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INT2_ARATH
ID   INT2_ARATH              Reviewed;         580 AA.
AC   Q9C757;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Probable inositol transporter 2;
GN   Name=INT2; OrderedLocusNames=At1g30220; ORFNames=F12P21.2;
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].
RX   PubMed=16603666; DOI=10.1104/pp.106.077123;
RA   Schneider S., Schneidereit A., Konrad K.R., Hajirezaei M.-R., Gramann M.,
RA   Hedrich R., Sauer N.;
RT   "Arabidopsis INOSITOL TRANSPORTER4 mediates high-affinity H+ symport of
RT   myoinositol across the plasma membrane.";
RL   Plant Physiol. 141:565-577(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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].
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   GENE FAMILY.
RX   PubMed=16923188; DOI=10.1186/1471-2148-6-64;
RA   Johnson D.A., Hill J.P., Thomas M.A.;
RT   "The monosaccharide transporter gene family in land plants is ancient and
RT   shows differential subfamily expression and expansion across lineages.";
RL   BMC Evol. Biol. 6:64-64(2006).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP   SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=17951450; DOI=10.1104/pp.107.109033;
RA   Schneider S., Schneidereit A., Udvardi P., Hammes U., Gramann M.,
RA   Dietrich P., Sauer N.;
RT   "Arabidopsis INOSITOL TRANSPORTER2 mediates H+ symport of different
RT   inositol epimers and derivatives across the plasma membrane.";
RL   Plant Physiol. 145:1395-1407(2007).
RN   [7]
RP   DOMAIN, MUTAGENESIS OF CYS-399; CYS-402; CYS-410 AND CYS-413, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=20230529; DOI=10.1111/j.1600-0854.2010.01057.x;
RA   Dotzauer D., Wolfenstetter S., Eibert D., Schneider S., Dietrich P.,
RA   Sauer N.;
RT   "Novel PSI domains in plant and animal H+-inositol symporters.";
RL   Traffic 11:767-781(2010).
CC   -!- FUNCTION: Plasma membrane inositol-proton symporter. Specific for
CC       several inositol epimers, such as myoinositol and scylloinositol. D-
CC       chiroinositol, mucoinositol, alloinositol and pinitol are also
CC       transported with a lower activity. Not active with galactinol and
CC       phytate. {ECO:0000269|PubMed:17951450}.
CC   -!- ACTIVITY REGULATION: Inhibited by nickel and to a lesser extent by
CC       cobalt.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.16 mM for inositol {ECO:0000269|PubMed:17951450,
CC         ECO:0000269|PubMed:20230529};
CC       pH dependence:
CC         Optimum pH is 5.5-7.0. {ECO:0000269|PubMed:17951450,
CC         ECO:0000269|PubMed:20230529};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17951450};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:17951450}.
CC   -!- TISSUE SPECIFICITY: Expressed in the tapetum, but not in pollen grains.
CC       Detected in leaf vascular tissue and in roots.
CC       {ECO:0000269|PubMed:17951450}.
CC   -!- DOMAIN: The PSI domain (383-450) is not involved in the plasma membrane
CC       targeting and is dispensable for the transport function, but is
CC       required for the inhibition by nickel. {ECO:0000269|PubMed:20230529}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000269|PubMed:17951450}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR   EMBL; AJ973176; CAJ00304.1; -; mRNA.
DR   EMBL; AC073506; AAG50560.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31194.1; -; Genomic_DNA.
DR   EMBL; AY074333; AAL67029.1; -; mRNA.
DR   EMBL; AY123031; AAM67564.1; -; mRNA.
DR   PIR; D86426; D86426.
DR   RefSeq; NP_174313.1; NM_102761.4.
DR   AlphaFoldDB; Q9C757; -.
DR   SMR; Q9C757; -.
DR   STRING; 3702.AT1G30220.1; -.
DR   TCDB; 2.A.1.1.63; the major facilitator superfamily (mfs).
DR   PaxDb; Q9C757; -.
DR   PRIDE; Q9C757; -.
DR   ProteomicsDB; 248466; -.
DR   EnsemblPlants; AT1G30220.1; AT1G30220.1; AT1G30220.
DR   GeneID; 839902; -.
