MTV1_ARATH
ID MTV1_ARATH Reviewed; 690 AA.
AC Q9C5H4; C0Z301; O04329; Q9LU19;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Protein MODIFIED TRANSPORT TO THE VACUOLE 1 {ECO:0000303|PubMed:23771894};
GN Name=MTV1 {ECO:0000303|PubMed:23771894};
GN OrderedLocusNames=At3g16270 {ECO:0000312|Araport:AT3G16270};
GN ORFNames=T02O04.23 {ECO:0000312|EMBL:AAB63649.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Rosette leaf;
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. 0:0-0(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
RP CLATHRIN, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=23771894; DOI=10.1105/tpc.113.111724;
RA Sauer M., Delgadillo M.O., Zouhar J., Reynolds G.D., Pennington J.G.,
RA Jiang L., Liljegren S.J., Stierhof Y.-D., De Jaeger G., Otegui M.S.,
RA Bednarek S.Y., Rojo E.;
RT "MTV1 and MTV4 encode plant-specific ENTH and ARF GAP proteins that mediate
RT clathrin-dependent trafficking of vacuolar cargo from the trans-Golgi
RT network.";
RL Plant Cell 25:2217-2235(2013).
RN [9]
RP STRUCTURE BY NMR OF 9-135.
RX PubMed=15014234; DOI=10.1023/b:jnmr.0000019239.44783.66;
RA Lopez-Mendez B., Pantoja-Uceda D., Tomizawa T., Koshiba S., Kigawa T.,
RA Shirouzu M., Terada T., Inoue M., Yabuki T., Aoki M., Seki E., Matsuda T.,
RA Hirota H., Yoshida M., Tanaka A., Osanai T., Seki M., Shinozaki K.,
RA Yokoyama S., Guntert P.;
RT "NMR assignment of the hypothetical ENTH-VHS domain At3g16270 from
RT Arabidopsis thaliana.";
RL J. Biomol. NMR 29:205-206(2004).
RN [10]
RP STRUCTURE BY NMR OF 9-135.
RX PubMed=17017791; DOI=10.1021/ja061136l;
RA Lopez-Mendez B., Guntert P.;
RT "Automated protein structure determination from NMR spectra.";
RL J. Am. Chem. Soc. 128:13112-13122(2006).
CC -!- FUNCTION: Mediates clathrin-dependent trafficking of vacuolar cargo
CC from the trans-Golgi network (TGN). Promotes plant growth.
CC {ECO:0000269|PubMed:23771894}.
CC -!- SUBUNIT: Binds to clathrin heavy chain. {ECO:0000269|PubMed:23771894}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:23771894}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000269|PubMed:23771894}. Note=Colocalizes with clathrin
CC at the trans-Golgi network (TGN). {ECO:0000269|PubMed:23771894}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C5H4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C5H4-2; Sequence=VSP_059635;
CC -!- TISSUE SPECIFICITY: Expressed in inflorescence stems, stigmas, roots,
CC roots meristems, embryos, and floral and leaf vasculatures, but absent
CC from the floral abscission zone. {ECO:0000269|PubMed:23771894}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in developing and mature
CC embryos. {ECO:0000269|PubMed:23771894}.
CC -!- DISRUPTION PHENOTYPE: Abnormal vacuolar trafficking of soluble cargo
CC proteins, and premature termination of the shoot apical meristem and of
CC floral meristems. Plant missing both AGD5 and MTV1 are severely
CC dwarfed, develop short siliques, exhibit abscission defect, and have
CC altered subcellular distribution of clathrin-coated vesicle (CCV) cargo
CC exported from the trans-Golgi network (TGN).
CC {ECO:0000269|PubMed:23771894}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB63649.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB01267.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC001645; AAB63649.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB023046; BAB01267.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75792.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64206.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64207.1; -; Genomic_DNA.
DR EMBL; AF360245; AAK25955.1; -; mRNA.
DR EMBL; AY040043; AAK64101.1; -; mRNA.
DR EMBL; AK318965; BAH57080.1; -; mRNA.
DR RefSeq; NP_001326251.1; NM_001338225.1. [Q9C5H4-1]
DR RefSeq; NP_001326252.1; NM_001338226.1. [Q9C5H4-1]
DR RefSeq; NP_566540.1; NM_112498.4. [Q9C5H4-1]
DR PDB; 1VDY; NMR; -; A=9-135.
DR PDB; 2DCP; NMR; -; A=9-135.
DR PDBsum; 1VDY; -.
DR PDBsum; 2DCP; -.
DR AlphaFoldDB; Q9C5H4; -.
DR BMRB; Q9C5H4; -.
DR SMR; Q9C5H4; -.
DR BioGRID; 6207; 3.
