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BASS5_ARATH
ID   BASS5_ARATH             Reviewed;         407 AA.
AC   F4JPW1; Q94A17; Q9SZ68;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Probable sodium/metabolite cotransporter BASS5, chloroplastic;
DE   AltName: Full=Bile acid transporter 5;
DE   AltName: Full=Bile acid-sodium symporter family protein 5;
DE   Flags: Precursor;
GN   Name=BASS5; Synonyms=BAT5; OrderedLocusNames=At4g12030;
GN   ORFNames=F16J13.100;
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=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   [2]
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   [3]
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   [4]
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   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19542295; DOI=10.1105/tpc.109.066399;
RA   Gigolashvili T., Yatusevich R., Rollwitz I., Humphry M., Gershenzon J.,
RA   Fluegge U.-I.;
RT   "The plastidic bile acid transporter 5 is required for the biosynthesis of
RT   methionine-derived glucosinolates in Arabidopsis thaliana.";
RL   Plant Cell 21:1813-1829(2009).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19633020; DOI=10.1093/pcp/pcp110;
RA   Sawada Y., Toyooka K., Kuwahara A., Sakata A., Nagano M., Saito K.,
RA   Hirai M.Y.;
RT   "Arabidopsis bile acid:sodium symporter family protein 5 is involved in
RT   methionine-derived glucosinolate biosynthesis.";
RL   Plant Cell Physiol. 50:1579-1586(2009).
CC   -!- FUNCTION: Plastidic transporter involved in the biosynthesis of
CC       aliphatic glucosinolates by translocating the biosynthetic
CC       intermediates of Met-derived glucosinolates across chloroplast
CC       membranes. Transports short chain (C2) alpha-keto acids, such as 4-
CC       methylsulfanyl-2-oxobutanoic acid, from the cytosol to the chloroplast
CC       where they are subjected to chain elongation cycles. Functions also in
CC       the transport of chain-elongated (C3 to C8) Met derivatives from the
CC       chloroplast to the cytosol. Does not seem to be involved in the
CC       transport of indole-derived glucosinolates.
CC       {ECO:0000269|PubMed:19542295, ECO:0000269|PubMed:19633020}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:19542295}; Multi-
CC       pass membrane protein {ECO:0000305|PubMed:19542295}. Plastid,
CC       chloroplast envelope {ECO:0000305|PubMed:19542295}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=F4JPW1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=F4JPW1-2; Sequence=VSP_044057;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:19542295}.
CC   -!- INDUCTION: By wounding and methyl jasmonate (MeJa). Down-regulated by
CC       salicylic acid (SA). {ECO:0000269|PubMed:19542295}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but plants contain reduced levels of aliphatic
CC       glucosinolates. {ECO:0000269|PubMed:19542295,
CC       ECO:0000269|PubMed:19633020}.
CC   -!- SIMILARITY: Belongs to the bile acid:sodium symporter (BASS) (TC
CC       2.A.28) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK91464.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAB40944.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB78246.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL049638; CAB40944.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161533; CAB78246.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE83087.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83088.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66697.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66698.1; -; Genomic_DNA.
DR   EMBL; AY050449; AAK91464.1; ALT_FRAME; mRNA.
DR   EMBL; AY097358; AAM19874.1; -; mRNA.
DR   EMBL; BX828262; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; T06610; T06610.
DR   RefSeq; NP_001319909.1; NM_001340768.1. [F4JPW1-2]
DR   RefSeq; NP_001328579.1; NM_001340769.1. [F4JPW1-2]
DR   RefSeq; NP_567385.1; NM_117273.3. [F4JPW1-2]
DR   RefSeq; NP_974538.1; NM_202809.3. [F4JPW1-1]
DR   AlphaFoldDB; F4JPW1; -.
DR   SMR; F4JPW1; -.
DR   BioGRID; 12109; 2.
DR   IntAct; F4JPW1; 2.
DR   STRING; 3702.AT4G12030.2; -.
DR   PaxDb; F4JPW1; -.
