VAP22_ARATH
ID VAP22_ARATH Reviewed; 386 AA.
AC B9DHD7; Q6UQE9; Q8VXW8; Q9FRQ7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Vesicle-associated protein 2-2;
DE AltName: Full=Plant VAP homolog 22;
DE Short=AtPVA22;
DE AltName: Full=VAMP-associated protein 2-2;
DE AltName: Full=Vesicle-associated protein 27-2;
GN Name=PVA22; Synonyms=VAP27-2; OrderedLocusNames=At1g08820;
GN ORFNames=F22O13.31;
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=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 [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=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 236-386.
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 [MRNA] OF 266-386, AND INTERACTION WITH COWPEA MOSAIC
RP VIRUS NTB 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 [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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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: May play a role in vesicle trafficking. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with cowpea mosaic virus (CPMV) NTP-binding protein
CC (NTB). {ECO:0000269|PubMed:11907339}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type IV membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VAMP-associated protein (VAP) (TC 9.B.17)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF99771.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC003981; AAF99771.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28352.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28353.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59286.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59287.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59288.1; -; Genomic_DNA.
DR EMBL; AK317489; BAH20154.1; -; mRNA.
DR EMBL; AK317626; BAH20288.1; -; mRNA.
DR EMBL; AY074512; AAL67126.1; -; mRNA.
DR EMBL; AY364004; AAQ63967.1; -; mRNA.
DR PIR; B86220; B86220.
DR PIR; T00738; T00738.
DR RefSeq; NP_001031004.1; NM_001035927.2.
DR RefSeq; NP_001321655.1; NM_001331792.1.
DR RefSeq; NP_001321656.1; NM_001331793.1.
DR RefSeq; NP_001321657.1; NM_001331791.1.
DR RefSeq; NP_172359.2; NM_100756.2.
DR AlphaFoldDB; B9DHD7; -.
DR SMR; B9DHD7; -.
DR BioGRID; 22645; 7.
DR IntAct; B9DHD7; 4.
DR STRING; 3702.AT1G08820.1; -.
DR iPTMnet; B9DHD7; -.
DR PaxDb; B9DHD7; -.
DR PRIDE; B9DHD7; -.
DR ProteomicsDB; 242312; -.
DR EnsemblPlants; AT1G08820.1; AT1G08820.1; AT1G08820.
DR EnsemblPlants; AT1G08820.2; AT1G08820.2; AT1G08820.
DR EnsemblPlants; AT1G08820.3; AT1G08820.3; AT1G08820.
DR EnsemblPlants; AT1G08820.4; AT1G08820.4; AT1G08820.
DR EnsemblPlants; AT1G08820.5; AT1G08820.5; AT1G08820.
DR GeneID; 837404; -.
DR Gramene; AT1G08820.1; AT1G08820.1; AT1G08820.
DR Gramene; AT1G08820.2; AT1G08820.2; AT1G08820.
DR Gramene; AT1G08820.3; AT1G08820.3; AT1G08820.
DR Gramene; AT1G08820.4; AT1G08820.4; AT1G08820.
DR Gramene; AT1G08820.5; AT1G08820.5; AT1G08820.
DR KEGG; ath:AT1G08820; -.
DR Araport; AT1G08820; -.
DR TAIR; locus:2025585; AT1G08820.
DR eggNOG; KOG0439; Eukaryota.
DR HOGENOM; CLU_036554_0_0_1; -.
DR InParanoid; B9DHD7; -.
DR OMA; ISFQHRE; -.
DR OrthoDB; 1332028at2759; -.
DR PhylomeDB; B9DHD7; -.
DR PRO; PR:B9DHD7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; B9DHD7; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
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: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; 2.
DR Pfam; PF00635; Motile_Sperm; 1.
DR SUPFAM; SSF49354; SSF49354; 1.
DR PROSITE; PS50202; MSP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Endoplasmic reticulum; Host-virus interaction;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..386
FT /note="Vesicle-associated protein 2-2"
FT /id="PRO_0000402174"
FT TOPO_DOM 1..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
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 COILED 300..353
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SHC8"
SQ SEQUENCE 386 AA; 43270 MW; AC0307DD110E2739 CRC64;
MNMPLLDIQP RTLQFAVDLK KQTSCVVQLT NTTHHYVAFK VKTTSPKKYC VRPNVGVVAP
KSTCEFTVIM QAFKEPPPDM VCKDKFLIQS TAVSAETTDE DITASMFSKA EGKHIEENKL
RVTLVPPSDS PELSPINTPK QGAVFEDSIL KDRLYSQSET LAPPQYEGEI VKEPRMVGHD
ELKAADNAKE LKTPKMATVD FVEDRYTAND LKATKDSYDS SRMAKETGFD PIRSHKDADD
GRAIKATTNL DAPMKKAMDL PRDQGFTNGI AVDSEPKISK ERDVVQLQKT DGQNVRGLDE
LKLVKDIEEM KLKVDALESK LKQADSTISK LMEERSISSQ HRQSLQHELA ELRTKKIVKE
VHNGFPLLYV CVVAFIAYVI GHFLRT