VAP11_ARATH
ID VAP11_ARATH Reviewed; 256 AA.
AC Q8VZ95; B9DHW7; Q2V3M6; Q2V3M7; Q8LDM1; Q9M003;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Vesicle-associated protein 1-1;
DE AltName: Full=Plant VAP homolog 11;
DE Short=AtPVA11;
DE AltName: Full=VAMP-associated protein 1-1;
DE AltName: Full=Vesicle-associated protein 27-1;
DE Contains:
DE RecName: Full=Vesicle-associated protein 1-1, N-terminally processed;
GN Name=PVA11; Synonyms=VAP27, VAP27-1; OrderedLocusNames=At3g60600;
GN ORFNames=T4C21.10;
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], AND INTERACTION WITH COWPEA MOSAIC VIRUS NTB
RP PROTEIN.
RX PubMed=11907339; DOI=10.1099/0022-1317-83-4-885;
RA Carette J.E., Verver J., Martens J., van Kampen T., Wellink J.,
RA van Kammen A.;
RT "Characterization of plant proteins that interact with cowpea mosaic virus
RT '60K' protein in the yeast two-hybrid system.";
RL J. Gen. Virol. 83:885-893(2002).
RN [2]
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 [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] (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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 128-256 (ISOFORM 1).
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=16227454; DOI=10.1105/tpc.105.035212;
RA Oufattole M., Park J.H., Poxleitner M., Jiang L., Rogers J.C.;
RT "Selective membrane protein internalization accompanies movement from the
RT endoplasmic reticulum to the protein storage vacuole pathway in
RT Arabidopsis.";
RL Plant Cell 17:3066-3080(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [10]
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 [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH NET3C, AND
RP MUTAGENESIS OF 59-LYS--TYR-61.
RX PubMed=24909329; DOI=10.1016/j.cub.2014.05.003;
RA Wang P., Hawkins T.J., Richardson C., Cummins I., Deeks M.J., Sparkes I.,
RA Hawes C., Hussey P.J.;
RT "The plant cytoskeleton, NET3C, and VAP27 mediate the link between the
RT plasma membrane and endoplasmic reticulum.";
RL Curr. Biol. 24:1397-1405(2014).
CC -!- FUNCTION: Part of a membrane-cytoskeletal adapter complex that forms a
CC bridge between the endoplasmic reticulum and the plasma membrane.
CC Associates with microtubules. {ECO:0000269|PubMed:24909329}.
CC -!- SUBUNIT: Homodimer or homooligomer (PubMed:24909329). Interacts with
CC the cowpea mosaic virus (CPMV) NTP-binding protein (NTB)
CC (PubMed:11907339). Interacts with NET3C (PubMed:24909329).
CC {ECO:0000269|PubMed:11907339, ECO:0000269|PubMed:24909329}.
CC -!- INTERACTION:
CC Q8VZ95; Q84W04: At1g12390; NbExp=2; IntAct=EBI-2010972, EBI-4444417;
CC Q8VZ95; Q9SHG7: At1g17080; NbExp=3; IntAct=EBI-2010972, EBI-4436589;
CC Q8VZ95; Q9LXV1: At5g12880; NbExp=3; IntAct=EBI-2010972, EBI-4430604;
CC Q8VZ95; P93004: PIP2-7; NbExp=3; IntAct=EBI-2010972, EBI-4434233;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16227454, ECO:0000269|PubMed:24909329}; Single-pass
CC type IV membrane protein {ECO:0000269|PubMed:16227454}. Protein storage
CC vacuole membrane {ECO:0000269|PubMed:16227454}; Single-pass type IV
CC membrane protein {ECO:0000269|PubMed:16227454}; Cytoplasmic side
CC {ECO:0000269|PubMed:16227454}. Note=Localizes to immobile punctate
CC structures reminiscent of the ER-plasma membrane contact sites.
CC {ECO:0000269|PubMed:24909329}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8VZ95-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VZ95-2; Sequence=VSP_040252, VSP_040255;
CC Name=3;
CC IsoId=Q8VZ95-3; Sequence=VSP_040253, VSP_040254;
CC -!- SIMILARITY: Belongs to the VAMP-associated protein (VAP) (TC 9.B.17)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM63134.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM63134.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BX824970; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=CAB82664.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY364005; AAQ63968.1; -; mRNA.
DR EMBL; AL162295; CAB82664.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80086.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80087.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80088.1; -; Genomic_DNA.
DR EMBL; AY065144; AAL38320.1; -; mRNA.
DR EMBL; BT006297; AAP13405.1; -; mRNA.
DR EMBL; BX822165; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX824970; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY085922; AAM63134.1; ALT_SEQ; mRNA.
DR EMBL; AK317675; BAH20334.1; -; mRNA.
DR PIR; T47871; T47871.
