PRAF1_MOUSE
ID PRAF1_MOUSE Reviewed; 185 AA.
AC Q9Z0S9; Q3TDB4;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Prenylated Rab acceptor protein 1;
DE AltName: Full=PRA1 family protein 1;
DE AltName: Full=Prenylin;
GN Name=Rabac1; Synonyms=Pra, Pra1, Praf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10964695; DOI=10.1006/bbrc.2000.3316;
RA Liang Z., Li G.;
RT "Mouse prenylated Rab acceptor is a novel Golgi membrane protein.";
RL Biochem. Biophys. Res. Commun. 275:509-516(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=B-cell lymphoma;
RA Behrend E.N., Kemppainen R.J.;
RT "Specific interaction of Dexras with prenylated rab acceptor 1 (PRA1).";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Small intestine, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-36 AND 73-104, AND INTERACTION WITH RAB5
RP AND RAB6.
RX PubMed=7782346; DOI=10.1074/jbc.270.24.14801;
RA Janoueix-Lerosey I., Jollivet F., Camonis J., Marche P.N., Goud B.;
RT "Two-hybrid system screen with the small GTP-binding protein Rab6.
RT Identification of a novel mouse GDP dissociation inhibitor isoform and two
RT other potential partners of Rab6.";
RL J. Biol. Chem. 270:14801-14808(1995).
RN [6]
RP FUNCTION, INTERACTION WITH MEMBERS OF RAS SUPERFAMILY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11335720; DOI=10.1074/jbc.m101763200;
RA Figueroa C., Taylor J., Vojtek A.B.;
RT "Prenylated Rab acceptor protein is a receptor for prenylated small
RT GTPases.";
RL J. Biol. Chem. 276:28219-28225(2001).
RN [7]
RP TOPOLOGY.
RX PubMed=11535589; DOI=10.1074/jbc.m103475200;
RA Lin J., Liang Z., Zhang Z., Li G.;
RT "Membrane topography and topogenesis of prenylated Rab acceptor (PRA1).";
RL J. Biol. Chem. 276:41733-41741(2001).
RN [8]
RP SUBCELLULAR LOCATION, HOMODIMERIZATION, AND MUTAGENESIS OF ASP-176;
RP GLY-177; GLU-178; GLU-179 AND VAL-185.
RX PubMed=14979871; DOI=10.1042/bj20031788;
RA Liang Z., Veeraprame H., Bayan N., Li G.;
RT "The C-terminus of prenylin is important in forming a dimer conformation
RT necessary for endoplasmic-reticulum-to-Golgi transport.";
RL Biochem. J. 380:43-49(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:11335720}.
CC -!- SUBUNIT: Homodimer. Interacts with VAMP2 (synaptobrevin-2), GDI1, NRDG1
CC and PCLO (By similarity). Interacts with prenylated Rab proteins
CC (including RAB5 and RAB6), and with the members of the Ras superfamily
CC HRAS, RHOA, TC21, and RAP1A. {ECO:0000250, ECO:0000269|PubMed:11335720,
CC ECO:0000269|PubMed:7782346}.
CC -!- INTERACTION:
CC Q9Z0S9; P01112: HRAS; Xeno; NbExp=4; IntAct=EBI-476965, EBI-350145;
CC Q9Z0S9; P61586: RHOA; Xeno; NbExp=2; IntAct=EBI-476965, EBI-446668;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O35394};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000250|UniProtKB:O35394}. Golgi apparatus
CC {ECO:0000250|UniProtKB:O35394}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle {ECO:0000250|UniProtKB:O35394}. Note=According to
CC PubMed:11535589, it is an integral membrane protein, while other
CC authors showed that it is cytoplasmic and membrane-associated to Golgi
CC and synaptic vesicles. {ECO:0000250|UniProtKB:O35394}.
CC -!- SIMILARITY: Belongs to the PRA1 family. {ECO:0000305}.
CC -!- CAUTION: Interaction with the Ras-like GTPases failed to be confirmed
CC in other species. {ECO:0000305}.
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DR EMBL; AF252856; AAF68476.1; -; mRNA.
DR EMBL; AF120162; AAD17296.1; -; mRNA.
DR EMBL; AK008559; BAB25744.1; -; mRNA.
DR EMBL; AK009726; BAB26465.1; -; mRNA.
DR EMBL; AK150681; BAE29761.1; -; mRNA.
DR EMBL; AK170289; BAE41689.1; -; mRNA.
DR EMBL; BC008242; AAH08242.1; -; mRNA.
DR CCDS; CCDS20968.1; -.
DR PIR; JC7369; JC7369.
