PTR3_ARATH
ID PTR3_ARATH Reviewed; 582 AA.
AC Q9FNL7; Q8VZK3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Protein NRT1/ PTR FAMILY 5.2;
DE Short=AtNPF5.2;
DE AltName: Full=Peptide transporter PTR3-A;
DE Short=AtPTR3;
GN Name=NPF5.2; Synonyms=PTR3-A; OrderedLocusNames=At5g46050;
GN ORFNames=MCL19.10;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 INDUCTION BY WOUNDING; AMINO ACIDS AND SALT, AND FUNCTION.
RC STRAIN=cv. C24;
RX PubMed=15889294; DOI=10.1007/s00894-005-0257-6;
RA Karim S., Lundh D., Holmstroem K.-O., Mandal A., Pirhonen M.;
RT "Structural and functional characterization of AtPTR3, a stress-induced
RT peptide transporter of Arabidopsis.";
RL J. Mol. Model. 11:226-236(2005).
RN [5]
RP TISSUE SPECIFICITY, AND GENE FAMILY.
RX PubMed=17481610; DOI=10.1016/j.febslet.2007.04.047;
RA Tsay Y.F., Chiu C.C., Tsai C.B., Ho C.H., Hsu P.K.;
RT "Nitrate transporters and peptide transporters.";
RL FEBS Lett. 581:2290-2300(2007).
RN [6]
RP INDUCTION BY SALT; SALICYLIC ACIDS; ABSCISIC ACID AND METHYL JASMONATE, AND
RP FUNCTION.
RX PubMed=17143616; DOI=10.1007/s00425-006-0451-5;
RA Karim S., Holmstroem K.-O., Mandal A., Dahl P., Hohmann S., Brader G.,
RA Palva E.T., Pirhonen M.;
RT "AtPTR3, a wound-induced peptide transporter needed for defence against
RT virulent bacterial pathogens in Arabidopsis.";
RL Planta 225:1431-1445(2007).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=24055139; DOI=10.1016/j.tplants.2013.08.008;
RA Leran S., Varala K., Boyer J.C., Chiurazzi M., Crawford N.,
RA Daniel-Vedele F., David L., Dickstein R., Fernandez E., Forde B.,
RA Gassmann W., Geiger D., Gojon A., Gong J.M., Halkier B.A., Harris J.M.,
RA Hedrich R., Limami A.M., Rentsch D., Seo M., Tsay Y.F., Zhang M.,
RA Coruzzi G., Lacombe B.;
RT "A unified nomenclature of NITRATE TRANSPORTER 1/PEPTIDE TRANSPORTER family
RT members in plants.";
RL Trends Plant Sci. 19:5-9(2014).
CC -!- FUNCTION: Peptide transporter involved in stress tolerance in seeds
CC during germination and in defense against virulent bacterial pathogens.
CC {ECO:0000269|PubMed:15889294, ECO:0000269|PubMed:17143616}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. Detected in shoots, leaves and
CC flowers. {ECO:0000269|PubMed:17481610}.
CC -!- INDUCTION: By wounding, salicylic acid, abscisic acid, methyl
CC jasmonate, salt treatment and amino acids histidine, leucine and
CC phenylalanine. No induction by glutamic acid, methionine or tryptophan.
CC {ECO:0000269|PubMed:15889294, ECO:0000269|PubMed:17143616}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
CC {ECO:0000305}.
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DR EMBL; AB006698; BAB08250.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95332.1; -; Genomic_DNA.
DR EMBL; AY150511; AAN13027.1; -; mRNA.
DR EMBL; AY064057; AAL36413.1; -; mRNA.
DR RefSeq; NP_199417.1; NM_123973.4.
DR AlphaFoldDB; Q9FNL7; -.
DR SMR; Q9FNL7; -.
DR STRING; 3702.AT5G46050.1; -.
DR TCDB; 2.A.17.3.4; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR iPTMnet; Q9FNL7; -.
DR PaxDb; Q9FNL7; -.
DR PRIDE; Q9FNL7; -.
DR ProteomicsDB; 226438; -.
DR EnsemblPlants; AT5G46050.1; AT5G46050.1; AT5G46050.
DR GeneID; 834646; -.
DR Gramene; AT5G46050.1; AT5G46050.1; AT5G46050.
DR KEGG; ath:AT5G46050; -.
DR Araport; AT5G46050; -.
DR TAIR; locus:2161438; AT5G46050.
DR eggNOG; KOG1237; Eukaryota.
DR HOGENOM; CLU_009313_0_1_1; -.
DR InParanoid; Q9FNL7; -.
DR OMA; LYFYMMI; -.
DR OrthoDB; 365203at2759; -.
DR PhylomeDB; Q9FNL7; -.
DR PRO; PR:Q9FNL7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNL7; baseline and differential.
DR Genevisible; Q9FNL7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IGI:TAIR.
DR GO; GO:0042937; F:tripeptide transmembrane transporter activity; IGI:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0042938; P:dipeptide transport; IGI:TAIR.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0080052; P:response to histidine; IEP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0043201; P:response to leucine; IEP:TAIR.
DR GO; GO:0080053; P:response to phenylalanine; IEP:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR GO; GO:0042939; P:tripeptide transport; IGI:TAIR.
DR CDD; cd17417; MFS_NPF5; 1.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR044739; NRT1/PTR.
DR InterPro; IPR000109; POT_fam.
DR PANTHER; PTHR11654; PTHR11654; 1.
DR Pfam; PF00854; PTR2; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 2: Evidence at transcript level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..582
FT /note="Protein NRT1/ PTR FAMILY 5.2"
FT /id="PRO_0000300100"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 552
FT /note="V -> I (in Ref. 3; AAL36413)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 582 AA; 65271 MW; A9FCA16346CBAC60 CRC64;
MTVEEVGDDY TKDGTVDLQG NPVRRSIRGR WKACSFVVVY EVFERMAYYG ISSNLFIYMT
TKLHQGTVKS SNNVTNWVGT SWLTPILGAY VGDALLGRYI TFVISCAIYF SGMMVLTLSV
TIPGIKPPEC STTNVENCEK ASVLQLAVFF GALYTLAIGT GGTKPNISTI GADQFDVFDP
KEKTQKLSFF NWWMFSIFFG TLFANTVLVY VQDNVGWTLG YGLPTLGLAI SITIFLLGTP
FYRHKLPTGS PFTKMARVIV ASFRKANAPM THDITSFHEL PSLEYERKGA FPIHPTPSLR
FLDRASLKTG TNHKWNLCTT TEVEETKQML RMLPVLFITF VPSMMLAQIN TLFVKQGTTL
DRKVTGSFSI PPASLSGFVT LSMLISIVLY DRVFVKITRK FTGNPRGITL LQRMGIGLIF
HILIMIVASV TERYRLKVAA DHGLIHQTGV KLPLTIFALL PQFVLMGMAD SFLEVAKLEF
FYDQAPESMK SLGTSYSTTS LAIGNFMSSF LLSTVSEITK KRGRGWILNN LNESRLDYYY
LFFAVLNLVN FVLFLVVVKF YVYRAEVTDS VDVKEVEMKE TE
