PRAF1_HUMAN
ID PRAF1_HUMAN Reviewed; 185 AA.
AC Q9UI14; Q7Z4Y2; Q9Y3R1;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Prenylated Rab acceptor protein 1;
DE AltName: Full=PRA1 family protein 1;
GN Name=RABAC1; Synonyms=PRA1, PRAF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RAB GTPASES, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Brain, and Placenta;
RX PubMed=10329441; DOI=10.1006/bbrc.1999.0651;
RA Bucci C., Chiariello M., Lattero D., Maiorano M., Bruni C.B.;
RT "Interaction cloning and characterization of the cDNA encoding the human
RT prenylated rab acceptor (PRA1).";
RL Biochem. Biophys. Res. Commun. 258:657-662(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hypothalamus;
RA Jin W., Huang C., Wu T., Peng Y., Gu Y., Zhang L., Jiang C., Li Y., Han Z.,
RA Wang Y., Chen Z., Fu G.;
RT "A novel gene expressed in human hypothalamus.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Fu Q., Yu L., Yue P., Dai F.Y., Wang X.K., Zhao S.Y.;
RT "Cloning and characterization of a new human cDNA homologous to Rattus
RT norvegicus prenylated rab acceptor 1 (PRA1) mRNA.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11520070; DOI=10.1006/bbrc.2001.5466;
RA Bucci C., De Gregorio L., Bruni C.B.;
RT "Expression analysis and chromosomal assignment of PRA1 and RILP genes.";
RL Biochem. Biophys. Res. Commun. 286:815-819(2001).
RN [8]
RP INTERACTION WITH NDRG1.
RX PubMed=15922294; DOI=10.1016/j.bbrc.2005.05.050;
RA Hunter M., Angelicheva D., Tournev I., Ingley E., Chan D.C., Watts G.F.,
RA Kremensky I., Kalaydjieva L.;
RT "NDRG1 interacts with APO A-I and A-II and is a functional candidate for
RT the HDL-C QTL on 8q24.";
RL Biochem. Biophys. Res. Commun. 332:982-992(2005).
RN [9]
RP NOMENCLATURE.
RX PubMed=16481131; DOI=10.1016/j.gene.2005.12.009;
RA Fo C.S., Coleman C.S., Wallick C.J., Vine A.L., Bachmann A.S.;
RT "Genomic organization, expression profile, and characterization of the new
RT protein PRA1 domain family, member 2 (PRAF2).";
RL Gene 371:154-165(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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 GDI.
CC {ECO:0000250|UniProtKB:O35394}.
CC -!- SUBUNIT: Homodimer. Interacts with VAMP2 (synaptobrevin-2), GDI1, and
CC PCLO (By similarity). Interacts specifically with prenylated Rab
CC proteins; strongly with RAB4B, RAB5A and RAB5C, and weakly with RAB4A,
CC RAB6, RAB7A, RAB17 and RAB22. Interacts with NDRG1. {ECO:0000250,
CC ECO:0000269|PubMed:10329441, ECO:0000269|PubMed:15922294}.
CC -!- INTERACTION:
CC Q9UI14; Q8TB40: ABHD4; NbExp=3; IntAct=EBI-712367, EBI-7131019;
CC Q9UI14; O95873: C6orf47; NbExp=3; IntAct=EBI-712367, EBI-719613;
CC Q9UI14; Q8NI60: COQ8A; NbExp=12; IntAct=EBI-712367, EBI-745535;
CC Q9UI14; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-712367, EBI-17233035;
CC Q9UI14; Q53TN4: CYBRD1; NbExp=3; IntAct=EBI-712367, EBI-8637742;
CC Q9UI14; Q9UNI6: DUSP12; NbExp=7; IntAct=EBI-712367, EBI-715161;
CC Q9UI14; O14681: EI24; NbExp=3; IntAct=EBI-712367, EBI-2339413;
CC Q9UI14; P54849: EMP1; NbExp=3; IntAct=EBI-712367, EBI-4319440;
CC Q9UI14; Q9Y624: F11R; NbExp=3; IntAct=EBI-712367, EBI-742600;
CC Q9UI14; P51114: FXR1; NbExp=2; IntAct=EBI-712367, EBI-713291;
CC Q9UI14; P51116: FXR2; NbExp=3; IntAct=EBI-712367, EBI-740459;
CC Q9UI14; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-712367, EBI-13345167;
CC Q9UI14; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-712367, EBI-18053395;
CC Q9UI14; Q9Y2U8: LEMD3; NbExp=3; IntAct=EBI-712367, EBI-2561428;
