PR1B1_ARATH
ID PR1B1_ARATH Reviewed; 209 AA.
AC Q9LYN0; Q940J2;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=PRA1 family protein B1;
DE Short=AtPRA1.B1;
DE AltName: Full=Prenylated Rab acceptor 6;
GN Name=PRA1B1; Synonyms=PRA6; OrderedLocusNames=At3g56110;
GN ORFNames=F18O21.70;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Pay A., Nagy F., Merkle T.;
RT "Isolation and characterization of members of a new protein family from
RT Arabidopsis thaliana that specifically interact with prenylated Rab
RT proteins and SNAREs.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH PRA1B2; PRA1B3; PRA1B4;
RP PRA1B5; PRA1B6 AND PRA1E, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18583532; DOI=10.1104/pp.108.122226;
RA Alvim Kamei C.L., Boruc J., Vandepoele K., Van den Daele H., Maes S.,
RA Russinova E., Inze D., de Veylder L.;
RT "The PRA1 gene family in Arabidopsis.";
RL Plant Physiol. 147:1735-1749(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: May be involved in both secretory and endocytic intracellular
CC trafficking in the endosomal/prevacuolar compartments. {ECO:0000250}.
CC -!- SUBUNIT: Can form homodimer. Interacts with PRA1B2, PRA1B3, PRA1B4,
CC PRA1B5, PRA1B6 and PRA1E. {ECO:0000269|PubMed:18583532}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:18583532};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18583532}.
CC -!- SIMILARITY: Belongs to the PRA1 family. {ECO:0000305}.
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DR EMBL; AJ249560; CAC80650.1; -; mRNA.
DR EMBL; AL163763; CAB87410.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79478.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79479.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65409.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65410.1; -; Genomic_DNA.
DR EMBL; AY054569; AAK96760.1; -; mRNA.
DR EMBL; AY064659; AAL47368.1; -; mRNA.
DR EMBL; AY084557; AAM61124.1; -; mRNA.
DR PIR; T47728; T47728.
DR RefSeq; NP_001190100.1; NM_001203171.2.
DR RefSeq; NP_001319766.1; NM_001339767.1.
DR RefSeq; NP_001327380.1; NM_001339768.1.
DR RefSeq; NP_191170.1; NM_115469.3.
DR AlphaFoldDB; Q9LYN0; -.
DR BioGRID; 10093; 3.
DR IntAct; Q9LYN0; 3.
DR STRING; 3702.AT3G56110.1; -.
DR TCDB; 9.A.49.1.4; the prenylated rab acceptor protein 1 (pra1) family.
DR iPTMnet; Q9LYN0; -.
DR PaxDb; Q9LYN0; -.
DR PRIDE; Q9LYN0; -.
DR ProteomicsDB; 226499; -.
DR EnsemblPlants; AT3G56110.1; AT3G56110.1; AT3G56110.
DR EnsemblPlants; AT3G56110.2; AT3G56110.2; AT3G56110.
DR EnsemblPlants; AT3G56110.3; AT3G56110.3; AT3G56110.
DR EnsemblPlants; AT3G56110.4; AT3G56110.4; AT3G56110.
DR GeneID; 824777; -.
DR Gramene; AT3G56110.1; AT3G56110.1; AT3G56110.
DR Gramene; AT3G56110.2; AT3G56110.2; AT3G56110.
DR Gramene; AT3G56110.3; AT3G56110.3; AT3G56110.
DR Gramene; AT3G56110.4; AT3G56110.4; AT3G56110.
DR KEGG; ath:AT3G56110; -.
DR Araport; AT3G56110; -.
DR TAIR; locus:2078371; AT3G56110.
DR eggNOG; KOG3142; Eukaryota.
DR HOGENOM; CLU_060198_1_0_1; -.
DR InParanoid; Q9LYN0; -.
DR OMA; MRRPPIQ; -.
DR OrthoDB; 1344798at2759; -.
DR PhylomeDB; Q9LYN0; -.
DR PRO; PR:Q9LYN0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LYN0; baseline and differential.
DR Genevisible; Q9LYN0; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA:TAIR.
DR InterPro; IPR004895; Prenylated_rab_accept_PRA1.
DR PANTHER; PTHR19317; PTHR19317; 1.
DR Pfam; PF03208; PRA1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endosome; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..209
FT /note="PRA1 family protein B1"
FT /id="PRO_0000352250"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 18
FT /note="Q -> R (in Ref. 4; AAK96760/AAL47368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 209 AA; 22618 MW; 867E6FD58C39BADC CRC64;
MATPPTLPVT NQQAVQSQPP INTPAFRTFF SRLSTSIRDG LSQRRPWTEL IDRSSMARPE
SLTDALSRIR KNLAYFKVNY VAIVSLVLAF SLFSHPLSLL VLIGLLGGWM FLYLFRPSDQ
PLVVFGRTFS DRETLLALVL STIVVVFMTS VGSLLTSALM IGVAIVCVHG AFVVPDDLFL
DEQEPANAGL LSFLGGSATS AAAAVSGRV
