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SNAG_MOUSE
ID   SNAG_MOUSE              Reviewed;         312 AA.
AC   Q9CWZ7; Q3TPT4;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Gamma-soluble NSF attachment protein {ECO:0000250|UniProtKB:Q99747};
DE            Short=SNAP-gamma {ECO:0000250|UniProtKB:Q99747};
DE   AltName: Full=N-ethylmaleimide-sensitive factor attachment protein gamma {ECO:0000312|MGI:MGI:104561};
GN   Name=Napg {ECO:0000312|MGI:MGI:104561};
GN   Synonyms=Snapg {ECO:0000303|PubMed:9705316};
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryonic stem cell;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=8455721; DOI=10.1038/362353a0;
RA   Whiteheart S.W., Griff I.C., Brunner M., Clary D.O., Mayer T., Buhrow S.A.,
RA   Rothman J.E.;
RT   "SNAP family of NSF attachment proteins includes a brain-specific
RT   isoform.";
RL   Nature 362:353-355(1993).
RN   [4]
RP   INTERACTION WITH VTI1A, AND SUBCELLULAR LOCATION.
RX   PubMed=9705316; DOI=10.1074/jbc.273.34.21783;
RA   Xu Y., Wong S.H., Tang B.L., Subramaniam V.N., Zhang T., Hong W.;
RT   "A 29-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment
RT   protein receptor (Vti1-rp2) implicated in protein trafficking in the
RT   secretory pathway.";
RL   J. Biol. Chem. 273:21783-21789(1998).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; THR-287 AND SER-308, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Required for vesicular transport between the endoplasmic
CC       reticulum and the Golgi apparatus. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RAB11FIP5 (By similarity). Interacts with VTI1A
CC       (PubMed:9705316). {ECO:0000250|UniProtKB:Q99747,
CC       ECO:0000269|PubMed:9705316}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P81127};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P81127}. Golgi
CC       apparatus {ECO:0000269|PubMed:9705316}.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in the heart, liver and
CC       kidneys with lower expression in the brain, spleen, lung, muscle and
CC       testes. {ECO:0000269|PubMed:8455721}.
CC   -!- SIMILARITY: Belongs to the SNAP family. {ECO:0000305}.
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DR   EMBL; AK010275; BAB26812.1; -; mRNA.
DR   EMBL; AK154573; BAE32685.1; -; mRNA.
DR   EMBL; AK164149; BAE37651.1; -; mRNA.
DR   EMBL; AK167372; BAE39468.1; -; mRNA.
DR   EMBL; BC026977; AAH26977.1; -; mRNA.
DR   CCDS; CCDS29295.1; -.
DR   RefSeq; NP_082293.1; NM_028017.1.
DR   AlphaFoldDB; Q9CWZ7; -.
DR   SMR; Q9CWZ7; -.
DR   BioGRID; 223846; 4.
DR   IntAct; Q9CWZ7; 1.
DR   MINT; Q9CWZ7; -.
DR   STRING; 10090.ENSMUSP00000025474; -.
DR   iPTMnet; Q9CWZ7; -.
DR   PhosphoSitePlus; Q9CWZ7; -.
DR   SwissPalm; Q9CWZ7; -.
DR   EPD; Q9CWZ7; -.
DR   jPOST; Q9CWZ7; -.
DR   MaxQB; Q9CWZ7; -.
DR   PaxDb; Q9CWZ7; -.
DR   PeptideAtlas; Q9CWZ7; -.
DR   PRIDE; Q9CWZ7; -.
DR   ProteomicsDB; 261590; -.
DR   Antibodypedia; 2189; 186 antibodies from 28 providers.
DR   Ensembl; ENSMUST00000025474; ENSMUSP00000025474; ENSMUSG00000024581.
DR   GeneID; 108123; -.
DR   KEGG; mmu:108123; -.
DR   UCSC; uc008fdp.2; mouse.
DR   CTD; 8774; -.
DR   MGI; MGI:104561; Napg.
DR   VEuPathDB; HostDB:ENSMUSG00000024581; -.
DR   eggNOG; KOG1585; Eukaryota.
DR   GeneTree; ENSGT00390000005826; -.
DR   HOGENOM; CLU_063974_1_0_1; -.
DR   InParanoid; Q9CWZ7; -.
DR   OMA; MHKENGN; -.
DR   OrthoDB; 1540214at2759; -.
DR   PhylomeDB; Q9CWZ7; -.
DR   TreeFam; TF312872; -.
DR   Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR   Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR   Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   BioGRID-ORCS; 108123; 2 hits in 72 CRISPR screens.
DR   ChiTaRS; Napg; mouse.
DR   PRO; PR:Q9CWZ7; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q9CWZ7; protein.
DR   Bgee; ENSMUSG00000024581; Expressed in retrosplenial region and 251 other tissues.
DR   ExpressionAtlas; Q9CWZ7; baseline and differential.
DR   Genevisible; Q9CWZ7; MM.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; ISO:MGI.
DR   GO; GO:0005483; F:soluble NSF attachment protein activity; IBA:GO_Central.
DR   GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   CDD; cd15832; SNAP; 1.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR000744; NSF_attach.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR13768; PTHR13768; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
PE   1: Evidence at protein level;
KW   ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..312
FT                   /note="Gamma-soluble NSF attachment protein"
FT                   /id="PRO_0000219064"
FT   REGION          281..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         287
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         308
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   312 AA;  34732 MW;  12F47490EAFC57F3 CRC64;
     MAAQKINEGL EHLAKAEKYL KTGFLKWKPD YDSAASEYGK AAVAFKNAKQ FEQAKDACLR
     EAVAHENNRA LFHAAKAYEQ AGMMLKEMQK LPEAVQLIEK ASMMYLENGT PDTAAMALER
     AGKLIENVDP EKAVQLYQQT ANVFENEERL RQAVELLGKA SRLLVRGRRF DEAALSIQKE
     KNIYKEIENY PTCYKKTIAQ VLVHLHRNDY VAAERCVRES YSIPGFNGSE DCAALEQLLE
     GYDQQDQDQV SEVCNSPLFK YMDNDYAKLG LSLVVPGGGI KKKSPATPQA KPDGAAGMAA
     EEEEDEYSGG LC
 
 
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