PTR2_ARATH
ID PTR2_ARATH Reviewed; 585 AA.
AC P46032;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein NRT1/ PTR FAMILY 8.3;
DE Short=AtNPF8.3;
DE AltName: Full=Histidine-transporting protein;
DE AltName: Full=Peptide transporter PTR2;
GN Name=NPF8.3; Synonyms=NTR1, PTR2, PTR2-B; OrderedLocusNames=At2g02040;
GN ORFNames=F14H20.11;
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], BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8587981; DOI=10.1104/pp.110.1.171;
RA Song W., Steiner H.-Y., Zhang L., Naider F., Stacey G., Becker J.M.;
RT "Cloning of a second Arabidopsis peptide transport gene.";
RL Plant Physiol. 110:171-178(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. C24;
RX PubMed=8033999; DOI=10.1016/0014-5793(94)00533-8;
RA Frommer W.B., Hummel S., Rentsch D.;
RT "Cloning of an Arabidopsis histidine transporting protein related to
RT nitrate and peptide transporters.";
RL FEBS Lett. 347:185-189(1994).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA Garin J., Bourguignon J.;
RT "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT cell culture.";
RL Mol. Cell. Proteomics 6:394-412(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-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).
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, low capacity transporter. Can also
CC transport histidine.
CC -!- ACTIVITY REGULATION: Inhibited by leucyl-ethionine.
CC {ECO:0000269|PubMed:8587981}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14.4 uM for dileucine {ECO:0000269|PubMed:8587981};
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:17151019};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in young leaves, roots and
CC germinating seeds, intermediately in stems, flowers and mature leaves
CC and at low level in siliques. {ECO:0000269|PubMed:17481610,
CC ECO:0000269|PubMed:8587981}.
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; L39082; AAB00858.1; -; mRNA.
DR EMBL; X77503; CAA54634.1; -; mRNA.
DR EMBL; AC006532; AAD20096.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05538.1; -; Genomic_DNA.
DR EMBL; AF372946; AAK50086.1; -; mRNA.
DR EMBL; AY143954; AAN28893.1; -; mRNA.
DR PIR; C84432; C84432.
DR PIR; S46236; S46236.
DR RefSeq; NP_178313.1; NM_126265.4.
DR AlphaFoldDB; P46032; -.
DR SMR; P46032; -.
DR BioGRID; 138; 37.
DR IntAct; P46032; 17.
DR STRING; 3702.AT2G02040.1; -.
DR TCDB; 2.A.17.3.2; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR iPTMnet; P46032; -.
DR PaxDb; P46032; -.
DR PRIDE; P46032; -.
DR ProteomicsDB; 226106; -.
DR EnsemblPlants; AT2G02040.1; AT2G02040.1; AT2G02040.
DR GeneID; 814735; -.
DR Gramene; AT2G02040.1; AT2G02040.1; AT2G02040.
DR KEGG; ath:AT2G02040; -.
DR Araport; AT2G02040; -.
DR TAIR; locus:2041125; AT2G02040.
DR eggNOG; KOG1237; Eukaryota.
DR HOGENOM; CLU_009313_4_1_1; -.
DR InParanoid; P46032; -.
DR OMA; FPPINRI; -.
DR OrthoDB; 365203at2759; -.
DR PhylomeDB; P46032; -.
DR PRO; PR:P46032; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P46032; baseline and differential.
DR Genevisible; P46032; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015334; F:high-affinity oligopeptide 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:0015833; P:peptide transport; TAS: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 Acetylation; Membrane; Peptide transport; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..585
FT /note="Protein NRT1/ PTR FAMILY 8.3"
FT /id="PRO_0000064320"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 115
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q05085"
FT CONFLICT 334
FT /note="R -> ED (in Ref. 2; CAA54634)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 585 AA; 64421 MW; C58F8194776E2D97 CRC64;
MGSIEEEARP LIEEGLILQE VKLYAEDGSV DFNGNPPLKE KTGNWKACPF ILGNECCERL
AYYGIAGNLI TYLTTKLHQG NVSAATNVTT WQGTCYLTPL IGAVLADAYW GRYWTIACFS
GIYFIGMSAL TLSASVPALK PAECIGDFCP SATPAQYAMF FGGLYLIALG TGGIKPCVSS
FGADQFDDTD SRERVRKASF FNWFYFSINI GALVSSSLLV WIQENRGWGL GFGIPTVFMG
LAIASFFFGT PLYRFQKPGG SPITRISQVV VASFRKSSVK VPEDATLLYE TQDKNSAIAG
SRKIEHTDDC QYLDKAAVIS EEESKSGDYS NSWRLCTVTQ VEELKILIRM FPIWASGIIF
SAVYAQMSTM FVQQGRAMNC KIGSFQLPPA ALGTFDTASV IIWVPLYDRF IVPLARKFTG
VDKGFTEIQR MGIGLFVSVL CMAAAAIVEI IRLHMANDLG LVESGAPVPI SVLWQIPQYF
ILGAAEVFYF IGQLEFFYDQ SPDAMRSLCS ALALLTNALG NYLSSLILTL VTYFTTRNGQ
EGWISDNLNS GHLDYFFWLL AGLSLVNMAV YFFSAARYKQ KKASS
