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VA727_ARATH
ID   VA727_ARATH             Reviewed;         240 AA.
AC   Q9M376; Q53XE0;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 133.
DE   RecName: Full=Vesicle-associated membrane protein 727;
DE            Short=AtVAMP727;
GN   Name=VAMP727; OrderedLocusNames=At3g54300; ORFNames=F24B22.260;
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=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   [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;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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   GENE FAMILY, NOMENCLATURE, AND 3D-STRUCTURE MODELING.
RX   PubMed=19889231; DOI=10.1186/1471-2164-10-510;
RA   Vedovato M., Rossi V., Dacks J.B., Filippini F.;
RT   "Comparative analysis of plant genomes allows the definition of the
RT   'Phytolongins': a novel non-SNARE longin domain protein family.";
RL   BMC Genomics 10:510-510(2009).
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:0000250}.
CC   -!- SUBUNIT: Interacts with subunits of the class C core vacuole/endosome
CC       tethering (CORVET) complex including VPS11, VCL1, VPS18, VPS33, VPS3
CC       and VPS8. {ECO:0000269|PubMed:29463724}.
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane
CC       {ECO:0000269|PubMed:15342965}; Single-pass type IV membrane protein
CC       {ECO:0000250|UniProtKB:Q12255}. Endosome membrane
CC       {ECO:0000269|PubMed:15342965}; Single-pass type IV membrane protein
CC       {ECO:0000250|UniProtKB:Q12255}. Note=Co-localizes with VPS3.
CC       {ECO:0000269|PubMed:29463724}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in flowers. Detected in leaves,
CC       stems and roots. {ECO:0000269|PubMed:15342965}.
CC   -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR   EMBL; AL132957; CAB71004.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79210.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79211.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM64005.1; -; Genomic_DNA.
DR   EMBL; BT011606; AAS47612.1; -; mRNA.
DR   EMBL; BT012242; AAS76729.1; -; mRNA.
DR   EMBL; AK229117; BAF00993.1; -; mRNA.
DR   PIR; T47589; T47589.
DR   RefSeq; NP_001078283.1; NM_001084814.2.
DR   RefSeq; NP_001326058.1; NM_001339657.1.
DR   RefSeq; NP_190998.1; NM_115290.5.
DR   AlphaFoldDB; Q9M376; -.
DR   SMR; Q9M376; -.
DR   BioGRID; 9914; 5.
DR   IntAct; Q9M376; 3.
DR   STRING; 3702.AT3G54300.1; -.
DR   iPTMnet; Q9M376; -.
DR   PaxDb; Q9M376; -.
DR   PRIDE; Q9M376; -.
DR   ProteomicsDB; 228545; -.
DR   EnsemblPlants; AT3G54300.1; AT3G54300.1; AT3G54300.
DR   EnsemblPlants; AT3G54300.2; AT3G54300.2; AT3G54300.
DR   EnsemblPlants; AT3G54300.3; AT3G54300.3; AT3G54300.
DR   GeneID; 824597; -.
DR   Gramene; AT3G54300.1; AT3G54300.1; AT3G54300.
DR   Gramene; AT3G54300.2; AT3G54300.2; AT3G54300.
DR   Gramene; AT3G54300.3; AT3G54300.3; AT3G54300.
DR   KEGG; ath:AT3G54300; -.
DR   Araport; AT3G54300; -.
DR   TAIR; locus:2080340; AT3G54300.
DR   eggNOG; KOG0859; Eukaryota.
DR   HOGENOM; CLU_064620_1_0_1; -.
DR   InParanoid; Q9M376; -.
DR   OMA; SKFFIHC; -.
DR   OrthoDB; 1211929at2759; -.
DR   PhylomeDB; Q9M376; -.
DR   PRO; PR:Q9M376; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M376; baseline and differential.
DR   Genevisible; Q9M376; AT.
DR   GO; GO:0033263; C:CORVET complex; IDA:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; IDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031201; C:SNARE complex; IPI:TAIR.
DR   GO; GO:0006623; P:protein targeting to vacuole; IMP:TAIR.
DR   GO; GO:0007033; P:vacuole organization; 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   Endosome; Membrane; Protein transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..240
FT                   /note="Vesicle-associated membrane protein 727"
FT                   /id="PRO_0000206760"
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   TOPO_DOM        237..240
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          6..133
FT                   /note="Longin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00231"
FT   DOMAIN          149..209
FT                   /note="v-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
SQ   SEQUENCE   240 AA;  27460 MW;  4805B9406E95D47B CRC64;
     MSQKGLIYSF VAKGTVVLAE HTPYSGNFST IAVQCLQKLP TNSSKYTYSC DGHTFNFLVD
     NGFVFLVVAD ESTGRSVPFV FLERVKEDFK KRYEASIKND ERHPLADEDE DDDLFGDRFS
     VAYNLDREFG PILKEHMQYC MSHPEEMSKL SKLKAQITEV KGIMMDNIEK VLDRGEKIEL
     LVDKTENLQF QADSFQRQGR QLRRKMWLQS LQMKLMVAGA VFSFILIVWV VACGGFKCSS
 
 
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