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OPT3_ARATH
ID   OPT3_ARATH              Reviewed;         737 AA.
AC   O23482; F4JLS9; Q8H0V0; Q940I5;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 3.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Oligopeptide transporter 3;
DE            Short=AtOPT3;
GN   Name=OPT3; OrderedLocusNames=At4g16370; ORFNames=dl4215c, FCAALL.72;
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=9461215; DOI=10.1038/35140;
RA   Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA   Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA   Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA   Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA   De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA   Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA   Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA   Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA   Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA   Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA   Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA   Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT   "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT   thaliana.";
RL   Nature 391:485-488(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION.
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].
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   FUNCTION, NOMENCLATURE, AND TISSUE SPECIFICITY.
RX   PubMed=11788749; DOI=10.1104/pp.010332;
RA   Koh S., Wiles A.M., Sharp J.S., Naider F.R., Becker J.M., Stacey G.;
RT   "An oligopeptide transporter gene family in Arabidopsis.";
RL   Plant Physiol. 128:21-29(2002).
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=12417702; DOI=10.1105/tpc.005629;
RA   Stacey M.G., Koh S., Becker J., Stacey G.;
RT   "AtOPT3, a member of the oligopeptide transporter family, is essential for
RT   embryo development in Arabidopsis.";
RL   Plant Cell 14:2799-2811(2002).
RN   [7]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=13129917; DOI=10.1074/jbc.m309338200;
RA   Wintz H., Fox T., Wu Y.-Y., Feng V., Chen W., Chang H.-S., Zhu T.,
RA   Vulpe C.D.;
RT   "Expression profiles of Arabidopsis thaliana in mineral deficiencies reveal
RT   novel transporters involved in metal homeostasis.";
RL   J. Biol. Chem. 278:47644-47653(2003).
CC   -!- FUNCTION: May be involved in the translocation of tetra- and
CC       pentapeptides across the cellular membrane in an energy-dependent
CC       manner. Acts also as a metal transporter that could be a component of
CC       the copper transport machinery. Essential for early embryo development.
CC       {ECO:0000269|PubMed:11788749, ECO:0000269|PubMed:12417702,
CC       ECO:0000269|PubMed:13129917}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Strong expression in flowers, leaves and roots.
CC       Preferentially expressed in the vascular tissues of seedlings and
CC       mature plants as well as in pollen and developing embryos.
CC       {ECO:0000269|PubMed:11788749, ECO:0000269|PubMed:12417702}.
CC   -!- DEVELOPMENTAL STAGE: Expressed 2 to 4 hours after fertilization in the
CC       embryo sac and subsequently in developing maternal tissues. By the
CC       globular stage, expression is observed in the developing endosperm,
CC       integument layers, the embryo proper, and the suspensor of the
CC       developing embryo. From the heart stage onward, expression observed in
CC       the embryo but neither in the suspensor nor in the endosperm and
CC       integument tissues. {ECO:0000269|PubMed:12417702}.
CC   -!- INDUCTION: Highly induced by iron, copper and manganese deficiencies.
CC       {ECO:0000269|PubMed:13129917}.
CC   -!- SIMILARITY: Belongs to the oligopeptide OPT transporter (TC 2.A.67.1)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB10414.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB78679.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; Z97341; CAB10414.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161543; CAB78679.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE83738.1; -; Genomic_DNA.
DR   EMBL; BT002023; AAN72034.1; -; mRNA.
DR   EMBL; AY054590; AAK96781.1; -; mRNA.
DR   PIR; D71430; D71430.
DR   RefSeq; NP_567493.5; NM_117732.7.
DR   AlphaFoldDB; O23482; -.
DR   STRING; 3702.AT4G16370.1; -.
DR   TCDB; 2.A.67.1.7; the oligopeptide transporter (opt) family.
DR   PaxDb; O23482; -.
DR   PRIDE; O23482; -.
DR   ProteomicsDB; 248817; -.
DR   GeneID; 827332; -.
DR   KEGG; ath:AT4G16370; -.
DR   Araport; AT4G16370; -.
