MTP11_ARATH
ID MTP11_ARATH Reviewed; 394 AA.
AC O80632; B9DI01;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Metal tolerance protein 11;
DE Short=AtMTP11;
GN Name=MTP11; OrderedLocusNames=At2g39450; ORFNames=F12L6.11;
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=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 [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].
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] OF 150-394.
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17559518; DOI=10.1111/j.1365-313x.2007.03138.x;
RA Delhaize E., Gruber B.D., Pittman J.K., White R.G., Leung H., Miao Y.,
RA Jiang L., Ryan P.R., Richardson A.E.;
RT "A role for the AtMTP11 gene of Arabidopsis in manganese transport and
RT tolerance.";
RL Plant J. 51:198-210(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17494768; DOI=10.1073/pnas.0609507104;
RA Peiter E., Montanini B., Gobert A., Pedas P., Husted S., Maathuis F.J.,
RA Blaudez D., Chalot M., Sanders D.;
RT "A secretory pathway-localized cation diffusion facilitator confers plant
RT manganese tolerance.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8532-8537(2007).
CC -!- FUNCTION: Cation/proton antiporter involved in endogenous manganese
CC tolerance probably through vesicular trafficking and exocytosis.
CC {ECO:0000269|PubMed:17494768, ECO:0000269|PubMed:17559518}.
CC -!- SUBCELLULAR LOCATION: Prevacuolar compartment membrane. Golgi apparatus
CC membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17494768}.
CC -!- DISRUPTION PHENOTYPE: Increased accumulation of manganese and
CC hypersensitivity to elevated levels of manganese.
CC {ECO:0000269|PubMed:17494768, ECO:0000269|PubMed:17559518}.
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
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DR EMBL; AC004218; AAC27836.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09679.1; -; Genomic_DNA.
DR EMBL; AY136449; AAM97114.1; -; mRNA.
DR EMBL; BT008477; AAP37836.1; -; mRNA.
DR EMBL; AK317710; BAH20368.1; -; mRNA.
DR PIR; T00555; T00555.
DR RefSeq; NP_181477.1; NM_129503.4.
DR AlphaFoldDB; O80632; -.
DR BioGRID; 3868; 2.
DR IntAct; O80632; 2.
DR STRING; 3702.AT2G39450.1; -.
DR TCDB; 2.A.4.5.5; the cation diffusion facilitator (cdf) family.
DR PaxDb; O80632; -.
DR PRIDE; O80632; -.
DR ProteomicsDB; 251306; -.
DR EnsemblPlants; AT2G39450.1; AT2G39450.1; AT2G39450.
DR GeneID; 818530; -.
DR Gramene; AT2G39450.1; AT2G39450.1; AT2G39450.
DR KEGG; ath:AT2G39450; -.
DR Araport; AT2G39450; -.
DR TAIR; locus:2039697; AT2G39450.
DR eggNOG; KOG1485; Eukaryota.
DR HOGENOM; CLU_013430_2_3_1; -.
DR InParanoid; O80632; -.
DR OMA; SKLKWWI; -.
DR OrthoDB; 874665at2759; -.
DR PhylomeDB; O80632; -.
DR PRO; PR:O80632; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80632; baseline and differential.
DR Genevisible; O80632; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0010486; F:manganese:proton antiporter activity; IDA:TAIR.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IMP:TAIR.
DR GO; GO:0046688; P:response to copper ion; IDA:TAIR.
DR GO; GO:0010042; P:response to manganese ion; IDA:TAIR.
DR Gene3D; 1.20.1510.10; -; 1.
DR Gene3D; 3.30.70.1350; -; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR027470; Cation_efflux_CTD.
DR InterPro; IPR036837; Cation_efflux_CTD_sf.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR Pfam; PF01545; Cation_efflux; 1.
DR Pfam; PF16916; ZT_dimer; 1.
DR SUPFAM; SSF160240; SSF160240; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 2: Evidence at transcript level;
KW Golgi apparatus; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..394
FT /note="Metal tolerance protein 11"
FT /id="PRO_0000400007"
FT TOPO_DOM 1..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..130
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..212
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 394 AA; 44631 MW; 3EE85971D17BC51C CRC64;
MVEPASPDSD EGISLLEFHG NGDRSWQLNF DDFQVSPEHK EKKSPSKLHN CLGCLGPEDN
VADYYQQQVE MLEGFTEMDE LAERGFVPGM SKEEQDNLAK SETLAIRISN IANMLLFAAK
VYASVTSGSL AIIASTLDSL LDLLSGFILW FTAFSMQTPN PYQYPIGKKR MQPLGILVFA
SVMATLGLQI ILESLRTMLS SHKEFNLTKE QESWVVGIML SVTLVKLLLV LYCRSFTNEI
VKAYAQDHFF DVITNIIGLI AVILANYIDY WIDPVGAIIL ALYTIRTWSM TVLENVNSLV
GKSARPEYLQ KLTYLCWNHH KAIRHIDTVR AYTFGSHYFV EVDIVLPADM PLQVAHDIGE
SLQEKLELLE EIERAFVHLD YEYTHKPEHA RSHC
