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SNARE-associated protein Snapin (Biogenesis of lysosome-related organelles complex 1 subunit 7) (BLOC-1 subunit 7) (Synaptosomal-associated protein 25-binding protein) (SNAP-associated protein)

 SNAPN_MOUSE             Reviewed;         136 AA.
Q9Z266; Q3U8V4; Q922V7;
16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
27-SEP-2017, entry version 134.
RecName: Full=SNARE-associated protein Snapin;
AltName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 7;
Short=BLOC-1 subunit 7;
AltName: Full=Synaptosomal-associated protein 25-binding protein;
Short=SNAP-associated protein;
Name=Snapin; Synonyms=Bloc1s7, Snap25bp, Snapap;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH SNAP25.
TISSUE=Brain;
PubMed=10195194; DOI=10.1038/5673;
Ilardi J.M., Mochida S., Sheng Z.-H.;
"Snapin: a SNARE-associated protein implicated in synaptic
transmission.";
Nat. Neurosci. 2:119-124(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
TISSUE=Bone marrow, Forelimb, Head, Liver, Pancreas, and Retina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Limb, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION
WITH SNAP23 AND STX4A.
PubMed=12877659; DOI=10.1042/BJ20030427;
Buxton P., Zhang X.-M., Walsh B., Sriratana A., Schenberg I.,
Manickam E., Rowe T.;
"Identification and characterization of Snapin as a ubiquitously
expressed SNARE-binding protein that interacts with SNAP23 in non-
neuronal cells.";
Biochem. J. 375:433-440(2003).
[5]
PHOSPHORYLATION AT SER-50, INTERACTION WITH SNAP25, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF SER-42; SER-50 AND THR-63.
PubMed=11283605; DOI=10.1038/35070000;
Chheda M.G., Ashery U., Thakur P., Rettig J., Sheng Z.-H.;
"Phosphorylation of Snapin by PKA modulates its interaction with the
SNARE complex.";
Nat. Cell Biol. 3:331-338(2001).
[6]
REVIEW ON PHOSPHORYLATION.
PubMed=12887314; DOI=10.1042/BST0310824;
Evans G.J., Morgan A.;
"Regulation of the exocytotic machinery by cAMP-dependent protein
kinase: implications for presynaptic plasticity.";
Biochem. Soc. Trans. 31:824-827(2003).
[7]
PHOSPHORYLATION BY CSNK1D/CK1, SUBCELLULAR LOCATION, AND INTERACTION
WITH CSNK1D.
PubMed=17101137; DOI=10.1016/j.febslet.2006.10.068;
Wolff S., Stoeter M., Giamas G., Piesche M., Henne-Bruns D.,
Banting G., Knippschild U.;
"Casein kinase 1 delta (CK1delta) interacts with the SNARE associated
protein snapin.";
FEBS Lett. 580:6477-6484(2006).
[8]
FUNCTION.
PubMed=16760431; DOI=10.1091/mbc.E06-02-0103;
Salazar G., Craige B., Styers M.L., Newell-Litwa K.A., Doucette M.M.,
Wainer B.H., Falcon-Perez J.M., Dell'Angelica E.C., Peden A.A.,
Werner E., Faundez V.;
"BLOC-1 complex deficiency alters the targeting of adaptor protein
complex-3 cargoes.";
Mol. Biol. Cell 17:4014-4026(2006).
[9]
TISSUE SPECIFICITY.
PubMed=19168546; DOI=10.1093/molehr/gap004;
Ginter-Matuszewska B., Spik A., Rembiszewska A., Koyias C.,
Kupryjanczyk J., Jaruzelska J.;
"The SNARE-associated component SNAPIN binds PUMILIO2 and NANOS1
proteins in human male germ cells.";
Mol. Hum. Reprod. 15:173-179(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
FUNCTION.
PubMed=19546860; DOI=10.1038/mp.2009.58;
Ghiani C.A., Starcevic M., Rodriguez-Fernandez I.A., Nazarian R.,
Cheli V.T., Chan L.N., Malvar J.S., de Vellis J., Sabatti C.,
Dell'Angelica E.C.;
"The dysbindin-containing complex (BLOC-1) in brain: developmental
regulation, interaction with SNARE proteins and role in neurite
outgrowth.";
Mol. Psychiatry 15:204-215(2010).
[12]
FUNCTION, AND ASSOCIATION WITH THE AP-3 COMPLEX.
PubMed=21998198; DOI=10.1091/mbc.E11-07-0592;
Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A.,
Craige B., Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.;
"The schizophrenia susceptibility factor dysbindin and its associated
complex sort cargoes from cell bodies to the synapse.";
Mol. Biol. Cell 22:4854-4867(2011).
