VAP21_ARATH
ID VAP21_ARATH Reviewed; 220 AA.
AC Q9LVU1;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Vesicle-associated protein 2-1;
DE AltName: Full=Plant VAP homolog 21;
DE Short=AtPVA21;
DE AltName: Full=VAMP-associated protein 2-1;
DE Contains:
DE RecName: Full=Vesicle-associated protein 2-1, N-terminally processed;
GN Name=PVA21; OrderedLocusNames=At5g47180; ORFNames=MQL5.3;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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=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 ACETYLATION [LARGE SCALE ANALYSIS] AT THR-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: May play a role in vesicle trafficking. {ECO:0000250}.
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}.
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DR EMBL; AB018117; BAA97151.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95480.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95481.1; -; Genomic_DNA.
DR EMBL; AY035160; AAK59664.1; -; mRNA.
DR EMBL; AY063031; AAL34205.1; -; mRNA.
DR EMBL; AY085274; AAM62506.1; -; mRNA.
DR RefSeq; NP_199529.1; NM_124089.5.
DR RefSeq; NP_851144.1; NM_180813.4.
DR AlphaFoldDB; Q9LVU1; -.
DR SMR; Q9LVU1; -.
DR BioGRID; 20012; 76.
DR IntAct; Q9LVU1; 76.
DR STRING; 3702.AT5G47180.2; -.
DR iPTMnet; Q9LVU1; -.
DR PaxDb; Q9LVU1; -.
DR PRIDE; Q9LVU1; -.
DR ProteomicsDB; 242311; -.
DR EnsemblPlants; AT5G47180.1; AT5G47180.1; AT5G47180.
DR EnsemblPlants; AT5G47180.2; AT5G47180.2; AT5G47180.
DR GeneID; 834764; -.
DR Gramene; AT5G47180.1; AT5G47180.1; AT5G47180.
DR Gramene; AT5G47180.2; AT5G47180.2; AT5G47180.
DR KEGG; ath:AT5G47180; -.
DR Araport; AT5G47180; -.
DR TAIR; locus:2171594; AT5G47180.
DR eggNOG; KOG0439; Eukaryota.
DR HOGENOM; CLU_036554_1_2_1; -.
DR InParanoid; Q9LVU1; -.
DR OMA; NTGVIHP; -.
DR OrthoDB; 1332028at2759; -.
DR PhylomeDB; Q9LVU1; -.
DR PRO; PR:Q9LVU1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LVU1; baseline and differential.
DR Genevisible; Q9LVU1; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
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; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; 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 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;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..220
FT /note="Vesicle-associated protein 2-1"
FT /id="PRO_0000425786"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..220
FT /note="Vesicle-associated protein 2-1, N-terminally
FT processed"
FT /id="PRO_0000402173"
FT TOPO_DOM 1..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 9..129
FT /note="MSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00132"
FT REGION 133..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..188
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-acetylthreonine; in Vesicle-associated protein 2-
FT 1, N-terminally processed"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 220 AA; 24667 MW; AC6B7876969CED65 CRC64;
MTGVGENQLI SIQPDELKFL FELEKQSYCD LKVANKTENY VAFKVKTTSP KKYFVRPNTG
VIQPWDSCII RVTLQAQREY PPDMQCKDKF LLQSTIVPPH TDVDELPQDT FTKDSGKTLT
ECKLKVSYIT PSTTQRSSES GATNGDGQSS ETISTIQRLK EERDAAVKQT QQLQHELETV
RRRRNQRNSG NGLSLKLAAM VGLIGLIIGF ILKLTLASPT