DR RefSeq; NP_001030903.1; NM_001035826.1. [Q8VZ95-3]
DR RefSeq; NP_001030904.1; NM_001035827.1. [Q8VZ95-2]
DR RefSeq; NP_567101.1; NM_115924.4. [Q8VZ95-1]
DR AlphaFoldDB; Q8VZ95; -.
DR SMR; Q8VZ95; -.
DR BioGRID; 10545; 104.
DR IntAct; Q8VZ95; 90.
DR STRING; 3702.AT3G60600.1; -.
DR iPTMnet; Q8VZ95; -.
DR SwissPalm; Q8VZ95; -.
DR PaxDb; Q8VZ95; -.
DR PRIDE; Q8VZ95; -.
DR ProteomicsDB; 228551; -. [Q8VZ95-1]
DR EnsemblPlants; AT3G60600.1; AT3G60600.1; AT3G60600. [Q8VZ95-1]
DR EnsemblPlants; AT3G60600.2; AT3G60600.2; AT3G60600. [Q8VZ95-3]
DR EnsemblPlants; AT3G60600.3; AT3G60600.3; AT3G60600. [Q8VZ95-2]
DR GeneID; 825231; -.
DR Gramene; AT3G60600.1; AT3G60600.1; AT3G60600. [Q8VZ95-1]
DR Gramene; AT3G60600.2; AT3G60600.2; AT3G60600. [Q8VZ95-3]
DR Gramene; AT3G60600.3; AT3G60600.3; AT3G60600. [Q8VZ95-2]
DR KEGG; ath:AT3G60600; -.
DR Araport; AT3G60600; -.
DR TAIR; locus:2101766; AT3G60600.
DR eggNOG; KOG0439; Eukaryota.
DR HOGENOM; CLU_036554_1_0_1; -.
DR InParanoid; Q8VZ95; -.
DR OMA; QSVIAPE; -.
DR PhylomeDB; Q8VZ95; -.
DR PRO; PR:Q8VZ95; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VZ95; baseline and differential.
DR Genevisible; Q8VZ95; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0000326; C:protein storage vacuole; IDA:TAIR.
DR GO; GO:0032586; C:protein storage vacuole membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; IBA:GO_Central.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IBA:GO_Central.
DR GO; GO:0046907; P:intracellular transport; TAS:TAIR.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000535; MSP_dom.
DR InterPro; IPR008962; PapD-like_sf.
DR InterPro; IPR016763; VAP.
DR PANTHER; PTHR10809; PTHR10809; 1.
DR Pfam; PF00635; Motile_Sperm; 1.
DR PIRSF; PIRSF019693; VAMP-associated; 1.
DR SUPFAM; SSF49354; SSF49354; 1.
DR PROSITE; PS50202; MSP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Endoplasmic reticulum;
KW Host-virus interaction; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..256
FT /note="Vesicle-associated protein 1-1"
FT /id="PRO_0000425783"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..256
FT /note="Vesicle-associated protein 1-1, N-terminally
FT processed"
FT /id="PRO_0000402169"
FT TOPO_DOM 1..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 22..142
FT /note="MSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00132"
FT REGION 142..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 187..232
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:B9DHD7"
FT MOD_RES 2
FT /note="N-acetylserine; in Vesicle-associated protein 1-1,
FT N-terminally processed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SHC8"
FT VAR_SEQ 176..230
FT /note="FERFIVDNKAGHQENTSEARALITKLTEEKQSAIQLNNRLQRELDQLRRESK
FT KSQ -> IFMFNFSLRDLSWTTRLDIKKTHLRYFSQFFQVCHRQNHVTSSFAFALFKTD
FT FWR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_040252"
FT VAR_SEQ 194..217
FT /note="ARALITKLTEEKQSAIQLNNRLQR -> VFFTILPSLSPSKPCDIIFCFCSV
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_040253"
FT VAR_SEQ 218..256
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_040254"
FT VAR_SEQ 231..256
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_040255"
FT MUTAGEN 59..61
FT /note="KTT->NAA: Loss of interaction with NET3C and no ER-
FT plasma membrane association."
FT /evidence="ECO:0000269|PubMed:24909329"
FT CONFLICT 146
FT /note="R -> Q (in Ref. 6; AAM63134)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 256 AA; 28473 MW; 2D17D79F0F736068 CRC64;
MSNIDLIGMS NRDLIGMSNS ELLTVEPLDL QFPFELKKQI SCSLYLTNKT DNNVAFKVKT
TNPKKYCVRP NTGVVLPRST CEVLVTMQAQ KEAPSDMQCK DKFLLQGVIA SPGVTAKEVT
PEMFSKEAGH RVEETKLRVT YVAPPRPPSP VHEGSEEGSS PRASVSDNGH GSEFSFERFI
VDNKAGHQEN TSEARALITK LTEEKQSAIQ LNNRLQRELD QLRRESKKSQ SGGIPFMYVL
LVGLIGLILG YIMKRT