CC Q9UI14; P36941: LTBR; NbExp=3; IntAct=EBI-712367, EBI-3509981;
CC Q9UI14; Q96C03: MIEF2; NbExp=3; IntAct=EBI-712367, EBI-750153;
CC Q9UI14; Q96C03-3: MIEF2; NbExp=3; IntAct=EBI-712367, EBI-11988931;
CC Q9UI14; Q9UN36-1: NDRG2; NbExp=7; IntAct=EBI-712367, EBI-8084503;
CC Q9UI14; Q9ULP0: NDRG4; NbExp=3; IntAct=EBI-712367, EBI-10323810;
CC Q9UI14; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-712367, EBI-11978907;
CC Q9UI14; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-712367, EBI-740897;
CC Q9UI14; Q96HA8: NTAQ1; NbExp=9; IntAct=EBI-712367, EBI-741158;
CC Q9UI14; Q6ZVK8: NUDT18; NbExp=3; IntAct=EBI-712367, EBI-740486;
CC Q9UI14; Q96AL5: PBX3; NbExp=5; IntAct=EBI-712367, EBI-741171;
CC Q9UI14; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-712367, EBI-742388;
CC Q9UI14; Q14088: RAB33A; NbExp=3; IntAct=EBI-712367, EBI-744685;
CC Q9UI14; Q9UI14: RABAC1; NbExp=6; IntAct=EBI-712367, EBI-712367;
CC Q9UI14; Q9BRK0: REEP2; NbExp=3; IntAct=EBI-712367, EBI-11337973;
CC Q9UI14; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-712367, EBI-10192441;
CC Q9UI14; Q9NPQ8-4: RIC8A; NbExp=3; IntAct=EBI-712367, EBI-9091816;
CC Q9UI14; Q99942: RNF5; NbExp=3; IntAct=EBI-712367, EBI-348482;
CC Q9UI14; A8MRB1: S100B; NbExp=3; IntAct=EBI-712367, EBI-16432654;
CC Q9UI14; Q8IVP1: SH3GL3; NbExp=3; IntAct=EBI-712367, EBI-6503765;
CC Q9UI14; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-712367, EBI-2623095;
CC Q9UI14; Q96DU3: SLAMF6; NbExp=3; IntAct=EBI-712367, EBI-14058448;
CC Q9UI14; P37840: SNCA; NbExp=4; IntAct=EBI-712367, EBI-985879;
CC Q9UI14; Q13596: SNX1; NbExp=3; IntAct=EBI-712367, EBI-2822329;
CC Q9UI14; Q8N5Z3: SNX10; NbExp=3; IntAct=EBI-712367, EBI-10266928;
CC Q9UI14; Q9Y5X0: SNX10; NbExp=3; IntAct=EBI-712367, EBI-10329478;
CC Q9UI14; Q9Y5W9: SNX11; NbExp=6; IntAct=EBI-712367, EBI-10329449;
CC Q9UI14; Q9NRS6: SNX15; NbExp=4; IntAct=EBI-712367, EBI-725924;
CC Q9UI14; Q15036: SNX17; NbExp=3; IntAct=EBI-712367, EBI-1752620;
CC Q9UI14; Q9Y5X2: SNX8; NbExp=3; IntAct=EBI-712367, EBI-1752557;
CC Q9UI14; Q9NZD8: SPG21; NbExp=7; IntAct=EBI-712367, EBI-742688;
CC Q9UI14; Q9UNL2: SSR3; NbExp=3; IntAct=EBI-712367, EBI-1043938;
CC Q9UI14; Q13586: STIM1; NbExp=3; IntAct=EBI-712367, EBI-448878;
CC Q9UI14; Q9UJZ1: STOML2; NbExp=3; IntAct=EBI-712367, EBI-1044428;
CC Q9UI14; Q17RD7: SYT16; NbExp=8; IntAct=EBI-712367, EBI-10238936;
CC Q9UI14; Q12893: TMEM115; NbExp=3; IntAct=EBI-712367, EBI-8633987;
CC Q9UI14; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-712367, EBI-8638294;
CC Q9UI14; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-712367, EBI-12038591;
CC Q9UI14; Q9Y320: TMX2; NbExp=3; IntAct=EBI-712367, EBI-6447886;
CC Q9UI14; Q13049: TRIM32; NbExp=10; IntAct=EBI-712367, EBI-742790;
CC Q9UI14; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-712367, EBI-10180829;
CC Q9UI14; Q9Y4P8: WIPI2; NbExp=3; IntAct=EBI-712367, EBI-719396;
CC Q9UI14; Q9Y4P8-4: WIPI2; NbExp=3; IntAct=EBI-712367, EBI-12205107;
CC Q9UI14; Q9BQ24: ZFYVE21; NbExp=6; IntAct=EBI-712367, EBI-2849569;
CC Q9UI14; P03230: LMP1; Xeno; NbExp=9; IntAct=EBI-712367, EBI-6973030;
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 some
CC authors, it is an integral membrane protein, while others showed that
CC it is cytoplasmic and membrane-associated to Golgi and synaptic
CC vesicles. {ECO:0000250|UniProtKB:O35394}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Strongest expression found in placenta,
CC pituitary gland, kidney, lung and stomach.
CC {ECO:0000269|PubMed:11520070}.