DR   TAIR; locus:2130529; AT4G16370.
DR   eggNOG; KOG2262; Eukaryota.
DR   HOGENOM; CLU_004965_0_1_1; -.
DR   InParanoid; O23482; -.
DR   OrthoDB; 190227at2759; -.
DR   PRO; PR:O23482; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O23482; baseline and differential.
DR   Genevisible; O23482; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; ISS:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0035673; F:oligopeptide transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0046915; F:transition metal ion transmembrane transporter activity; IDA:TAIR.
DR   GO; GO:0006875; P:cellular metal ion homeostasis; IMP:TAIR.
DR   GO; GO:0055072; P:iron ion homeostasis; IDA:TAIR.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:1990388; P:xylem-to-phloem iron transport; IEP:TAIR.
DR   InterPro; IPR004648; Oligpept_transpt.
DR   InterPro; IPR004813; OPT.
DR   PANTHER; PTHR22601; PTHR22601; 1.
DR   Pfam; PF03169; OPT; 1.
DR   TIGRFAMs; TIGR00727; ISP4_OPT; 1.
DR   TIGRFAMs; TIGR00728; OPT_sfam; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Membrane; Peptide transport; Protein transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..737
FT                   /note="Oligopeptide transporter 3"
FT                   /id="PRO_0000213780"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        418..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        446..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        478..498
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        532..552
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        604..624
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        629..649
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        650..670
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        681..701
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        45
FT                   /note="A -> T (in Ref. 4; AAK96781)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        81
FT                   /note="V -> G (in Ref. 1; CAB10414 and 2; CAB78679)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        239
FT                   /note="F -> S (in Ref. 1; CAB10414 and 2; CAB78679)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        322
FT                   /note="F -> S (in Ref. 1; CAB10414 and 2; CAB78679)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        527
FT                   /note="R -> P (in Ref. 1; CAB10414 and 2; CAB78679)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        605..606
FT                   /note="WL -> GF (in Ref. 1; CAB10414 and 2; CAB78679)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        605
FT                   /note="W -> G (in Ref. 3; AEE83738)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   737 AA;  82441 MW;  8E3A03673C0C12D6 CRC64;
     MDAEKATDKT NVHLSSDHER CPVEEVALVV PETDDPSLPV MTFRAWFLGL TSCVLLIFLN
     TFFTYRTQPL TISAILMQIA VLPIGKFMAR TLPTTSHNLL GWSFSLNPGP FNIKEHVIIT
     IFANCGVAYG GGDAYSIGAI TVMKAYYKQS LSFICGLFIV LTTQILGYGW AGILRRYLVD
     PVDMWWPSNL AQVSLFRALH EKENKSKGLT RMKFFLVALG ASFIYYALPG YLFPILTFFS
     WVCWAWPNSI TAQQVGSGYH GLGVGAFTLD WAGISAYHGS PLVAPWSSIL NVGVGFIMFI
     YIIVPVCYWK FNTFDARKFP IFSNQLFTTS GQKYDTTKIL TPQFDLDIGA YNNYGKLYLS
     PLFALSIGSG FARFTATLTH VALFNGRDIW KQTWSAVNTT KLDIHGKLMQ SYKKVPEWWF
     YILLAGSVAM SLLMSFVWKE SVQLPWWGML FAFALAFIVT LPIGVIQATT NQQPGYDIIG
     QFIIGYILPG KPIANLIFKI YGRISTVHAL SFLADLKLGH YMKIPPRCMY TAQLVGTVVA
     GVVNLGVAWW MLESIQDICD IEGDHPNSPW TCPKYRVTFD ASVIWGLIGP RRLFGPGGMY
     RNLVWLFLIG AVLPVPVWAL SKIFPNKKWI PLINIPVISY GFAGMPPATP TNIASWLVTG
     TIFNYFVFNY HKRWWQKYNY VLSAALDAGT AFMGVLLFFA LQNAGHDLKW WGTEVDHCPL
     ASCPTAPGIK AKGCPVF
 
 
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