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BET1L_MOUSE
ID   BET1L_MOUSE             Reviewed;         111 AA.
AC   O35153; Q9D0E4;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=BET1-like protein;
DE   AltName: Full=Golgi SNARE with a size of 15 kDa;
DE            Short=GOS-15;
DE            Short=GS15;
DE   AltName: Full=Vesicle transport protein GOS15;
GN   Name=Bet1l {ECO:0000312|MGI:MGI:1913128};
GN   Synonyms=Gs15 {ECO:0000312|MGI:MGI:1913128};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAB66321.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J {ECO:0000269|PubMed:9242691};
RC   TISSUE=Embryo {ECO:0000269|PubMed:9242691};
RX   PubMed=9242691; DOI=10.1074/jbc.272.32.20162;
RA   Xu Y., Wong S.H., Zhang T., Subramaniam V.N., Hong W.;
RT   "GS15, a 15-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor
RT   attachment protein receptor (SNARE) homologous to rbet1.";
RL   J. Biol. Chem. 272:20162-20166(1997).
RN   [2] {ECO:0000312|EMBL:BAB27666.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB27666.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:BAB27666.1}, and
RC   Head {ECO:0000312|EMBL:BAE36260.1};
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Vesicle SNARE required for targeting and fusion of retrograde
CC       transport vesicles with the Golgi complex. Required for the integrity
CC       of the Golgi complex (By similarity). {ECO:0000250|UniProtKB:O35152}.
CC   -!- SUBUNIT: Component of a SNARE complex consisting of STX5, YKT6, GOSR2
CC       and BET1L. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type IV membrane protein {ECO:0000250}. Golgi apparatus, trans-
CC       Golgi network membrane {ECO:0000250}. Note=Present throughout the Golgi
CC       apparatus, with increasing concentration from cis-Golgi to the trans-
CC       Golgi face of the stacks. {ECO:0000250}.
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DR   EMBL; AF003999; AAB66321.1; -; mRNA.
DR   EMBL; AK011508; BAB27666.1; -; mRNA.
DR   EMBL; AK161239; BAE36260.1; -; mRNA.
DR   CCDS; CCDS21987.1; -.
DR   RefSeq; NP_061212.3; NM_018742.5.
DR   AlphaFoldDB; O35153; -.
DR   SMR; O35153; -.
DR   STRING; 10090.ENSMUSP00000026557; -.
DR   iPTMnet; O35153; -.
DR   PhosphoSitePlus; O35153; -.
DR   SwissPalm; O35153; -.
DR   jPOST; O35153; -.
DR   MaxQB; O35153; -.
DR   PaxDb; O35153; -.
DR   PeptideAtlas; O35153; -.
DR   PRIDE; O35153; -.
DR   DNASU; 54399; -.
DR   Ensembl; ENSMUST00000026557; ENSMUSP00000026557; ENSMUSG00000025484.
DR   GeneID; 54399; -.
DR   KEGG; mmu:54399; -.
DR   UCSC; uc009kii.2; mouse.
DR   CTD; 51272; -.
DR   MGI; MGI:1913128; Bet1l.
DR   VEuPathDB; HostDB:ENSMUSG00000025484; -.
DR   eggNOG; KOG3385; Eukaryota.
DR   GeneTree; ENSGT00960000190623; -.
DR   HOGENOM; CLU_086133_2_2_1; -.
DR   InParanoid; O35153; -.
DR   OMA; HEEVEIH; -.
DR   OrthoDB; 1536545at2759; -.
DR   PhylomeDB; O35153; -.
DR   TreeFam; TF323307; -.
DR   Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR   BioGRID-ORCS; 54399; 1 hit in 73 CRISPR screens.
DR   ChiTaRS; Bet1l; mouse.
DR   PRO; PR:O35153; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; O35153; protein.
DR   Bgee; ENSMUSG00000025484; Expressed in dentate gyrus of hippocampal formation granule cell and 253 other tissues.
DR   ExpressionAtlas; O35153; baseline and differential.
DR   Genevisible; O35153; MM.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005768; C:endosome; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR   GO; GO:0005795; C:Golgi stack; IDA:MGI.
DR   GO; GO:0000138; C:Golgi trans cisterna; IBA:GO_Central.
DR   GO; GO:0005798; C:Golgi-associated vesicle; ISO:MGI.
DR   GO; GO:0030173; C:integral component of Golgi membrane; ISO:MGI.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR   GO; GO:0005484; F:SNAP receptor activity; IDA:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:2000156; P:regulation of retrograde vesicle-mediated transport, Golgi to ER; ISO:MGI.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR   CDD; cd15853; SNARE_Bet1; 1.
DR   InterPro; IPR039897; BET1.
DR   InterPro; IPR039899; BET1_SNARE.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR12791; PTHR12791; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..111
FT                   /note="BET1-like protein"
FT                   /id="PRO_0000233057"
FT   TOPO_DOM        1..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        108..111
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          15..77
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYM9"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYM9"
FT   CONFLICT        108
FT                   /note="R -> S (in Ref. 2; BAB27666)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   111 AA;  12428 MW;  854B3523B71BE5BE CRC64;
     MADWTRAQSS GAVEDILDRE NKRMADSLAS KVTRLKSLAL DIDRDTEDQN RYLDGMDSDF
     TSVTGLLTGS VKRFSTMARS GRDNRKLLCG MAVVLIVAFF ILSYLLSRTR T
 
 
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