SNP47_MOUSE
ID SNP47_MOUSE Reviewed; 413 AA.
AC Q8R570; Q3UNK4; Q8BK87;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Synaptosomal-associated protein 47;
DE Short=SNAP-47;
DE AltName: Full=Synaptosomal-associated 47 kDa protein;
GN Name=Snap47;
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 [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16621800; DOI=10.1074/jbc.m513838200;
RA Holt M., Varoqueaux F., Wiederhold K., Takamori S., Urlaub H.,
RA Fasshauer D., Jahn R.;
RT "Identification of SNAP-47, a novel Qbc-SNARE with ubiquitous expression.";
RL J. Biol. Chem. 281:17076-17083(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C3H/HeJ, and C57BL/6J;
RC TISSUE=Brain, Cerebellum, Embryo, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, and Spleen;
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: May play a role in intracellular membrane fusion.
CC {ECO:0000269|PubMed:16621800}.
CC -!- SUBUNIT: Associates with the BLOC-1 complex. Interacts with BLOC1S6 (By
CC similarity). Forms a complex containing SNAP47, VAMP2 and STX1A.
CC {ECO:0000250, ECO:0000269|PubMed:16621800}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000269|PubMed:16621800}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:16621800}. Note=Appears to be exclusively membrane-
CC bound. In primary neurons, widely distributed in both cell bodies and
CC neuronal processes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R570-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R570-2; Sequence=VSP_028615, VSP_028616;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with the most abundant
CC expression in the brain. In brain, most highly expressed in the
CC glomerular layer of the olfactory bulb, the cortex, striatum,
CC hippocampus, and colliculi (at protein level).
CC {ECO:0000269|PubMed:16621800}.
CC -!- DEVELOPMENTAL STAGE: Expressed as early as 10 dpc in developing brain
CC and reaches maximal levels at 18 dpc. {ECO:0000269|PubMed:16621800}.
CC -!- SIMILARITY: Belongs to the SVAP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC35874.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK028053; BAC25723.1; -; mRNA.
DR EMBL; AK049330; BAC33686.1; -; mRNA.
DR EMBL; AK075640; BAC35874.1; ALT_FRAME; mRNA.
DR EMBL; AK144165; BAE25743.1; -; mRNA.
DR EMBL; AL713994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023182; AAH23182.1; -; mRNA.
DR EMBL; BC029025; AAH29025.1; -; mRNA.
DR CCDS; CCDS24767.1; -. [Q8R570-1]
DR RefSeq; NP_653104.1; NM_144521.2. [Q8R570-1]
DR RefSeq; XP_006534084.1; XM_006534021.2.
DR RefSeq; XP_006534085.1; XM_006534022.3. [Q8R570-1]
DR RefSeq; XP_006534086.1; XM_006534023.1. [Q8R570-1]
DR RefSeq; XP_006534087.1; XM_006534024.3. [Q8R570-1]
DR AlphaFoldDB; Q8R570; -.
DR SMR; Q8R570; -.
DR BioGRID; 212462; 7.
DR IntAct; Q8R570; 1.
DR STRING; 10090.ENSMUSP00000010038; -.
DR iPTMnet; Q8R570; -.
DR PhosphoSitePlus; Q8R570; -.
DR SwissPalm; Q8R570; -.
DR EPD; Q8R570; -.
DR MaxQB; Q8R570; -.
DR PaxDb; Q8R570; -.
DR PeptideAtlas; Q8R570; -.
DR PRIDE; Q8R570; -.
DR ProteomicsDB; 261389; -. [Q8R570-1]
DR ProteomicsDB; 261390; -. [Q8R570-2]
DR Antibodypedia; 34657; 45 antibodies from 17 providers.
DR DNASU; 67826; -.
DR Ensembl; ENSMUST00000010038; ENSMUSP00000010038; ENSMUSG00000009894. [Q8R570-1]
DR GeneID; 67826; -.
DR KEGG; mmu:67826; -.
DR UCSC; uc007jds.1; mouse. [Q8R570-1]
DR CTD; 116841; -.
DR MGI; MGI:1915076; Snap47.
DR VEuPathDB; HostDB:ENSMUSG00000009894; -.
DR eggNOG; KOG3065; Eukaryota.
DR GeneTree; ENSGT00950000182843; -.
DR InParanoid; Q8R570; -.
DR OMA; FDNMMQG; -.
DR OrthoDB; 662135at2759; -.
DR PhylomeDB; Q8R570; -.
DR TreeFam; TF331066; -.
DR BioGRID-ORCS; 67826; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Snap47; mouse.
DR PRO; PR:Q8R570; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8R570; protein.
DR Bgee; ENSMUSG00000009894; Expressed in facial nucleus and 257 other tissues.
DR ExpressionAtlas; Q8R570; baseline and differential.
DR Genevisible; Q8R570; MM.
DR GO; GO:0032279; C:asymmetric synapse; ISO:MGI.
DR GO; GO:0031083; C:BLOC-1 complex; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IDA:SynGO.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; IDA:SynGO.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000727; T_SNARE_dom.
DR PROSITE; PS50192; T_SNARE; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Membrane; Reference proteome;
KW Repeat.
FT CHAIN 1..413
FT /note="Synaptosomal-associated protein 47"
FT /id="PRO_0000307152"
FT DOMAIN 109..171
FT /note="t-SNARE coiled-coil homology 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT DOMAIN 350..412
FT /note="t-SNARE coiled-coil homology 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 321..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 326..333
FT /note="RPKGCTPH -> CHLFLIIS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028615"
FT VAR_SEQ 334..413
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028616"
FT CONFLICT 355
FT /note="F -> S (in Ref. 2; BAC35874)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 46524 MW; A923C061BE7E569D CRC64;
MSSDMRVHSW SCSYYLDLEK QWVSGKLTLT PHSLKFIVEK TEEVLVGLPL SSIIEIRKES
SLFIFGAITV LEKGQTKHWF SSLQPSRNVV FNVIEHFWRE LLLSQPGTAA NIPSHVTRGQ
ELIGLMANSQ KRMEDTAKDL QQQSEQLDSV LKGLEKMESD LDVADRLLTE LETPSWWPFG
SKFWKMPAEE NLKEGVSSTC EPFGKEGVVI TVPAIISERA ESHSKLGKLT VLVSALEIYD
SCSLLLHRFE KEDVDDIKVH SPYEVSIRQR FIGKPDVAYQ LISAKMPEVI PILEVQFSSK
IELLEDALVL RNKVFASSAE RHAASRPKGC TPHRELPTGG QEGEQLQLQK NLPLFSEGEA
QELTQILSKM KGLALDTEAE LERQDAALDG ITVAVDRATL NVDKQNRRMR KLM