-!- FUNCTION: Component of the BLOC-1 complex, a complex that is
required for normal biogenesis of lysosome-related organelles
(LRO), such as platelet dense granules and melanosomes. In concert
with the AP-3 complex, the BLOC-1 complex is required to target
membrane protein cargos into vesicles assembled at cell bodies for
delivery into neurites and nerve terminals. The BLOC-1 complex, in
association with SNARE proteins, is also proposed to be involved
in neurite extension. Plays a role in intracellular vesicle
trafficking and synaptic vesicle recycling. May modulate a step
between vesicle priming, fusion and calcium-dependent
neurotransmitter release through its ability to potentiate the
interaction of synaptotagmin with the SNAREs and the plasma-
membrane-associated protein SNAP25. Its phosphorylation state
influences exocytotic protein interactions and may regulate
synaptic vesicle exocytosis. May also have a role in the
mechanisms of SNARE-mediated membrane fusion in non-neuronal cells
(PubMed:16760431, PubMed:19546860, PubMed:21998198). As part of
the BORC complex may play a role in lysosomes movement and
localization at the cell periphery. Associated with the cytosolic
face of lysosomes, the BORC complex may recruit ARL8B and couple
lysosomes to microtubule plus-end-directed kinesin motor (By
similarity). {ECO:0000250|UniProtKB:O95295,
ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:19546860,
ECO:0000269|PubMed:21998198}.
-!- SUBUNIT: Component of the biogenesis of lysosome-related
organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2,
BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and
SNAPIN/BLOC1S8. Octamer composed of one copy each BLOC1S1,
BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and
SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3
protein complex and membrane protein cargos (PubMed:21998198).
Component of the BLOC-one-related complex (BORC) which is composed
of BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and
SNAPIN (By similarity). Associates with the SNARE complex.
Interacts with CSNK1D, SNAP23 and STX4A but not with STX1A, VAMP2
and SYT1 (PubMed:12877659, PubMed:17101137). Interacts with
SNAP25; the interaction with SNAP25 is increased by its
phosphorylation (PubMed:10195194, PubMed:11283605). Interacts with
CNTRL, NANOS1, PUM2 and RGS7. Interacts with TOR1A; the
interaction is direct and associates SNAPIN with the CSN complex
(By similarity). {ECO:0000250|UniProtKB:O95295,
ECO:0000269|PubMed:10195194, ECO:0000269|PubMed:11283605,
ECO:0000269|PubMed:12877659, ECO:0000269|PubMed:17101137,
ECO:0000269|PubMed:21998198}.
-!- INTERACTION:
Q06486-2:Csnk1d (xeno); NbExp=4; IntAct=EBI-6170320, EBI-7088890;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12877659};
Peripheral membrane protein {ECO:0000269|PubMed:12877659};
Cytoplasmic side {ECO:0000269|PubMed:12877659}. Cytoplasm, cytosol
{ECO:0000269|PubMed:12877659}. Cytoplasm, perinuclear region
{ECO:0000269|PubMed:12877659}. Golgi apparatus membrane
{ECO:0000269|PubMed:17101137}. Lysosome membrane
{ECO:0000250|UniProtKB:P60192}. Cytoplasmic vesicle, secretory
vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:11283605}.
Note=Colocalizes with NANOS1 and PUM2 in the perinuclear region of
germ cells. {ECO:0000250|UniProtKB:O95295}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Z266-1; Sequence=Displayed;
Name=2;
IsoId=Q9Z266-2; Sequence=VSP_009165, VSP_009166;
-!- TISSUE SPECIFICITY: Strongly expressed in heart, brain, testis,
kidney and liver; low expression in spleen, lung and skeletal
muscle. In the testis, expressed in the seminiferous tubules.
{ECO:0000269|PubMed:12877659, ECO:0000269|PubMed:19168546}.
-!- PTM: Phosphorylated by PKD, phosphorylation controls SNAPIN
protein stability (By similarity). Phosphorylated by CSNK1D/CK1.
{ECO:0000250, ECO:0000269|PubMed:11283605,
ECO:0000269|PubMed:17101137}.
-!- SIMILARITY: Belongs to the SNAPIN family. {ECO:0000305}.
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EMBL; AF086838; AAD11418.1; -; mRNA.
EMBL; AK007458; BAB25049.1; -; mRNA.
EMBL; AK048007; BAC33212.1; -; mRNA.
EMBL; AK050151; BAC34095.1; -; mRNA.
EMBL; AK077840; BAC37029.1; -; mRNA.
EMBL; AK080718; BAC37991.1; -; mRNA.
EMBL; AK152057; BAE30913.1; -; mRNA.
EMBL; BC006744; AAH06744.1; -; mRNA.
EMBL; BC048691; AAH48691.1; -; mRNA.
CCDS; CCDS17531.1; -. [Q9Z266-1]
RefSeq; NP_598615.1; NM_133854.3. [Q9Z266-1]
UniGene; Mm.331182; -.
BioGrid; 203363; 4.
CORUM; Q9Z266; -.
IntAct; Q9Z266; 5.
MINT; MINT-3389684; -.
STRING; 10090.ENSMUSP00000122090; -.
iPTMnet; Q9Z266; -.
PhosphoSitePlus; Q9Z266; -.
