VAP12_ARATH
ID VAP12_ARATH Reviewed; 239 AA.
AC Q9SHC8;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Vesicle-associated protein 1-2;
DE AltName: Full=Plant VAP homolog 12;
DE Short=AtPVA12;
DE AltName: Full=VAMP-associated protein 1-2;
DE Contains:
DE RecName: Full=Vesicle-associated protein 1-2, N-terminally processed;
GN Name=PVA12; Synonyms=VAP12; OrderedLocusNames=At2g45140; ORFNames=T14P1.5;
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].
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-164, AND
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ORP3A.
RX PubMed=19207211; DOI=10.1111/j.1365-313x.2009.03815.x;
RA Saravanan R.S., Slabaugh E., Singh V.R., Lapidus L.J., Haas T.,
RA Brandizzi F.;
RT "The targeting of the oxysterol-binding protein ORP3a to the endoplasmic
RT reticulum relies on the plant VAP33 homolog PVA12.";
RL Plant J. 58:817-830(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-164, AND
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 [9]
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).
CC -!- FUNCTION: Vesicle-associated protein that binds the oxysterol-binding
CC protein ORP3A and allows its targeting to the ER.
CC {ECO:0000269|PubMed:19207211}.
CC -!- SUBUNIT: Interacts with ORP3A. {ECO:0000269|PubMed:19207211}.
CC -!- INTERACTION:
CC Q9SHC8; Q9LZM1: ORP3A; NbExp=3; IntAct=EBI-2292633, EBI-2292648;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19207211}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:19207211}; Cytoplasmic side
CC {ECO:0000269|PubMed:19207211}.
CC -!- SIMILARITY: Belongs to the VAMP-associated protein (VAP) (TC 9.B.17)
CC family. {ECO:0000305}.
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DR EMBL; CP002685; AEC10514.1; -; Genomic_DNA.
DR EMBL; AY093014; AAM13013.1; -; mRNA.
DR EMBL; BT006283; AAP13391.1; -; mRNA.
DR EMBL; AY088399; AAM65937.1; -; mRNA.
DR PIR; H84886; H84886.
DR RefSeq; NP_182039.1; NM_130077.3.
DR AlphaFoldDB; Q9SHC8; -.
DR SMR; Q9SHC8; -.
DR BioGRID; 4458; 4.
DR IntAct; Q9SHC8; 1.
DR STRING; 3702.AT2G45140.1; -.
DR iPTMnet; Q9SHC8; -.
DR PaxDb; Q9SHC8; -.
DR PRIDE; Q9SHC8; -.
DR ProteomicsDB; 243258; -.
DR EnsemblPlants; AT2G45140.1; AT2G45140.1; AT2G45140.
DR GeneID; 819122; -.
DR Gramene; AT2G45140.1; AT2G45140.1; AT2G45140.
DR KEGG; ath:AT2G45140; -.
DR Araport; AT2G45140; -.
DR TAIR; locus:2055557; AT2G45140.
DR eggNOG; KOG0439; Eukaryota.
DR HOGENOM; CLU_036554_1_2_1; -.
DR InParanoid; Q9SHC8; -.
DR OrthoDB; 1332028at2759; -.
DR PhylomeDB; Q9SHC8; -.
DR PRO; PR:Q9SHC8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SHC8; baseline and differential.
DR Genevisible; Q9SHC8; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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:0006605; P:protein targeting; IDA:UniProtKB.
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; Coiled coil; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..239
FT /note="Vesicle-associated protein 1-2"
FT /id="PRO_0000425784"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..239
FT /note="Vesicle-associated protein 1-2, N-terminally
FT processed"
FT /id="PRO_0000402170"
FT TOPO_DOM 1..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 5..125
FT /note="MSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00132"
FT REGION 123..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 169..215
FT /evidence="ECO:0000255"
FT COMPBIAS 142..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 1-2,
FT N-terminally processed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
SQ SEQUENCE 239 AA; 26442 MW; B5F876B24D738243 CRC64;
MSNELLTIDP VDLQFPFELK KQISCSLYLG NKTDNYVAFK VKTTNPKKYC VRPNTGVVHP
RSSSEVLVTM QAQKEAPADL QCKDKFLLQC VVASPGATPK DVTHEMFSKE AGHRVEETKL
RVVYVAPPRP PSPVREGSEE GSSPRASVSD NGNASDFTAA PRFSADRVDA QDNSSEARAL
VTKLTEEKNS AVQLNNRLQQ ELDQLRRESK RSKSGGIPFM YVLLVGLIGL ILGYIMKRT