DR   Gramene; AT1G30220.1; AT1G30220.1; AT1G30220.
DR   KEGG; ath:AT1G30220; -.
DR   Araport; AT1G30220; -.
DR   TAIR; locus:2009832; AT1G30220.
DR   eggNOG; KOG0254; Eukaryota.
DR   HOGENOM; CLU_001265_30_5_1; -.
DR   InParanoid; Q9C757; -.
DR   OMA; PECGFCA; -.
DR   OrthoDB; 326501at2759; -.
DR   PhylomeDB; Q9C757; -.
DR   PRO; PR:Q9C757; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C757; baseline and differential.
DR   Genevisible; Q9C757; 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:0090406; C:pollen tube; TAS:TAIR.
DR   GO; GO:0005366; F:myo-inositol:proton symporter activity; IDA:TAIR.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015798; P:myo-inositol transport; IDA:TAIR.
DR   GO; GO:0023052; P:signaling; TAS:TAIR.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.20.1250.20; -; 2.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR003663; Sugar/inositol_transpt.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF00083; Sugar_tr; 2.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00879; SP; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Reference proteome; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..580
FT                   /note="Probable inositol transporter 2"
FT                   /id="PRO_0000259876"
FT   TRANSMEM        36..56
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..295
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..335
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        452..472
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        490..510
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        521..541
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         399
FT                   /note="C->A: Strongly decreased nickel inhibition; when
FT                   associated with A-402, A-410 and A-413."
FT                   /evidence="ECO:0000269|PubMed:20230529"
FT   MUTAGEN         399
FT                   /note="C->S: No effect on inostol transport or nickel
FT                   inhibition. No effect on inostol transport or nickel
FT                   inhibition; when associated with S-410."
FT                   /evidence="ECO:0000269|PubMed:20230529"
FT   MUTAGEN         402
FT                   /note="C->A: Strongly decreased nickel inhibition; when
FT                   associated with A-399, A-410 and A-413."
FT                   /evidence="ECO:0000269|PubMed:20230529"
FT   MUTAGEN         410
FT                   /note="C->A: Strongly decreased nickel inhibition; when
FT                   associated with A-399, A-402 and A-413."
FT                   /evidence="ECO:0000269|PubMed:20230529"
FT   MUTAGEN         410
FT                   /note="C->S: No effect on inostol transport or nickel
FT                   inhibition; when associated with S-399."
FT                   /evidence="ECO:0000269|PubMed:20230529"
FT   MUTAGEN         413
FT                   /note="C->A: Strongly decreased nickel inhibition; when
FT                   associated with A-399, A-402 and A-410."
FT                   /evidence="ECO:0000269|PubMed:20230529"
SQ   SEQUENCE   580 AA;  63449 MW;  B8E03518F05EED79 CRC64;
     MEGGIIHGGA DESAFKECFS LTWKNPYVLR LAFSAGIGGL LFGYDTGVIS GALLYIRDDF
     KSVDRNTWLQ EMIVSMAVAG AIVGAAIGGW ANDKLGRRSA ILMADFLFLL GAIIMAAAPN
     PSLLVVGRVF VGLGVGMASM TAPLYISEAS PAKIRGALVS TNGFLITGGQ FLSYLINLAF
     TDVTGTWRWM LGIAGIPALL QFVLMFTLPE SPRWLYRKGR EEEAKAILRR IYSAEDVEQE
     IRALKDSVET EILEEGSSEK INMIKLCKAK TVRRGLIAGV GLQVFQQFVG INTVMYYSPT
     IVQLAGFASN RTALLLSLVT AGLNAFGSII SIYFIDRIGR KKLLIISLFG VIISLGILTG
     VFYEAATHAP AISSLETQRF NNISCPDYKS AMNTNAWDCM TCLKASSPSC GYCSSPIGKE
     HPGACWISDD SVKDLCHNEN RLWYTRGCPS NFGWFALLGL GLYIIFFSPG MGTVPWIVNS
     EIYPLRFRGI CGGIAATANW ISNLIVAQSF LSLTEAIGTS WTFLIFGVIS VIALLFVMVC
     VPETKGMPME EIEKMLERRS MEFKFWKKKS KLVEKQNQSA
 
 
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