECO:0000305}.
CC -!- CAUTION: In contrast to the mouse ortholog, it does not interact with
CC the Ras-like GTPases RAC1 and RHOA. {ECO:0000305}.
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DR EMBL; AF025506; AAB81721.1; -; mRNA.
DR EMBL; BC086387; AAH86387.1; -; mRNA.
DR RefSeq; NP_113962.1; NM_031774.1.
DR AlphaFoldDB; O35394; -.
DR IntAct; O35394; 2.
DR STRING; 10116.ENSRNOP00000027435; -.
DR PaxDb; O35394; -.
DR Ensembl; ENSRNOT00000027435; ENSRNOP00000027435; ENSRNOG00000020233.
DR GeneID; 83583; -.
DR KEGG; rno:83583; -.
DR UCSC; RGD:621002; rat.
DR CTD; 10567; -.
DR RGD; 621002; Rabac1.
DR eggNOG; KOG3142; Eukaryota.
DR GeneTree; ENSGT00390000010549; -.
DR HOGENOM; CLU_103851_0_2_1; -.
DR InParanoid; O35394; -.
DR OMA; AAFGCHK; -.
DR OrthoDB; 1344798at2759; -.
DR PhylomeDB; O35394; -.
DR TreeFam; TF324857; -.
DR PRO; PR:O35394; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020233; Expressed in pancreas and 20 other tissues.
DR Genevisible; O35394; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0070064; F:proline-rich region binding; IPI:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; NAS:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; NAS:RGD.
DR InterPro; IPR004895; Prenylated_rab_accept_PRA1.
DR PANTHER; PTHR19317; PTHR19317; 1.
DR Pfam; PF03208; PRA1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..185
FT /note="Prenylated Rab acceptor protein 1"
FT /id="PRO_0000220880"
FT TOPO_DOM 1..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 79..94
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 95..112
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 113..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 132..148
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 149..165
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 166..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 30..54
FT /note="Required for interaction with prenylated RAB3A and
FT VAMP2"
FT REGION 165..185
FT /note="Required for interaction with GDI1"
FT /evidence="ECO:0000269|PubMed:10751420"
FT REGION 175..185
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 175..185
FT /note="Required for interaction with prenylated RAB3A and
FT VAMP2"
FT MUTAGEN 70
FT /note="N->T: Retained in endoplasmic reticulum, no
FT interaction with RAB3A or VAMP2."
FT /evidence="ECO:0000269|PubMed:12107180"
FT MUTAGEN 73
FT /note="Y->A: Retained in endoplasmic reticulum, Golgi and
FT tubular structures, no interaction with RAB3A."
FT /evidence="ECO:0000269|PubMed:12107180"
FT MUTAGEN 76
FT /note="S->A,V: Increased interaction with RAB3A or VAMP2,
FT Golgi condensation."
FT /evidence="ECO:0000269|PubMed:12107180"
FT MUTAGEN 77
FT /note="N->A: No effect."
FT /evidence="ECO:0000269|PubMed:12107180"
FT MUTAGEN 78
FT /note="Y->A: Retained in endoplasmic reticulum, no
FT interaction with RAB3A or VAMP2."
FT /evidence="ECO:0000269|PubMed:12107180"
FT MUTAGEN 154
FT /note="W->A: No effect."
FT /evidence="ECO:0000269|PubMed:12107180"
FT MUTAGEN 161
FT /note="V->A: Increased interaction with RAB3A or VAMP2,
FT Golgi condensation."
FT /evidence="ECO:0000269|PubMed:12107180"
FT MUTAGEN 166
FT /note="H->A: Retained in endoplasmic reticulum, Golgi and
FT tubular structures, no interaction with RAB3A."
FT /evidence="ECO:0000269|PubMed:12107180"
FT MUTAGEN 176
FT /note="D->A: Retained in endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:11096102"
FT MUTAGEN 178
FT /note="E->A: Retained in endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:11096102"
FT MUTAGEN 179
FT /note="E->A: Retained in endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:11096102"
SQ SEQUENCE 185 AA; 20643 MW; DA6341AE66F5C2F0 CRC64;
MAAQKDQQKD AEVEGLSATT LLPKLIPSGA GREWLERRRA TIRPWGTFVD QQRFSRPRNV
GELCQRLVRN VEYYQSNYVF VFLGLILYCV VTSPMLLVAL AVFFGACYIL YLRTLQSKLV
LFGREVSPAH QYALAGGVSF PFFWLAGAGS AVFWVLGATL VLIGSHAAFH QIEPADGEEL
QMEPV
