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LAX1_ARATH
ID   LAX1_ARATH              Reviewed;         488 AA.
AC   Q9LFB2; Q9SMW2;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Auxin transporter-like protein 1;
DE   AltName: Full=AUX1-like protein 1;
GN   Name=LAX1; OrderedLocusNames=At5g01240; ORFNames=F7J8_220;
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], GENE FAMILY, AND NOMENCLATURE.
RX   DOI=10.1007/s003440010030;
RA   Parry P.G., Marchant A., May S.T., Swarup R., Swarup K., James N.,
RA   Graham N., Allen T., Martucci T., Yemm A., Napier R., Manning K., King G.,
RA   Bennett M.J.;
RT   "Quick on the uptake: characterization of a family of plant auxin influx
RT   carriers.";
RL   J. Plant Growth Regul. 20:217-225(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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).
CC   -!- FUNCTION: Carrier protein involved in proton-driven auxin influx.
CC       Mediates the formation of auxin gradient from developing leaves (site
CC       of auxin biosynthesis) to tips by contributing to the loading of auxin
CC       in vascular tissues and facilitating acropetal (base to tip) auxin
CC       transport within inner tissues of the root apex, and basipetal (tip to
CC       base) auxin transport within outer tissues of the root apex (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9LFB2-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC       Amino acid/auxin permease (AAAP) (TC 2.A.18.1) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ249442; CAB55758.1; -; mRNA.
DR   EMBL; AL137189; CAB69852.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90315.1; -; Genomic_DNA.
DR   PIR; T45964; T45964.
DR   RefSeq; NP_195744.1; NM_120202.5. [Q9LFB2-1]
DR   AlphaFoldDB; Q9LFB2; -.
DR   BioGRID; 17142; 1.
DR   STRING; 3702.AT5G01240.1; -.
DR   iPTMnet; Q9LFB2; -.
DR   PaxDb; Q9LFB2; -.
DR   PRIDE; Q9LFB2; -.
DR   ProteomicsDB; 237076; -. [Q9LFB2-1]
DR   EnsemblPlants; AT5G01240.1; AT5G01240.1; AT5G01240. [Q9LFB2-1]
DR   GeneID; 831866; -.
DR   Gramene; AT5G01240.1; AT5G01240.1; AT5G01240. [Q9LFB2-1]
DR   KEGG; ath:AT5G01240; -.
DR   Araport; AT5G01240; -.
DR   TAIR; locus:2150089; AT5G01240.
DR   eggNOG; KOG1303; Eukaryota.
DR   InParanoid; Q9LFB2; -.
DR   OMA; FANCYQC; -.
DR   OrthoDB; 509343at2759; -.
DR   PhylomeDB; Q9LFB2; -.
DR   PRO; PR:Q9LFB2; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LFB2; baseline and differential.
DR   Genevisible; Q9LFB2; 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; HDA:TAIR.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0010328; F:auxin influx transmembrane transporter activity; IDA:TAIR.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR   GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0048829; P:root cap development; IGI:TAIR.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   Pfam; PF01490; Aa_trans; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Amino-acid transport; Auxin signaling pathway;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..488
FT                   /note="Auxin transporter-like protein 1"
FT                   /id="PRO_0000093842"
FT   TOPO_DOM        1..64
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        83..84
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        106..141
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..178
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        200..202
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        224..238
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        260..273
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        295..320
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        342..362
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        384
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        406..427
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        449..488
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        16..17
FT                   /note="ED -> DE (in Ref. 1; CAB55758)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        293
FT                   /note="V -> L (in Ref. 1; CAB55758)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        365..366
FT                   /note="VV -> C (in Ref. 1; CAB55758)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        372..373
FT                   /note="LA -> WP (in Ref. 1; CAB55758)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        379..381
FT                   /note="FGP -> SA (in Ref. 1; CAB55758)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        413..416
FT                   /note="RRNA -> AER (in Ref. 1; CAB55758)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   488 AA;  54601 MW;  06B0BF524EDE2BD8 CRC64;
     MSGEKQAEES IVVSGEDEVA GRKVEDSAAE EDIDGNGGNG FSMKSFLWHG GSAWDAWFSC
     ASNQVAQVLL TLPYSFSQLG MLSGILLQIF YGLMGSWTAY LISVLYVEYR ARMEKQEAKS
     FKNHVIQWFE VLDGLLGPYW KAAGLAFNCT FLLFGSVIQL IACASNIYYI NDRLDKRTWT
     YIFGACCATT VFIPSFHNYR IWSFLGLGMT TYTAWYLTIA SFLHGQAEGV THSGPTKLVL
     YFTGATNILY TFGGHAVTVE IMHAMWKPRK FKSIYLMATL YVFTLTLPSA SAVYWAFGDQ
     LLNHSNAFSL LPKTRFRDTA VILMLIHQFI TFGFACTPLY FVWEKAIGMH HTKSLCLRAL
     VRLPVVVPIW FLAIIFPFFG PINSAVGALL VTFTVYIIPA LAHMLTYRTA SARRNAAEKP
     PFFIPSWAGV YVINAFIVVW VLVLGFGFGG WASMTNFIRQ IDTFGLFAKC YQCKPPPAPI
     AAGAHHRR
 
 
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