PRA1D_ARATH
ID PRA1D_ARATH Reviewed; 182 AA.
AC P93829; Q8LC18;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=PRA1 family protein D;
DE Short=AtPRA1.D;
DE AltName: Full=CAMV MOVEMENT PROTEIN-INTERACTING PROTEIN 7;
DE AltName: Full=Prenylated Rab acceptor 5;
GN Name=PRA1D; Synonyms=MPI7, MPIP7, PRA5; OrderedLocusNames=At1g04260;
GN ORFNames=F19P19.30;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 TISSUE SPECIFICITY, AND INTERACTION WITH CAULIFLOWER MOSAIC VIRUS MOVEMENT
RP PROTEIN.
RX PubMed=11725951; DOI=10.1023/a:1012491913431;
RA Huang Z., Andrianov V.M., Han Y., Howell S.H.;
RT "Identification of arabidopsis proteins that interact with the cauliflower
RT mosaic virus (CaMV) movement protein.";
RL Plant Mol. Biol. 47:663-675(2001).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PRA1F2 AND
RP PRA1F3, 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 PRA1F2 and PRA1F3. Interacts with the
CC cauliflower mosaic virus (CaMV) movement protein (via N-terminus).
CC {ECO:0000269|PubMed:11725951, ECO:0000269|PubMed:18583532}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:18583532};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18583532}.
CC -!- TISSUE SPECIFICITY: Expressed in hypocotyls, roots, lateral roots,
CC lateral root caps, columella cells, leaves, shoot apex, stems and
CC flowers. {ECO:0000269|PubMed:11725951, ECO:0000269|PubMed:18583532}.
CC -!- SIMILARITY: Belongs to the PRA1 family. {ECO:0000305}.
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DR EMBL; AJ249730; CAC80648.1; -; mRNA.
DR EMBL; AC000104; AAB70450.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27675.1; -; Genomic_DNA.
DR EMBL; AF370283; AAK44098.1; -; mRNA.
DR EMBL; AY063049; AAL34223.1; -; mRNA.
DR EMBL; AY086858; AAM63905.1; -; mRNA.
DR PIR; A86174; A86174.
DR RefSeq; NP_563704.1; NM_100307.3.
DR AlphaFoldDB; P93829; -.
DR STRING; 3702.AT1G04260.1; -.
DR iPTMnet; P93829; -.
DR PaxDb; P93829; -.
DR PRIDE; P93829; -.
DR ProteomicsDB; 234869; -.
DR EnsemblPlants; AT1G04260.1; AT1G04260.1; AT1G04260.
DR GeneID; 839565; -.
DR Gramene; AT1G04260.1; AT1G04260.1; AT1G04260.
DR KEGG; ath:AT1G04260; -.
DR Araport; AT1G04260; -.
DR TAIR; locus:2018359; AT1G04260.
DR eggNOG; KOG3142; Eukaryota.
DR HOGENOM; CLU_060198_2_1_1; -.
DR InParanoid; P93829; -.
DR OMA; PWPLFID; -.
DR OrthoDB; 1344798at2759; -.
DR PhylomeDB; P93829; -.
DR PRO; PR:P93829; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P93829; baseline and differential.
DR Genevisible; P93829; AT.
DR GO; GO:0005737; C:cytoplasm; IDA: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; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046739; P:transport of virus in multicellular host; TAS:TAIR.
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; Host-virus interaction; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..182
FT /note="PRA1 family protein D"
FT /id="PRO_0000352257"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 163..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 179
FT /note="Y -> N (in Ref. 5; AAM63905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 182 AA; 19325 MW; D7DECF0998EBECE5 CRC64;
MANQVITGIK ETAQSITGAA RPWGDFLDLS AFSFPSSIAD ATTRVTQNLT HFRINYSIIL
SILLGLTLIT RPIAILAFIA VGLAWFFLYF AREEPLTIFG FTIDDGIVAV LLIGLSIGSL
VTTGVWLRAL TTVGFGVLVL ILHAALRGTD DLVSDDLESP YGPMLSTSGG GNDGARGDYS
GI
