VA713_ARATH
ID VA713_ARATH Reviewed; 221 AA.
AC Q9LFP1;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Vesicle-associated membrane protein 713 {ECO:0000303|PubMed:11115874};
DE Short=AtVAMP713 {ECO:0000303|PubMed:11115874};
GN Name=VAMP713 {ECO:0000303|PubMed:11115874};
GN OrderedLocusNames=At5g11150 {ECO:0000312|Araport:AT5G11150};
GN ORFNames=F2I11.40 {ECO:0000312|EMBL:CAB96650.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11115874; DOI=10.1104/pp.124.4.1558;
RA Sanderfoot A.A., Assaad F.F., Raikhel N.V.;
RT "The Arabidopsis genome. An abundance of soluble N-ethylmaleimide-sensitive
RT factor adaptor protein receptors.";
RL Plant Physiol. 124:1558-1569(2000).
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15342965; DOI=10.1247/csf.29.49;
RA Uemura T., Ueda T., Ohniwa R.L., Nakano A., Takeyasu K., Sato M.H.;
RT "Systematic analysis of SNARE molecules in Arabidopsis: dissection of the
RT post-Golgi network in plant cells.";
RL Cell Struct. Funct. 29:49-65(2004).
RN [6]
RP DOMAIN.
RX PubMed=15876431; DOI=10.1016/j.febslet.2005.04.022;
RA Uemura T., Sato M.H., Takeyasu K.;
RT "The longin domain regulates subcellular targeting of VAMP7 in Arabidopsis
RT thaliana.";
RL FEBS Lett. 579:2842-2846(2005).
RN [7]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=29463724; DOI=10.1073/pnas.1717839115;
RA Takemoto K., Ebine K., Askani J.C., Krueger F., Gonzalez Z.A., Ito E.,
RA Goh T., Schumacher K., Nakano A., Ueda T.;
RT "Distinct sets of tethering complexes, SNARE complexes, and Rab GTPases
RT mediate membrane fusion at the vacuole in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E2457-E2466(2018).
CC -!- FUNCTION: Involved in the targeting and/or fusion of transport vesicles
CC to their target membrane. {ECO:0000305|PubMed:11115874}.
CC -!- SUBUNIT: Interacts with subunits of the vacuole protein sorting (HOPS)
CC complex including VPS11, VCL1, VPS18, VPS33, VPS39 and VPS41.
CC {ECO:0000269|PubMed:29463724}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:15342965};
CC Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q12255}.
CC Prevacuolar compartment membrane {ECO:0000269|PubMed:15342965}; Single-
CC pass type IV membrane protein {ECO:0000250|UniProtKB:Q12255}.
CC Note=Strong colocalization with VAMP713 at the contact sites of two
CC vacuoles. {ECO:0000269|PubMed:29463724}.
CC -!- TISSUE SPECIFICITY: Highly expressed in stems and roots. Detected in
CC flowers and leaves. {ECO:0000269|PubMed:15342965}.
CC -!- DOMAIN: The longin domain is critical for the vacuolar localization.
CC {ECO:0000269|PubMed:15876431}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL360314; CAB96650.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91639.1; -; Genomic_DNA.
DR EMBL; AY091002; AAM14024.1; -; mRNA.
DR EMBL; AY122934; AAM67467.1; -; mRNA.
DR RefSeq; NP_196676.1; NM_121153.5.
DR AlphaFoldDB; Q9LFP1; -.
DR SMR; Q9LFP1; -.
DR BioGRID; 16262; 1.
DR IntAct; Q9LFP1; 1.
DR STRING; 3702.AT5G11150.1; -.
DR PaxDb; Q9LFP1; -.
DR PRIDE; Q9LFP1; -.
DR ProteomicsDB; 242305; -.
DR EnsemblPlants; AT5G11150.1; AT5G11150.1; AT5G11150.
DR GeneID; 830984; -.
DR Gramene; AT5G11150.1; AT5G11150.1; AT5G11150.
DR KEGG; ath:AT5G11150; -.
DR Araport; AT5G11150; -.
DR TAIR; locus:2147952; AT5G11150.
DR eggNOG; KOG0859; Eukaryota.
DR HOGENOM; CLU_064620_1_2_1; -.
DR InParanoid; Q9LFP1; -.
DR OMA; TNIMERG; -.
DR PhylomeDB; Q9LFP1; -.
DR PRO; PR:Q9LFP1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFP1; baseline and differential.
DR Genevisible; Q9LFP1; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0030897; C:HOPS complex; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; TAS:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd14824; Longin; 1.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR010908; Longin_dom.
DR InterPro; IPR001388; Synaptobrevin.
DR InterPro; IPR042855; V_SNARE_CC.
DR Pfam; PF13774; Longin; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
DR SMART; SM01270; Longin; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS50859; LONGIN; 1.
DR PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O49377"
FT CHAIN 2..221
FT /note="Vesicle-associated membrane protein 713"
FT /id="PRO_0000206752"
FT TOPO_DOM 2..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..221
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 7..112
FT /note="Longin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00231"
FT DOMAIN 127..187
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O49377"
SQ SEQUENCE 221 AA; 25320 MW; 09E54407A67A5A3D CRC64;
MAIIFALVAR GTVVLSEFSA TSTNASSISK QILEKLPGND SDSHMSYSQD RYIFHVKRTD
GLTVLCMADE TAGRNIPFAF LDDIHQRFVK TYGRAIHSAQ AYSMNDEFSR VLSQQMEFYS
NDPNADRMSR IKGEMSQVRN VMIENIDKVL DRGERLELLV DKTENMQGNT FRFRKQARRY
RTIMWWRNVK LTIALILVLA LVVYIAMAFV CHGPSLPSCF K
