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PILS5_ARATH
ID   PILS5_ARATH             Reviewed;         396 AA.
AC   Q9SHL8; B9DG37; Q8LGC5;
DT   08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Protein PIN-LIKES 5 {ECO:0000303|PubMed:22504182};
DE   AltName: Full=Auxin efflux carrier-like protein 5 {ECO:0000303|PubMed:22504182};
GN   Name=PILS5 {ECO:0000303|PubMed:22504182};
GN   OrderedLocusNames=At2g17500 {ECO:0000312|Araport:AT2G17500};
GN   ORFNames=MJB20.6 {ECO:0000312|EMBL:AAD32907.1};
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-210.
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, INDUCTION BY AUXIN, GENE FAMILY,
RP   NOMENCLATURE, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=22504182; DOI=10.1038/nature11001;
RA   Barbez E., Kubes M., Rolcik J., Beziat C., Pencik A., Wang B.,
RA   Rosquete M.R., Zhu J., Dobrev P.I., Lee Y., Zazimalova E., Petrasek J.,
RA   Geisler M., Friml J., Kleine-Vehn J.;
RT   "A novel putative auxin carrier family regulates intracellular auxin
RT   homeostasis in plants.";
RL   Nature 485:119-122(2012).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=23091477; DOI=10.3389/fpls.2012.00227;
RA   Feraru E., Vosolsobe S., Feraru M.I., Petrasek J., Kleine-Vehn J.;
RT   "Evolution and structural diversification of PILS putative auxin carriers
RT   in plants.";
RL   Front. Plant Sci. 3:227-227(2012).
CC   -!- FUNCTION: Involved in cellular auxin homeostasis by regulating auxin
CC       metabolism. Regulates intracellular auxin accumulation at the
CC       endoplasmic reticulum and thus auxin availability for nuclear auxin
CC       signaling. {ECO:0000269|PubMed:22504182}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:22504182}; Multi-pass membrane protein
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in seedlings, cauline leaves and flowers.
CC       {ECO:0000269|PubMed:22504182}.
CC   -!- INDUCTION: Up-regulated by auxin application.
CC       {ECO:0000269|PubMed:22504182}.
CC   -!- DISRUPTION PHENOTYPE: Increased root growth and lateral root
CC       initiation. {ECO:0000269|PubMed:22504182}.
CC   -!- SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.2) family.
CC       {ECO:0000305}.
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DR   EMBL; AC007584; AAD32907.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06634.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06635.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06636.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06637.1; -; Genomic_DNA.
DR   EMBL; AK226321; BAE98473.1; -; mRNA.
DR   EMBL; AY084347; AAM60930.1; -; mRNA.
DR   EMBL; AK317010; BAH19704.1; -; mRNA.
DR   PIR; H84552; H84552.
DR   RefSeq; NP_001031363.1; NM_001036286.3.
DR   RefSeq; NP_565417.1; NM_127304.3.
DR   RefSeq; NP_849964.1; NM_179633.4.
DR   RefSeq; NP_973479.1; NM_201750.2.
DR   AlphaFoldDB; Q9SHL8; -.
DR   STRING; 3702.AT2G17500.2; -.
DR   PaxDb; Q9SHL8; -.
DR   PRIDE; Q9SHL8; -.
DR   ProteomicsDB; 235017; -.
DR   EnsemblPlants; AT2G17500.1; AT2G17500.1; AT2G17500.
DR   EnsemblPlants; AT2G17500.2; AT2G17500.2; AT2G17500.
DR   EnsemblPlants; AT2G17500.3; AT2G17500.3; AT2G17500.
DR   EnsemblPlants; AT2G17500.4; AT2G17500.4; AT2G17500.
DR   GeneID; 816256; -.
DR   Gramene; AT2G17500.1; AT2G17500.1; AT2G17500.
DR   Gramene; AT2G17500.2; AT2G17500.2; AT2G17500.
DR   Gramene; AT2G17500.3; AT2G17500.3; AT2G17500.
DR   Gramene; AT2G17500.4; AT2G17500.4; AT2G17500.
DR   KEGG; ath:AT2G17500; -.
DR   Araport; AT2G17500; -.
DR   TAIR; locus:2053908; AT2G17500.
DR   eggNOG; KOG2722; Eukaryota.
DR   HOGENOM; CLU_044945_0_0_1; -.
DR   InParanoid; Q9SHL8; -.
DR   OMA; IFGAVRW; -.
DR   OrthoDB; 1055578at2759; -.
DR   PhylomeDB; Q9SHL8; -.
DR   PRO; PR:Q9SHL8; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SHL8; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0010329; F:auxin efflux transmembrane transporter activity; IMP:UniProtKB.
DR   GO; GO:0010252; P:auxin homeostasis; IDA:UniProtKB.
DR   GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0080162; P:endoplasmic reticulum to cytosol auxin transport; IEA:InterPro.
DR   GO; GO:0010311; P:lateral root formation; IMP:UniProtKB.
DR   GO; GO:0040009; P:regulation of growth rate; IMP:UniProtKB.
DR   GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
DR   InterPro; IPR004776; Mem_trans.
DR   InterPro; IPR045033; PILS1/3/4/5/7.
DR   PANTHER; PTHR31651; PTHR31651; 1.
DR   Pfam; PF03547; Mem_trans; 1.
PE   2: Evidence at transcript level;
KW   Auxin signaling pathway; Endoplasmic reticulum; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..396
FT                   /note="Protein PIN-LIKES 5"
FT                   /id="PRO_0000436500"
FT   TOPO_DOM        1..5
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:23091477"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..45
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:23091477"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        67..73
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:23091477"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        95..106
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:23091477"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        128..144
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:23091477"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        166..229
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:23091477"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..273
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:23091477"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        295..312
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:23091477"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        334..337
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:23091477"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        359..370
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:23091477"
FT   TRANSMEM        371..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        392..396
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:23091477"
FT   CONFLICT        216
FT                   /note="K -> E (in Ref. 4; AAM60930)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        311
FT                   /note="V -> A (in Ref. 4; AAM60930)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   396 AA;  43394 MW;  81A78C8A017CF67D CRC64;
     MGFWSLLEVA SMPVIQVLFM SLVGAFMASD RCKLFPVEAR NSMNKVVFVL FAPALMFANL
     AQTVTLEDII SWWFMPVNMG LTFLIGGLLG WLVVKILKPP PYLEGLIVAT CSAGNMGNLP
     IILVPAICDE DKSPFGNRSV CRTVGLSYAS FSMALGGFYI WTYTFRLIKG SAMKVQAIEE
     SEKIAIKSSN SDLEADHKTH LLGAPEDKEN KVVKEKTGFW RKGVDFLHEI LEELLAPPTL
     GAIIGFIFGA VRWLRNLIIG DDAPLRIVQS TAKLLGDGTI PCMTIILGGN LIQGLRSSAV
     KPMVVLGIVC VRYIAMPIIG IGIVLTAANL GFLPADPLFQ YVLMLQFTLP PAMNIGTMTQ
     LYNVAQDECS VLMLWTYLVA ILALTVWSTI FLHLLV
 
 
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