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PR1F3_ARATH
ID   PR1F3_ARATH             Reviewed;         188 AA.
AC   Q9LIC6; Q8L959;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=PRA1 family protein F3 {ECO:0000303|PubMed:18583532};
DE            Short=AtPRA1.F3 {ECO:0000303|PubMed:18583532};
DE   AltName: Full=Prenylated Rab acceptor 8 {ECO:0000303|PubMed:18845362};
GN   Name=PRA1F3 {ECO:0000303|PubMed:18583532};
GN   Synonyms=PRA8 {ECO:0000303|PubMed:18845362};
GN   OrderedLocusNames=At3g13720 {ECO:0000312|Araport:AT3G13720};
GN   ORFNames=MMM17.14 {ECO:0000312|EMBL:BAB01921.1};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PRA1F2 AND
RP   PRA1D, 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   [6]
RP   INTERACTION WITH ACD11 AND BPA1, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=18845362; DOI=10.1016/j.jplph.2008.08.003;
RA   Petersen N.H., Joensen J., McKinney L.V., Brodersen P., Petersen M.,
RA   Hofius D., Mundy J.;
RT   "Identification of proteins interacting with Arabidopsis ACD11.";
RL   J. Plant Physiol. 166:661-666(2009).
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 PRA1D (PubMed:18583532). Interacts
CC       with ACD11 and BPA1 (PubMed:18845362). {ECO:0000269|PubMed:18583532,
CC       ECO:0000269|PubMed:18845362}.
CC   -!- INTERACTION:
CC       Q9LIC6; Q9M354: AGD6; NbExp=3; IntAct=EBI-2010961, EBI-21138098;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000305|PubMed:18583532}; Multi-pass membrane protein
CC       {ECO:0000305|PubMed:18583532}. Membrane {ECO:0000269|PubMed:18845362};
CC       Multi-pass membrane protein {ECO:0000255}. Cytoplasm
CC       {ECO:0000269|PubMed:18845362}.
CC   -!- TISSUE SPECIFICITY: Expressed in lateral roots, lateral root caps and
CC       columella cells. {ECO:0000269|PubMed:18583532}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000305|PubMed:18845362}.
CC   -!- SIMILARITY: Belongs to the PRA1 family. {ECO:0000305}.
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DR   EMBL; AP001307; BAB01921.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75403.1; -; Genomic_DNA.
DR   EMBL; BT004174; AAO42194.1; -; mRNA.
DR   EMBL; BT004952; AAO50485.1; -; mRNA.
DR   EMBL; AY088623; AAM66945.1; -; mRNA.
DR   RefSeq; NP_566461.1; NM_112222.4.
DR   AlphaFoldDB; Q9LIC6; -.
DR   BioGRID; 5915; 49.
DR   IntAct; Q9LIC6; 42.
DR   STRING; 3702.AT3G13720.1; -.
DR   PaxDb; Q9LIC6; -.
DR   PRIDE; Q9LIC6; -.
DR   ProteomicsDB; 225981; -.
DR   EnsemblPlants; AT3G13720.1; AT3G13720.1; AT3G13720.
DR   GeneID; 820581; -.
DR   Gramene; AT3G13720.1; AT3G13720.1; AT3G13720.
DR   KEGG; ath:AT3G13720; -.
DR   Araport; AT3G13720; -.
DR   TAIR; locus:2091556; AT3G13720.
DR   eggNOG; KOG3142; Eukaryota.
DR   HOGENOM; CLU_060198_2_1_1; -.
DR   InParanoid; Q9LIC6; -.
DR   OMA; DRWYAPV; -.
DR   OrthoDB; 1344798at2759; -.
DR   PhylomeDB; Q9LIC6; -.
DR   PRO; PR:Q9LIC6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LIC6; baseline and differential.
DR   Genevisible; Q9LIC6; 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; IBA:GO_Central.
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   Cytoplasm; Endoplasmic reticulum; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..188
FT                   /note="PRA1 family protein F3"
FT                   /id="PRO_0000352261"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        160
FT                   /note="S -> A (in Ref. 4; AAM66945)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   188 AA;  21116 MW;  FA3ECEC01E3CC94D CRC64;
     MTNYGAIPTS SHASPLVDVE SLSRAKHRIK AGLATRRAWR VMFDFHSMGL PHGVSDAFTR
     IKTNLAYFRM NYAIVVLIVI FFSLIWHPTS LIVFTVLVVV WIFLYFLRDE PIKLFRFQID
     DRTVLIVLSV LTVVLLLLTN ATFNIVGALV TGAVLVLIHS VVRKTEDLFL DEEAATTETS
     GLTSYPST
 
 
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