DR RefSeq; NP_034391.1; NM_010261.2.
DR AlphaFoldDB; Q9Z0S9; -.
DR BioGRID; 199848; 2.
DR IntAct; Q9Z0S9; 45.
DR STRING; 10090.ENSMUSP00000076227; -.
DR iPTMnet; Q9Z0S9; -.
DR PhosphoSitePlus; Q9Z0S9; -.
DR EPD; Q9Z0S9; -.
DR MaxQB; Q9Z0S9; -.
DR PaxDb; Q9Z0S9; -.
DR PeptideAtlas; Q9Z0S9; -.
DR PRIDE; Q9Z0S9; -.
DR ProteomicsDB; 289393; -.
DR Antibodypedia; 30866; 64 antibodies from 23 providers.
DR DNASU; 14470; -.
DR Ensembl; ENSMUST00000076961; ENSMUSP00000076227; ENSMUSG00000003380.
DR GeneID; 14470; -.
DR KEGG; mmu:14470; -.
DR UCSC; uc009frd.1; mouse.
DR CTD; 10567; -.
DR MGI; MGI:1201692; Rabac1.
DR VEuPathDB; HostDB:ENSMUSG00000003380; -.
DR eggNOG; KOG3142; Eukaryota.
DR GeneTree; ENSGT00390000010549; -.
DR HOGENOM; CLU_103851_0_2_1; -.
DR InParanoid; Q9Z0S9; -.
DR OMA; AAFGCHK; -.
DR OrthoDB; 1344798at2759; -.
DR PhylomeDB; Q9Z0S9; -.
DR TreeFam; TF324857; -.
DR BioGRID-ORCS; 14470; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Rabac1; mouse.
DR PRO; PR:Q9Z0S9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9Z0S9; protein.
DR Bgee; ENSMUSG00000003380; Expressed in choroid plexus of fourth ventricle and 251 other tissues.
DR ExpressionAtlas; Q9Z0S9; baseline and differential.
DR Genevisible; Q9Z0S9; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
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:MGI.
DR GO; GO:0070064; F:proline-rich region binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
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_0000220879"
FT TOPO_DOM 1..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:11535589"
FT TRANSMEM 79..94
FT /note="Helical"
FT TRANSMEM 95..112
FT /note="Helical"
FT TOPO_DOM 113..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:11535589"
FT TRANSMEM 132..148
FT /note="Helical"
FT TRANSMEM 149..165
FT /note="Helical"
FT TOPO_DOM 166..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:11535589"
FT REGION 30..54
FT /note="Required for interaction with prenylated RAB3A and
FT VAMP2"
FT /evidence="ECO:0000250"
FT REGION 165..185
FT /note="Required for interaction with GDI1"
FT /evidence="ECO:0000250"
FT REGION 175..185
FT /note="Homodimerization"
FT REGION 175..185
FT /note="Required for interaction with prenylated RAB3A and
FT VAMP2"
FT /evidence="ECO:0000250"
FT MUTAGEN 176
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:14979871"
FT MUTAGEN 177
FT /note="G->A: No effect."
FT /evidence="ECO:0000269|PubMed:14979871"
FT MUTAGEN 178
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:14979871"
FT MUTAGEN 179
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:14979871"
FT MUTAGEN 185
FT /note="V->A,C,I,P: Partial retention in the endoplasmic
FT reticulum."
FT /evidence="ECO:0000269|PubMed:14979871"
FT MUTAGEN 185
FT /note="V->D,K: Retention in the endoplasmic reticulum; does
FT not form homodimers."
FT /evidence="ECO:0000269|PubMed:14979871"
FT MUTAGEN 185
FT /note="V->M,N,Y,H,E,Q,T,S,L,W,F,G: Retention in the
FT endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:14979871"
FT MUTAGEN 185
FT /note="V->R: No effect."
FT /evidence="ECO:0000269|PubMed:14979871"
FT MUTAGEN 185
FT /note="Missing: Partial retention in the endoplasmic
FT reticulum; still forms homodimers."
FT /evidence="ECO:0000269|PubMed:14979871"
SQ SEQUENCE 185 AA; 20619 MW; 86C82C0502B5CB5B CRC64;
MAAQKDQQKD AEGEGLSATT LLPKLIPSGA GREWLERRRA TIRPWGTFVD QQRFSRPRNV
GELCQRLVRN VEYYQSNYVF VFLGLILYCV VTSPMLLVAL AVFFGACYIL YLRTLQSKLV
LFGREVSPAH QYALAGGVSF PFFWLAGAGS AVFWVLGATL VLIGSHAAFH QMEPADGEEL
QMEPV
