SNAPN_RAT
ID SNAPN_RAT Reviewed; 136 AA.
AC P60192;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=SNARE-associated protein Snapin;
DE AltName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 7;
DE Short=BLOC-1 subunit 7;
DE AltName: Full=Synaptosomal-associated protein 25-binding protein;
DE Short=SNAP-associated protein;
GN Name=Snapin; Synonyms=Bloc1s7, Snap25bp, Snapap;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
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]
RP FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10195194; DOI=10.1038/5673;
RA Ilardi J.M., Mochida S., Sheng Z.-H.;
RT "Snapin: a SNARE-associated protein implicated in synaptic transmission.";
RL Nat. Neurosci. 2:119-124(1999).
RN [3]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=11283605; DOI=10.1038/35070000;
RA Chheda M.G., Ashery U., Thakur P., Rettig J., Sheng Z.-H.;
RT "Phosphorylation of Snapin by PKA modulates its interaction with the SNARE
RT complex.";
RL Nat. Cell Biol. 3:331-338(2001).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12877659; DOI=10.1042/bj20030427;
RA Buxton P., Zhang X.-M., Walsh B., Sriratana A., Schenberg I., Manickam E.,
RA Rowe T.;
RT "Identification and characterization of Snapin as a ubiquitously expressed
RT SNARE-binding protein that interacts with SNAP23 in non-neuronal cells.";
RL Biochem. J. 375:433-440(2003).
RN [5]
RP IDENTIFICATION IN THE BLOC-1 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16760431; DOI=10.1091/mbc.e06-02-0103;
RA Salazar G., Craige B., Styers M.L., Newell-Litwa K.A., Doucette M.M.,
RA Wainer B.H., Falcon-Perez J.M., Dell'Angelica E.C., Peden A.A., Werner E.,
RA Faundez V.;
RT "BLOC-1 complex deficiency alters the targeting of adaptor protein complex-
RT 3 cargoes.";
RL Mol. Biol. Cell 17:4014-4026(2006).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=18167355; DOI=10.1074/jbc.m704097200;
RA Granata A., Watson R., Collinson L.M., Schiavo G., Warner T.T.;
RT "The dystonia-associated protein torsinA modulates synaptic vesicle
RT recycling.";
RL J. Biol. Chem. 283:7568-7579(2008).
CC -!- FUNCTION: Component of the BLOC-1 complex, a complex that is required
CC for normal biogenesis of lysosome-related organelles (LRO), such as
CC platelet dense granules and melanosomes. In concert with the AP-3
CC complex, the BLOC-1 complex is required to target membrane protein
CC cargos into vesicles assembled at cell bodies for delivery into
CC neurites and nerve terminals. The BLOC-1 complex, in association with
CC SNARE proteins, is also proposed to be involved in neurite extension.
CC Plays a role in intracellular vesicle trafficking and synaptic vesicle
CC recycling. May modulate a step between vesicle priming, fusion and
CC calcium-dependent neurotransmitter release through its ability to
CC potentiate the interaction of synaptotagmin with the SNAREs and the
CC plasma-membrane-associated protein SNAP25. Its phosphorylation state
CC influences exocytotic protein interactions and may regulate synaptic
CC vesicle exocytosis. May also have a role in the mechanisms of SNARE-
CC mediated membrane fusion in non-neuronal cells (PubMed:10195194,
CC PubMed:11283605). As part of the BORC complex may play a role in
CC lysosomes movement and localization at the cell periphery. Associated
CC with the cytosolic face of lysosomes, the BORC complex may recruit
CC ARL8B and couple lysosomes to microtubule plus-end-directed kinesin
CC motor (By similarity). {ECO:0000250|UniProtKB:O95295,
CC ECO:0000269|PubMed:10195194, ECO:0000269|PubMed:11283605}.
CC -!- SUBUNIT: Component of the biogenesis of lysosome-related organelles
CC complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4,
CC BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed
CC of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6,
CC DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with
CC the AP-3 protein complex and membrane protein cargos (PubMed:16760431).