CC -!- DEVELOPMENTAL STAGE: In fetal tissues, it is more abundant in kidney
CC and lung. {ECO:0000269|PubMed:11520070}.
CC -!- SIMILARITY: Belongs to the PRA1 family. {ECO:0000305}.
CC -!- CAUTION: In contrast to the mouse ortholog, it does not interact with
CC Ras. {ECO:0000305}.
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DR EMBL; AJ133534; CAB43107.1; -; mRNA.
DR EMBL; AF112202; AAF17190.1; -; mRNA.
DR EMBL; AF112996; AAP97229.1; -; mRNA.
DR EMBL; CR457214; CAG33495.1; -; mRNA.
DR EMBL; CR542116; CAG46913.1; -; mRNA.
DR EMBL; BT019964; AAV38767.1; -; mRNA.
DR EMBL; BC008950; AAH08950.1; -; mRNA.
DR CCDS; CCDS12593.1; -.
DR RefSeq; NP_006414.2; NM_006423.2.
DR AlphaFoldDB; Q9UI14; -.
DR BioGRID; 115818; 132.
DR IntAct; Q9UI14; 89.
DR MINT; Q9UI14; -.
DR STRING; 9606.ENSP00000222008; -.
DR TCDB; 9.A.49.1.1; the prenylated rab acceptor protein 1 (pra1) family.
DR iPTMnet; Q9UI14; -.
DR PhosphoSitePlus; Q9UI14; -.
DR BioMuta; RABAC1; -.
DR DMDM; 56404978; -.
DR EPD; Q9UI14; -.
DR jPOST; Q9UI14; -.
DR MassIVE; Q9UI14; -.
DR MaxQB; Q9UI14; -.
DR PaxDb; Q9UI14; -.
DR PeptideAtlas; Q9UI14; -.
DR PRIDE; Q9UI14; -.
DR ProteomicsDB; 84453; -.
DR TopDownProteomics; Q9UI14; -.
DR Antibodypedia; 30866; 64 antibodies from 23 providers.
DR DNASU; 10567; -.
DR Ensembl; ENST00000222008.11; ENSP00000222008.5; ENSG00000105404.11.
DR GeneID; 10567; -.
DR KEGG; hsa:10567; -.
DR MANE-Select; ENST00000222008.11; ENSP00000222008.5; NM_006423.3; NP_006414.2.
DR UCSC; uc002osf.4; human.
DR CTD; 10567; -.
DR DisGeNET; 10567; -.
DR GeneCards; RABAC1; -.
DR HGNC; HGNC:9794; RABAC1.
DR HPA; ENSG00000105404; Low tissue specificity.
DR MIM; 604925; gene.
DR neXtProt; NX_Q9UI14; -.
DR OpenTargets; ENSG00000105404; -.
DR PharmGKB; PA34155; -.
DR VEuPathDB; HostDB:ENSG00000105404; -.
DR eggNOG; KOG3142; Eukaryota.
DR GeneTree; ENSGT00390000010549; -.
DR HOGENOM; CLU_103851_0_2_1; -.
DR InParanoid; Q9UI14; -.
DR OMA; AAFGCHK; -.
DR OrthoDB; 1344798at2759; -.
DR PhylomeDB; Q9UI14; -.
DR TreeFam; TF324857; -.
DR PathwayCommons; Q9UI14; -.
DR SignaLink; Q9UI14; -.
DR BioGRID-ORCS; 10567; 16 hits in 1077 CRISPR screens.
DR GeneWiki; RABAC1; -.
DR GenomeRNAi; 10567; -.
DR Pharos; Q9UI14; Tbio.
DR PRO; PR:Q9UI14; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9UI14; protein.
DR Bgee; ENSG00000105404; Expressed in thoracic aorta and 95 other tissues.
DR ExpressionAtlas; Q9UI14; baseline and differential.
DR Genevisible; Q9UI14; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
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; IPI:IntAct.
DR GO; GO:0070064; F:proline-rich region binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
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_0000220878"
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 /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 /evidence="ECO:0000250"
FT REGION 175..185
FT /note="Required for interaction with prenylated RAB3A and
FT VAMP2"
FT /evidence="ECO:0000250"
FT CONFLICT 2
FT /note="Missing (in Ref. 3; AAP97229)"
FT /evidence="ECO:0000305"
FT CONFLICT 40..41
FT /note="AT -> GP (in Ref. 3; AAP97229)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="A -> E (in Ref. 1; CAB43107)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 185 AA; 20648 MW; A85BD5BDCF6C23E4 CRC64;
MAAQKDQQKD AEAEGLSGTT LLPKLIPSGA GREWLERRRA TIRPWSTFVD QQRFSRPRNL
GELCQRLVRN VEYYQSNYVF VFLGLILYCV VTSPMLLVAL AVFFGACYIL YLRTLESKLV
LFGREVSPAH QYALAGGISF PFFWLAGAGS AVFWVLGATL VVIGSHAAFH QIEAVDGEEL
QMEPV