DR   PRIDE; F4JPW1; -.
DR   ProteomicsDB; 240746; -. [F4JPW1-1]
DR   EnsemblPlants; AT4G12030.1; AT4G12030.1; AT4G12030. [F4JPW1-2]
DR   EnsemblPlants; AT4G12030.2; AT4G12030.2; AT4G12030. [F4JPW1-1]
DR   EnsemblPlants; AT4G12030.3; AT4G12030.3; AT4G12030. [F4JPW1-2]
DR   EnsemblPlants; AT4G12030.5; AT4G12030.5; AT4G12030. [F4JPW1-2]
DR   GeneID; 826811; -.
DR   Gramene; AT4G12030.1; AT4G12030.1; AT4G12030. [F4JPW1-2]
DR   Gramene; AT4G12030.2; AT4G12030.2; AT4G12030. [F4JPW1-1]
DR   Gramene; AT4G12030.3; AT4G12030.3; AT4G12030. [F4JPW1-2]
DR   Gramene; AT4G12030.5; AT4G12030.5; AT4G12030. [F4JPW1-2]
DR   KEGG; ath:AT4G12030; -.
DR   Araport; AT4G12030; -.
DR   TAIR; locus:2118021; AT4G12030.
DR   eggNOG; KOG2718; Eukaryota.
DR   HOGENOM; CLU_034788_3_1_1; -.
DR   InParanoid; F4JPW1; -.
DR   OrthoDB; 1148347at2759; -.
DR   PhylomeDB; F4JPW1; -.
DR   PRO; PR:F4JPW1; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JPW1; baseline and differential.
DR   Genevisible; F4JPW1; AT.
DR   GO; GO:0009941; C:chloroplast envelope; IMP:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009536; C:plastid; IDA:TAIR.
DR   GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; IMP:TAIR.
DR   GO; GO:0019761; P:glucosinolate biosynthetic process; IMP:TAIR.
DR   GO; GO:0033506; P:glucosinolate biosynthetic process from homomethionine; IMP:UniProtKB.
DR   GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR   GO; GO:0009611; P:response to wounding; IDA:TAIR.
DR   Gene3D; 1.20.1530.20; -; 1.
DR   InterPro; IPR002657; BilAc:Na_symport/Acr3.
DR   InterPro; IPR004710; Bilac:Na_transpt.
DR   InterPro; IPR038770; Na+/solute_symporter_sf.
DR   PANTHER; PTHR10361; PTHR10361; 1.
DR   Pfam; PF01758; SBF; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Chloroplast; Membrane; Plastid; Reference proteome;
KW   Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..57
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           58..407
FT                   /note="Probable sodium/metabolite cotransporter BASS5,
FT                   chloroplastic"
FT                   /id="PRO_0000418606"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        191..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..134
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14993207"
FT                   /id="VSP_044057"
FT   CONFLICT        153
FT                   /note="K -> N (in Ref. 4; BX828262)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   407 AA;  44582 MW;  1C0FB7E5700A3BD3 CRC64;
     MGVISPTETL FLKSQHRLLQ PRNYSYALAF HSTRRVANFP RNSFSSLGSC SVDFPLRSNP
     ISQNSKSIHP WRRYVSESDS NELYHKKVSS IMETLKQAYS FIPHGILLST ILALVYPPSF
     TWFKPRYFVP GLGFMMFAVG INSNERDFLE ALKRPDAIFA GYIGQYLIKP LLGYIFGVIA
     VSLFNLPTSI GAGIMLVSCV SGAQLSNYTT FLTDPSLAAL SIVMTSISTA TAVLVTPMLS
     LLLIGKKLPV DVFGMISSIL QVVITPIAAG LLLNRLFPRL SNAIKPFLPA LTVIDMSCCI
     GAPLALNIDS ILSPFGATIL FLVITFHLLA FVAGYFFTGF FFSKAPDVKA LQRTISYETG
     MQSSLLALAL ATKFFQDPLV GVPPAISTVV MSLMGVSLVT IWKNRKE
 
 
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