PR1B6_ARATH
ID PR1B6_ARATH Reviewed; 216 AA.
AC Q9LYQ4;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=PRA1 family protein B6;
DE Short=AtPRA1.B6;
DE AltName: Full=Prenylated Rab acceptor 3;
GN Name=PRA1B6; Synonyms=PRA3; OrderedLocusNames=At5g07110;
GN ORFNames=T28J14.50;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
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 [5]
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 [6]
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 [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PRA1B1; PRA1B2;
RP PRA1B3; PRA1B4; PRA1B5 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 [8]
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: Interacts with PRA1B1, PRA1B2, PRA1B3, PRA1B4, PRA1B5 and
CC PRA1E. {ECO:0000269|PubMed:18583532}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18583532}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18583532}.
CC -!- TISSUE SPECIFICITY: Expressed in hypocotyls, roots, lateral roots,
CC lateral root caps, columella cells, leaves and stomata.
CC {ECO:0000269|PubMed:18583532}.
CC -!- SIMILARITY: Belongs to the PRA1 family. {ECO:0000305}.
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DR EMBL; AJ249728; CAC80646.1; -; mRNA.
DR EMBL; AB010697; BAB11169.1; -; Genomic_DNA.
DR EMBL; AL163652; CAB87267.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91111.1; -; Genomic_DNA.
DR EMBL; AY127009; AAM83234.1; -; mRNA.
DR EMBL; BT000524; AAN18093.1; -; mRNA.
DR EMBL; AY086209; AAM64287.1; -; mRNA.
DR PIR; T48482; T48482.
DR RefSeq; NP_196328.1; NM_120793.4.
DR AlphaFoldDB; Q9LYQ4; -.
DR BioGRID; 15881; 12.
DR IntAct; Q9LYQ4; 12.
DR STRING; 3702.AT5G07110.1; -.
DR iPTMnet; Q9LYQ4; -.
DR PaxDb; Q9LYQ4; -.
DR PRIDE; Q9LYQ4; -.
DR ProteomicsDB; 234805; -.
DR EnsemblPlants; AT5G07110.1; AT5G07110.1; AT5G07110.
DR GeneID; 830602; -.
DR Gramene; AT5G07110.1; AT5G07110.1; AT5G07110.
DR KEGG; ath:AT5G07110; -.
DR Araport; AT5G07110; -.
DR TAIR; locus:2169364; AT5G07110.
DR eggNOG; KOG3142; Eukaryota.
DR HOGENOM; CLU_060198_1_0_1; -.
DR InParanoid; Q9LYQ4; -.
DR OMA; VRKNAAY; -.
DR OrthoDB; 1344798at2759; -.
DR PhylomeDB; Q9LYQ4; -.
DR PRO; PR:Q9LYQ4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LYQ4; baseline and differential.
DR Genevisible; Q9LYQ4; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA: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; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..216
FT /note="PRA1 family protein B6"
FT /id="PRO_0000352255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 216 AA; 23138 MW; 0FD986217670F7D1 CRC64;
MASPLLPTST TPDQLPGGDP QLLSSLRVLL SRVLATVRHA SADARPWAEL VDRSAFSRPP
SLSEATSRVR KNFSYFRANY ITLVAILLAA SLLTHPFALF LLASLAASWL FLYFFRPADQ
PLVIGGRTFS DLETLGILCL STVVVMFMTS VGSLLMSTLA VGIMGVAIHG AFRAPEDLFL
EEQEAIGSGL FAFFNNNASN AAAAAIATSA MSRVRV