CC Component of the BLOC-one-related complex (BORC) which is composed of
CC BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and SNAPIN (By
CC similarity). Associates with the SNARE complex. Interacts with CSNK1D,
CC SNAP23 and STX4A but not with STX1A, VAMP2 and SYT1. Interacts with
CC SNAP25; the interaction with SNAP25 is increased by its phosphorylation
CC (By similarity). Interacts with CNTRL, NANOS1, PUM2 and RGS7. Interacts
CC with TOR1A; the interaction is direct and associates SNAPIN with the
CC CSN complex (By similarity). {ECO:0000250|UniProtKB:O95295,
CC ECO:0000250|UniProtKB:Q9Z266, ECO:0000269|PubMed:16760431}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Z266};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z266}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q9Z266}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9Z266}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q9Z266}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9Z266}. Lysosome membrane
CC {ECO:0000250|UniProtKB:O95295}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000269|PubMed:18167355}.
CC Note=Colocalizes with NANOS1 and PUM2 in the perinuclear region of germ
CC cells. {ECO:0000250|UniProtKB:O95295}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in testis, spleen, kidney, liver
CC and brain; lower expression in heart, fat and skeletal muscle.
CC {ECO:0000269|PubMed:10195194, ECO:0000269|PubMed:12877659}.
CC -!- PTM: Phosphorylated by CSNK1D/CK1. {ECO:0000269|PubMed:11283605}.
CC -!- SIMILARITY: Belongs to the SNAPIN family. {ECO:0000305}.
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DR EMBL; AABR03012141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CB613900; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001164047.1; NM_001170576.1.
DR AlphaFoldDB; P60192; -.
DR SMR; P60192; -.
DR BioGRID; 254916; 1.
DR ELM; P60192; -.
DR IntAct; P60192; 7.
DR MINT; P60192; -.
DR STRING; 10116.ENSRNOP00000018830; -.
DR iPTMnet; P60192; -.
DR PhosphoSitePlus; P60192; -.
DR PaxDb; P60192; -.
DR PRIDE; P60192; -.
DR ABCD; P60192; 1 sequenced antibody.
DR GeneID; 295217; -.
DR KEGG; rno:295217; -.
DR UCSC; RGD:1560377; rat.
DR CTD; 23557; -.
DR RGD; 1560377; Snapin.
DR VEuPathDB; HostDB:ENSRNOG00000013356; -.
DR eggNOG; ENOG502S07W; Eukaryota.
DR HOGENOM; CLU_124640_1_0_1; -.
DR InParanoid; P60192; -.
DR OMA; QLDTHVH; -.
DR OrthoDB; 1532513at2759; -.
DR PhylomeDB; P60192; -.
DR TreeFam; TF319577; -.
DR Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis.
DR PRO; PR:P60192; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000013356; Expressed in ovary and 20 other tissues.
DR Genevisible; P60192; RN.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:RGD.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0031083; C:BLOC-1 complex; ISS:UniProtKB.
DR GO; GO:0099078; C:BORC complex; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002177; C:manchette; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:SynGO.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000149; F:SNARE binding; ISO:RGD.
DR GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0008333; P:endosome to lysosome transport; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:1902774; P:late endosome to lysosome transport; ISO:RGD.
DR GO; GO:0007042; P:lysosomal lumen acidification; ISO:RGD.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0051604; P:protein maturation; ISO:RGD.
DR GO; GO:0031503; P:protein-containing complex localization; ISO:RGD.
DR GO; GO:0043393; P:regulation of protein binding; ISO:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:0008090; P:retrograde axonal transport; ISO:RGD.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; ISO:RGD.
DR GO; GO:0016188; P:synaptic vesicle maturation; ISO:RGD.
DR GO; GO:0048489; P:synaptic vesicle transport; ISS:UniProtKB.
DR GO; GO:0072553; P:terminal button organization; ISO:RGD.
DR InterPro; IPR017246; Snapin.
DR InterPro; IPR028119; Snapin/Pallidin/Snn1.
DR PANTHER; PTHR31305; PTHR31305; 1.
DR Pfam; PF14712; Snapin_Pallidin; 1.
DR PIRSF; PIRSF037631; Snapin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Exocytosis;
KW Golgi apparatus; Lysosome; Membrane; Phosphoprotein; Reference proteome;
KW Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95295"
FT CHAIN 2..136
FT /note="SNARE-associated protein Snapin"
FT /id="PRO_0000097558"
FT REGION 83..136
FT /note="Interaction with TOR1A"
FT /evidence="ECO:0000250"
FT COILED 37..126
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O95295"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95295"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95295"
FT MOD_RES 50
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q9Z266"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95295"
FT MOD_RES 129
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O95295"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95295"
SQ SEQUENCE 136 AA; 14904 MW; C81AC2ABCDCA21FA CRC64;
MAAAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN
LATELCRINE DQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR
RAMLDSGVYP PGSPSK
