PROT2_ARATH
ID PROT2_ARATH Reviewed; 439 AA.
AC P92962; F4IY22;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Proline transporter 2;
DE Short=AtPROT2;
GN Name=PROT2; OrderedLocusNames=At3g55740; ORFNames=F1I16.150;
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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
RX PubMed=8776904; DOI=10.2307/3870312;
RA Rentsch D., Hirner B., Schmelzer E., Frommer W.B.;
RT "Salt stress-induced proline transporters and salt stress-repressed broad
RT specificity amino acid permeases identified by suppression of a yeast amino
RT acid permease-targeting mutant.";
RL Plant Cell 8:1437-1446(1996).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [6]
RP FUNCTION.
RX PubMed=10359089; DOI=10.1016/s0014-5793(99)00516-5;
RA Breitkreuz K.E., Shelp B.J., Fischer W.-N., Schwacke R., Rentsch D.;
RT "Identification and characterization of GABA, proline and quaternary
RT ammonium compound transporters from Arabidopsis thaliana.";
RL FEBS Lett. 450:280-284(1999).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=15618414; DOI=10.1104/pp.104.055079;
RA Grallath S., Weimar T., Meyer A., Gumy C., Suter-Grotemeyer M.,
RA Neuhaus J.M., Rentsch D.;
RT "The AtProT family. Compatible solute transporters with similar substrate
RT specificity but differential expression patterns.";
RL Plant Physiol. 137:117-126(2005).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20959625; DOI=10.1093/jxb/erq320;
RA Lehmann S., Gumy C., Blatter E., Boeffel S., Fricke W., Rentsch D.;
RT "In planta function of compatible solute transporters of the AtProT
RT family.";
RL J. Exp. Bot. 62:787-796(2011).
CC -!- FUNCTION: Proline transporter that mediates proline and glycine betaine
CC transport. May be involved in the uptake of compatible solutes from the
CC soil into the roots, or in retrieval of apoplastic amino acids
CC delivered to the roots via the phloem. May be involved in delivery of
CC proline to wounding sites. When expressed in a heterologous system
CC (yeast), imports D- and L-proline, glycine betaine and GABA across the
CC plasma membrane. Has the same affinity for D- and L-proline.
CC {ECO:0000269|PubMed:10359089, ECO:0000269|PubMed:15618414,
CC ECO:0000269|PubMed:20959625, ECO:0000269|PubMed:8776904}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.267 mM for glycine betaine {ECO:0000269|PubMed:15618414};
CC KM=0.5 mM for L-proline {ECO:0000269|PubMed:15618414};
CC KM=4.01 mM for GABA {ECO:0000269|PubMed:15618414};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15618414};
CC Multi-pass membrane protein {ECO:0000305|PubMed:15618414}. Note=Plasma
CC membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P92962-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P92962-2; Sequence=VSP_044100;
CC -!- TISSUE SPECIFICITY: Expressed in epidermal and cortex cells of roots.
CC Expressed in stipules. {ECO:0000269|PubMed:15618414,
CC ECO:0000269|PubMed:8776904}.
CC -!- INDUCTION: By wounding, drought and salt stress.
CC {ECO:0000269|PubMed:15618414, ECO:0000269|PubMed:8776904}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants grown with exogenous high concentrations
CC of D-proline show reduced inhibition of root growth.
CC {ECO:0000269|PubMed:20959625}.
CC -!- MISCELLANEOUS: Treatment with toxic concentrations of proline reduces
CC shoot growth and root elongation in wild-type plants, while plant lines
CC over-expressing PROT2 stop growing shortly after unfolding of
CC cotyledons. {ECO:0000305|PubMed:20959625}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC Amino acid/auxin permease (AAAP) (TC 2.A.18.3) subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX823265; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X95738; CAA65053.1; -; mRNA.
DR EMBL; AL161667; CAB81599.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79428.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79429.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63441.1; -; Genomic_DNA.
DR EMBL; AY081292; AAL91181.1; -; mRNA.
DR EMBL; BT008750; AAP49512.1; -; mRNA.
DR EMBL; BX823265; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T47713; T47713.
DR RefSeq; NP_001325527.1; NM_001339744.1. [P92962-2]
DR RefSeq; NP_191133.1; NM_115432.5. [P92962-1]
DR RefSeq; NP_974444.1; NM_202715.2. [P92962-2]
DR AlphaFoldDB; P92962; -.
DR SMR; P92962; -.
DR BioGRID; 10056; 21.
DR IntAct; P92962; 21.
DR STRING; 3702.AT3G55740.1; -.
DR PaxDb; P92962; -.
DR PRIDE; P92962; -.
DR ProteomicsDB; 226506; -. [P92962-1]
DR EnsemblPlants; AT3G55740.1; AT3G55740.1; AT3G55740. [P92962-1]
DR EnsemblPlants; AT3G55740.2; AT3G55740.2; AT3G55740. [P92962-2]
DR EnsemblPlants; AT3G55740.3; AT3G55740.3; AT3G55740. [P92962-2]
DR GeneID; 824740; -.
DR Gramene; AT3G55740.1; AT3G55740.1; AT3G55740. [P92962-1]
DR Gramene; AT3G55740.2; AT3G55740.2; AT3G55740. [P92962-2]
DR Gramene; AT3G55740.3; AT3G55740.3; AT3G55740. [P92962-2]
DR KEGG; ath:AT3G55740; -.
DR Araport; AT3G55740; -.
DR TAIR; locus:2078981; AT3G55740.
DR eggNOG; KOG1303; Eukaryota.
DR InParanoid; P92962; -.
DR OMA; HMYIIAM; -.
DR PhylomeDB; P92962; -.
DR SABIO-RK; P92962; -.
DR PRO; PR:P92962; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P92962; baseline and differential.
DR Genevisible; P92962; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015193; F:L-proline transmembrane transporter activity; IGI:TAIR.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0015824; P:proline transport; IGI:TAIR.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid transport; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..439
FT /note="Proline transporter 2"
FT /id="PRO_0000418994"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_044100"
SQ SEQUENCE 439 AA; 48086 MW; F1C6177A228490C8 CRC64;
MDTSEARNRK VVAVEQFDLE VPETAHQISS DSWFQVAFVL TTGINSAYVL GYSGTVMVPL
GWIGGVVGLI LATAISLYAN TLIAKLHEFG GKRHIRYRDL AGFIYGKKMY RVTWGLQYVN
LFMINCGFII LAGSALKAVY VLFRDDSLMK LPHFIAIAGV VCAIFAIGIP HLSALGIWLG
VSTILSIIYI IVAIVLSAKD GVNKPERDYN IQGSSINKLF TITGAAANLV FAFNTGMLPE
IQATVKQPVV KNMMKALYFQ FTVGVLPMYA VTFIGYWAYG SSTSTYLLNS VSGPVWVKAL
ANISAFLQSV ISLHIFASPT YEYMDTKYGV KGSPLAMKNL LFRTVARGSY IAVSTLLSAL
LPFLGDFMSL TGAISTFPLT FILANHMYLV AMNDELSLVQ KLWHWLNVCF FGLMSLAAAI
AAVRLISVDS KNFHVFADV
