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PROT1_ARATH
ID   PROT1_ARATH             Reviewed;         442 AA.
AC   P92961; O04746; Q8LAE3;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Proline transporter 1;
DE            Short=AtPROT1;
GN   Name=PROT1; OrderedLocusNames=At2g39890; ORFNames=T28M21.5;
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], FUNCTION, AND TISSUE SPECIFICITY.
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=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   [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].
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   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   [6]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
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   [7]
RP   FUNCTION, TISSUE SPECIFICITY, 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 long-distance transport of proline and
CC       required for phloem loading, retrieval of proline leaking from the
CC       phloem, or in xylem-to-phloem transfer. When expressed in a
CC       heterologous system (yeast), imports D- and L-proline, glycine betaine
CC       and GABA across the plasma membrane. Has the same affinity for D- and
CC       L-proline. {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=0.115 mM for glycine betaine {ECO:0000269|PubMed:15618414};
CC         KM=0.427 mM for L-proline {ECO:0000269|PubMed:15618414};
CC         KM=4.5 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   -!- TISSUE SPECIFICITY: Expressed in vascular tissues of roots, leaves,
CC       stems, sepals, petals, stamen and siliques. Expressed in pollen.
CC       {ECO:0000269|PubMed:15618414, ECO:0000269|PubMed:20959625,
CC       ECO:0000269|PubMed:8776904}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions. {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 PROT1 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}.
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DR   EMBL; X95737; CAA65052.1; -; mRNA.
DR   EMBL; AF002109; AAB95274.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09745.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09746.1; -; Genomic_DNA.
DR   EMBL; AY087868; AAM65420.1; -; mRNA.
DR   PIR; T50692; T50692.
DR   RefSeq; NP_001078025.1; NM_001084556.2.
DR   RefSeq; NP_181518.1; NM_129547.3.
DR   AlphaFoldDB; P92961; -.
DR   SMR; P92961; -.
DR   BioGRID; 3914; 16.
DR   IntAct; P92961; 16.
DR   STRING; 3702.AT2G39890.1; -.
DR   TCDB; 2.A.18.3.1; the amino acid/auxin permease (aaap) family.
DR   PaxDb; P92961; -.
DR   PRIDE; P92961; -.
DR   ProteomicsDB; 226375; -.
DR   EnsemblPlants; AT2G39890.1; AT2G39890.1; AT2G39890.
DR   EnsemblPlants; AT2G39890.2; AT2G39890.2; AT2G39890.
DR   GeneID; 818576; -.
DR   Gramene; AT2G39890.1; AT2G39890.1; AT2G39890.
DR   Gramene; AT2G39890.2; AT2G39890.2; AT2G39890.
DR   KEGG; ath:AT2G39890; -.
DR   Araport; AT2G39890; -.
DR   TAIR; locus:2061156; AT2G39890.
DR   eggNOG; KOG1303; Eukaryota.
DR   HOGENOM; CLU_031160_3_0_1; -.
DR   InParanoid; P92961; -.
DR   OMA; SITWALQ; -.
DR   OrthoDB; 570025at2759; -.
DR   PhylomeDB; P92961; -.
DR   SABIO-RK; P92961; -.
DR   PRO; PR:P92961; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P92961; baseline and differential.
DR   Genevisible; P92961; 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   Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..442
FT                   /note="Proline transporter 1"
FT                   /id="PRO_0000418993"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        351..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        372..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        411..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        82
FT                   /note="A -> T (in Ref. 4; AAM65420)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   442 AA;  48456 MW;  C630B01CE9A54A2C CRC64;
     MTATEAKNRK INVGDGDDVV DIEIPDTAHQ ISSDSWFQVA FVLTTGINSA YVLGYSGTIM
     VPLGWIGGVV GLLIATAISL YANTLIAKLH EFGGRRHIRY RDLAGFIYGR KAYHLTWGLQ
     YVNLFMINCG FIILAGSALK AVYVLFRDDH TMKLPHFIAI AGLICAIFAI GIPHLSALGV
     WLGVSTFLSL IYIVVAIVLS VRDGVKTPSR DYEIQGSSLS KLFTITGAAA NLVFAFNTGM
     LPEIQATVRQ PVVKNMMKAL YFQFTAGVLP MYAVTFIGYW AYGSSTSTYL LNSVNGPLWV
     KALANVSAIL QSVISLHIFA SPTYEYMDTK YGIKGNPFAI KNLLFRIMAR GGYIAVSTLI
     SALLPFLGDF MSLTGAVSTF PLTFILANHM YYKAKNNKLN AMQKLWHWLN VVFFSLMSVA
     AAIAAVRLIA VDSKNFHVFA DL
 
 
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