PTR1_ARATH
ID PTR1_ARATH Reviewed; 570 AA.
AC Q9M390;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Protein NRT1/ PTR FAMILY 8.1;
DE Short=AtNPF8.1;
DE AltName: Full=Peptide transporter PTR1;
GN Name=NPF8.1; Synonyms=PTR1; OrderedLocusNames=At3g54140;
GN ORFNames=F24B22.100;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15500465; DOI=10.1111/j.1365-313x.2004.02224.x;
RA Dietrich D., Hammes U., Thor K., Suter-Grotemeyer M., Flueckiger R.,
RA Slusarenko A.J., Ward J.M., Rentsch D.;
RT "AtPTR1, a plasma membrane peptide transporter expressed during seed
RT germination and in vascular tissue of Arabidopsis.";
RL Plant J. 40:488-499(2004).
RN [7]
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18753286; DOI=10.1104/pp.108.123844;
RA Komarova N.Y., Thor K., Gubler A., Meier S., Dietrich D., Weichert A.,
RA Suter Grotemeyer M., Tegeder M., Rentsch D.;
RT "AtPTR1 and AtPTR5 transport dipeptides in planta.";
RL Plant Physiol. 148:856-869(2008).
RN [9]
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. Mediates the transport of di- and
CC tripeptides. High affinity transporter with low selectivity. No
CC transport of amino acids. {ECO:0000269|PubMed:15500465,
CC ECO:0000269|PubMed:18753286}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15500465};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15500465}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, hypocotyls, leaves, roots,
CC flowers, pistils and vascular tissue of sepals, anthers, carpels and
CC funiculi. Not detected in seeds. {ECO:0000269|PubMed:15500465,
CC ECO:0000269|PubMed:17481610}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth and lower N content when
CC cultivated on dipeptides. No effect on germination.
CC {ECO:0000269|PubMed:18753286}.
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; AL132957; CAB70988.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79192.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64757.1; -; Genomic_DNA.
DR EMBL; AF360155; AAK25865.1; -; mRNA.
DR EMBL; AY113884; AAM44932.1; -; mRNA.
DR EMBL; AY084773; AAM61341.1; -; mRNA.
DR PIR; T47573; T47573.
DR RefSeq; NP_001326764.1; NM_001339651.1.
DR RefSeq; NP_190982.1; NM_115274.3.
DR AlphaFoldDB; Q9M390; -.
DR SMR; Q9M390; -.
DR BioGRID; 9898; 30.
DR IntAct; Q9M390; 28.
DR STRING; 3702.AT3G54140.1; -.
DR TCDB; 2.A.17.3.7; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR PaxDb; Q9M390; -.
DR PRIDE; Q9M390; -.
DR ProteomicsDB; 226444; -.
DR EnsemblPlants; AT3G54140.1; AT3G54140.1; AT3G54140.
DR EnsemblPlants; AT3G54140.2; AT3G54140.2; AT3G54140.
DR GeneID; 824581; -.
DR Gramene; AT3G54140.1; AT3G54140.1; AT3G54140.
DR Gramene; AT3G54140.2; AT3G54140.2; AT3G54140.
DR KEGG; ath:AT3G54140; -.
DR Araport; AT3G54140; -.
DR TAIR; locus:2080235; AT3G54140.
DR eggNOG; KOG1237; Eukaryota.
DR HOGENOM; CLU_009313_4_1_1; -.
DR InParanoid; Q9M390; -.
DR OMA; VAHVIMV; -.
DR OrthoDB; 365203at2759; -.
DR PhylomeDB; Q9M390; -.
DR BRENDA; 7.4.2.5; 399.
DR PRO; PR:Q9M390; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M390; baseline and differential.
DR Genevisible; Q9M390; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0042937; F:tripeptide transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0042938; P:dipeptide transport; IDA:TAIR.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IMP:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042939; P:tripeptide transport; IDA:TAIR.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000109; POT_fam.
DR InterPro; IPR018456; PTR2_symporter_CS.
DR PANTHER; PTHR11654; PTHR11654; 1.
DR Pfam; PF00854; PTR2; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS01022; PTR2_1; 1.
DR PROSITE; PS01023; PTR2_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Peptide transport; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..570
FT /note="Protein NRT1/ PTR FAMILY 8.1"
FT /id="PRO_0000378322"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 98
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q05085"
SQ SEQUENCE 570 AA; 64034 MW; 7366F068DD97B3ED CRC64;
MEEKDVYTQD GTVDIHKNPA NKEKTGNWKA CRFILGNECC ERLAYYGMGT NLVNYLESRL
NQGNATAANN VTNWSGTCYI TPLIGAFIAD AYLGRYWTIA TFVFIYVSGM TLLTLSASVP
GLKPGNCNAD TCHPNSSQTA VFFVALYMIA LGTGGIKPCV SSFGADQFDE NDENEKIKKS
SFFNWFYFSI NVGALIAATV LVWIQMNVGW GWGFGVPTVA MVIAVCFFFF GSRFYRLQRP
GGSPLTRIFQ VIVAAFRKIS VKVPEDKSLL FETADDESNI KGSRKLVHTD NLKFFDKAAV
ESQSDSIKDG EVNPWRLCSV TQVEELKSII TLLPVWATGI VFATVYSQMS TMFVLQGNTM
DQHMGKNFEI PSASLSLFDT VSVLFWTPVY DQFIIPLARK FTRNERGFTQ LQRMGIGLVV
SIFAMITAGV LEVVRLDYVK THNAYDQKQI HMSIFWQIPQ YLLIGCAEVF TFIGQLEFFY
DQAPDAMRSL CSALSLTTVA LGNYLSTVLV TVVMKITKKN GKPGWIPDNL NRGHLDYFFY
LLATLSFLNF LVYLWISKRY KYKKAVGRAH