EPD; Q9Z266; -.
PaxDb; Q9Z266; -.
PeptideAtlas; Q9Z266; -.
PRIDE; Q9Z266; -.
Ensembl; ENSMUST00000149884; ENSMUSP00000122090; ENSMUSG00000001018. [Q9Z266-1]
GeneID; 20615; -.
KEGG; mmu:20615; -.
UCSC; uc008qck.2; mouse. [Q9Z266-1]
CTD; 23557; -.
MGI; MGI:1333745; Snapin.
eggNOG; ENOG410J16C; Eukaryota.
eggNOG; ENOG4111JM9; LUCA.
GeneTree; ENSGT00390000008274; -.
HOGENOM; HOG000253926; -.
HOVERGEN; HBG056744; -.
InParanoid; Q9Z266; -.
KO; K20002; -.
OMA; INEHQKV; -.
OrthoDB; EOG091G0WH1; -.
PhylomeDB; Q9Z266; -.
TreeFam; TF319577; -.
Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
PRO; PR:Q9Z266; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000001018; -.
CleanEx; MM_SNAPIN; -.
ExpressionAtlas; Q9Z266; baseline and differential.
Genevisible; Q9Z266; MM.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0031083; C:BLOC-1 complex; IDA:MGI.
GO; GO:0099078; C:BORC complex; ISO:MGI.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
GO; GO:0045202; C:synapse; ISO:MGI.
GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0000149; F:SNARE binding; ISO:MGI.
GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
GO; GO:0048490; P:anterograde synaptic vesicle transport; IMP:UniProtKB.
GO; GO:0097352; P:autophagosome maturation; IMP:MGI.
GO; GO:0017156; P:calcium ion regulated exocytosis; TAS:ParkinsonsUK-UCL.
GO; GO:0034629; P:cellular protein complex localization; IMP:MGI.
GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
GO; GO:0008333; P:endosome to lysosome transport; ISO:MGI.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:1902774; P:late endosome to lysosome transport; IMP:MGI.
GO; GO:0007042; P:lysosomal lumen acidification; IMP:MGI.
GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
GO; GO:0007040; P:lysosome organization; IMP:MGI.
GO; GO:0010977; P:negative regulation of neuron projection development; IGI:ParkinsonsUK-UCL.
GO; GO:0031175; P:neuron projection development; NAS:UniProtKB.
GO; GO:0051604; P:protein maturation; IMP:MGI.
GO; GO:0043393; P:regulation of protein binding; ISO:MGI.
GO; GO:0008090; P:retrograde axonal transport; IMP:MGI.
GO; GO:0016079; P:synaptic vesicle exocytosis; ISO:MGI.
GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IMP:MGI.
GO; GO:0016188; P:synaptic vesicle maturation; IMP:MGI.
GO; GO:0048489; P:synaptic vesicle transport; ISS:UniProtKB.
GO; GO:0072553; P:terminal button organization; IMP:MGI.
InterPro; IPR017246; Snapin.
InterPro; IPR028119; Snapin/Pallidin/Snn1.
PANTHER; PTHR31305; PTHR31305; 1.
Pfam; PF14712; Snapin_Pallidin; 1.
PIRSF; PIRSF037631; Snapin; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell junction; Coiled coil;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Exocytosis;
Golgi apparatus; Lysosome; Membrane; Phosphoprotein;
Reference proteome; Synapse.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O95295}.
CHAIN 2 136 SNARE-associated protein Snapin.
/FTId=PRO_0000097557.
REGION 83 136 Interaction with TOR1A. {ECO:0000250}.
COILED 37 126 {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:O95295}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:O95295}.
MOD_RES 14 14 Phosphothreonine.
{ECO:0000250|UniProtKB:O95295}.
MOD_RES 50 50 Phosphoserine; by PKA; in vitro.
{ECO:0000269|PubMed:11283605}.
MOD_RES 126 126 Phosphoserine.
{ECO:0000250|UniProtKB:O95295}.
MOD_RES 129 129 Phosphotyrosine.
{ECO:0000250|UniProtKB:O95295}.
MOD_RES 133 133 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 54 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_009165.
VAR_SEQ 55 63 REQIDNLAT -> MLVAHFLFP (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_009166.
MUTAGEN 42 42 S->A: No effect.
{ECO:0000269|PubMed:11283605}.
MUTAGEN 50 50 S->A: Inhibition of phosphorylation.
{ECO:0000269|PubMed:11283605}.
MUTAGEN 50 50 S->D: 3.5-fold increase in SNAP25
binding. {ECO:0000269|PubMed:11283605}.
MUTAGEN 63 63 T->A: No effect.
{ECO:0000269|PubMed:11283605}.
SEQUENCE 136 AA; 14904 MW; C81AC2ABCDCA21FA CRC64;
MAAAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN
LATELCRINE DQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR
RAMLDSGVYP PGSPSK


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6017 Snell Ave, Ste 357
San Jose, CA 95123




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