GenomeNet

Database: UniProt
Entry: F1LNT8_RAT
LinkDB: F1LNT8_RAT
Original site: F1LNT8_RAT 
ID   F1LNT8_RAT              Unreviewed;       116 AA.
AC   F1LNT8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=Vesicle-associated membrane protein 8 {ECO:0000256|ARBA:ARBA00039271};
DE   AltName: Full=Endobrevin {ECO:0000256|ARBA:ARBA00042205};
GN   Name=Vamp8 {ECO:0000313|Ensembl:ENSRNOP00000017301.3,
GN   ECO:0000313|RGD:620421};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000017301.3, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000017301.3, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000017301.3,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000017301.3}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000017301.3};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004521};
CC       Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004521}.
CC       Early endosome membrane {ECO:0000256|ARBA:ARBA00037832}; Single-pass
CC       type IV membrane protein {ECO:0000256|ARBA:ARBA00037832}. Endosome
CC       membrane {ECO:0000256|ARBA:ARBA00037867}; Single-pass type IV membrane
CC       protein {ECO:0000256|ARBA:ARBA00037867}. Late endosome membrane
CC       {ECO:0000256|ARBA:ARBA00037845}; Single-pass type IV membrane protein
CC       {ECO:0000256|ARBA:ARBA00037845}. Lysosome membrane
CC       {ECO:0000256|ARBA:ARBA00037863}; Single-pass type IV membrane protein
CC       {ECO:0000256|ARBA:ARBA00037863}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein
CC       {ECO:0000256|ARBA:ARBA00004211}. Zymogen granule membrane
CC       {ECO:0000256|ARBA:ARBA00037825}; Single-pass type IV membrane protein
CC       {ECO:0000256|ARBA:ARBA00037825}.
CC   -!- SIMILARITY: Belongs to the synaptobrevin family.
CC       {ECO:0000256|ARBA:ARBA00008025}.
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DR   AlphaFoldDB; F1LNT8; -.
DR   IntAct; F1LNT8; 1.
DR   Ensembl; ENSRNOT00000017301.5; ENSRNOP00000017301.3; ENSRNOG00000012748.5.
DR   RGD; 620421; Vamp8.
DR   VEuPathDB; HostDB:ENSRNOG00000012748; -.
DR   GeneTree; ENSGT00940000160325; -.
DR   HOGENOM; CLU_064620_5_0_1; -.
DR   OMA; VRKKMWW; -.
DR   TreeFam; TF320419; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000012748; Expressed in lung and 20 other cell types or tissues.
DR   GO; GO:0035577; C:azurophil granule membrane; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0031902; C:late endosome membrane; IEA:Ensembl.
DR   GO; GO:0098594; C:mucin granule; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
DR   GO; GO:0031201; C:SNARE complex; IEA:Ensembl.
DR   GO; GO:0019869; F:chloride channel inhibitor activity; IEA:Ensembl.
DR   GO; GO:0016240; P:autophagosome membrane docking; IEA:Ensembl.
DR   GO; GO:0070254; P:mucus secretion; IEA:Ensembl.
DR   GO; GO:1903531; P:negative regulation of secretion by cell; IEA:Ensembl.
DR   GO; GO:1903595; P:positive regulation of histamine secretion by mast cell; IEA:Ensembl.
DR   GO; GO:1903076; P:regulation of protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:Ensembl.
DR   CDD; cd15868; R-SNARE_VAMP8; 1.
DR   Gene3D; 1.20.5.110; -; 1.
DR   InterPro; IPR001388; Synaptobrevin-like.
DR   InterPro; IPR016444; Synaptobrevin/VAMP.
DR   InterPro; IPR042855; V_SNARE_CC.
DR   PANTHER; PTHR45701; SYNAPTOBREVIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR45701:SF7; VESICLE-ASSOCIATED MEMBRANE PROTEIN 8; 1.
DR   Pfam; PF00957; Synaptobrevin; 1.
DR   PRINTS; PR00219; SYNAPTOBREVN.
DR   SUPFAM; SSF58038; SNARE fusion complex; 1.
DR   PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW   Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW   ProRule:PRU00290}; Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F1LNT8};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        92..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          27..87
FT                   /note="V-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50892"
SQ   SEQUENCE   116 AA;  13118 MW;  895D8F83C14EEBC7 CRC64;
     MGEHLGCLRR KSGFNLEEAS GSAGNDRVRN LQSEVEGVKN IMTQNVERIL ARGENLDHLR
     NKTEDLEATS EHFKTTSQKV ARKFWWKNVK MIVIICVIVL IILILIILFA TGTIPT
//
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