DR IntAct; Q9C5H4; 1.
DR STRING; 3702.AT3G16270.1; -.
DR iPTMnet; Q9C5H4; -.
DR PaxDb; Q9C5H4; -.
DR PRIDE; Q9C5H4; -.
DR ProteomicsDB; 238489; -. [Q9C5H4-1]
DR EnsemblPlants; AT3G16270.1; AT3G16270.1; AT3G16270. [Q9C5H4-1]
DR EnsemblPlants; AT3G16270.2; AT3G16270.2; AT3G16270. [Q9C5H4-1]
DR EnsemblPlants; AT3G16270.3; AT3G16270.3; AT3G16270. [Q9C5H4-1]
DR GeneID; 820873; -.
DR Gramene; AT3G16270.1; AT3G16270.1; AT3G16270. [Q9C5H4-1]
DR Gramene; AT3G16270.2; AT3G16270.2; AT3G16270. [Q9C5H4-1]
DR Gramene; AT3G16270.3; AT3G16270.3; AT3G16270. [Q9C5H4-1]
DR KEGG; ath:AT3G16270; -.
DR Araport; AT3G16270; -.
DR TAIR; locus:2094887; AT3G16270.
DR eggNOG; ENOG502QV38; Eukaryota.
DR HOGENOM; CLU_429860_0_0_1; -.
DR InParanoid; Q9C5H4; -.
DR OMA; SWQVRVK; -.
DR OrthoDB; 432528at2759; -.
DR PhylomeDB; Q9C5H4; -.
DR EvolutionaryTrace; Q9C5H4; -.
DR PRO; PR:Q9C5H4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9C5H4; baseline and differential.
DR Genevisible; Q9C5H4; AT.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0035652; P:clathrin-coated vesicle cargo loading; IMP:UniProtKB.
DR CDD; cd03572; ENTH_like_Tepsin; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR035802; ENTH/VHS_tepsin.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR039273; TEPSIN.
DR InterPro; IPR002014; VHS_dom.
DR PANTHER; PTHR21514; PTHR21514; 1.
DR Pfam; PF01417; ENTH; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50179; VHS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasmic vesicle; Golgi apparatus;
KW Reference proteome.
FT CHAIN 1..690
FT /note="Protein MODIFIED TRANSPORT TO THE VACUOLE 1"
FT /id="PRO_0000278823"
FT DOMAIN 20..150
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT REGION 228..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 678..690
FT /note="DHLTSARDTKRVS -> VSFAILLLIFDSKVWSICHLSLYM (in
FT isoform 2)"
FT /id="VSP_059635"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:1VDY"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:2DCP"
FT HELIX 30..42
FT /evidence="ECO:0007829|PDB:1VDY"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:1VDY"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1VDY"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:1VDY"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:1VDY"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:1VDY"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:1VDY"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:1VDY"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1VDY"
FT HELIX 114..129
FT /evidence="ECO:0007829|PDB:1VDY"
SQ SEQUENCE 690 AA; 74892 MW; 2B378B4AE7152C0D CRC64;
MDTSRRAVES YWRSRMIDAV TSDEDKVAPV YKLEEICDLL RSSHVSIVKE FSEFILKRLD
NKSPIVKQKA LRLIKYAVGK SGSEFRREMQ RNSVAVRNLF HYKGHPDPLK GDALNKAVRE
TAHETISAIF SEENGTKPAA PESINRRIEG FGNTNFQVPS NDNKSFLSEV VGIGSASIKQ
GISNFAQGHL PKKNENGSSS YRGPNLHRSL TMENENFSRY DPVKLGKDGN YGTSKNTTGG
SWGHASGEAS ESSASVRVES KTREEKLLET IVTSGGVRLQ PTRDALHVFI LEAAKMDAVA
LSIALDGKLH SPMWQVRMKA LCVLEAILRK KEDENFSIVH TYFSENLDAI QRCAESPQSS
LREKANKVLS LLNGGQSSGL MSSSDNTVKR EAAVDLPDLI DTGDSDDTLN NLNAIDTGST
VATAGPLMDD DWFGDSSDIG LSSSEKKTDD DPFADVSFHP NEEKESADDL FSGMTVGEKS
AAVGGNHVPD LFDMFGSTAK LEAEPKDAKN INDLMGSFSI DENNSNQKGS SSSTLPQDLF
AMPSTTSHQA PENPVGGILG SQNPGFIQNT MLPGGVMPFN FPQGMMMNPA FASQPLNYAA
MASLLAQQQQ YLGNMSNFQQ FGNLNAQGSG NVLSMGTSGG NQSALPDIFQ PNFGNQAPTS
TMNGSKKEDT RAFDFISDHL TSARDTKRVS
