SNPH_MOUSE
ID SNPH_MOUSE Reviewed; 495 AA.
AC Q80U23; A2AT08; A2AT09; A2AT10; A2AT11; A4FUV3; A4VCI7; Q4VA51; Q6GQX4;
AC Q8C8B8;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Syntaphilin;
GN Name=Snph; Synonyms=Kiaa0374;
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] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-204; THR-214 AND
RP SER-219, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Inhibits SNARE complex formation by absorbing free syntaxin-
CC 1. {ECO:0000250}.
CC -!- SUBUNIT: Binds to syntaxin-1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Synapse, synaptosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80U23-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80U23-2; Sequence=VSP_037439;
CC Name=3;
CC IsoId=Q80U23-3; Sequence=VSP_037440;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH72567.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH96541.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI39793.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC33090.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC65544.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK122262; BAC65544.1; ALT_INIT; mRNA.
DR EMBL; AK047568; BAC33090.1; ALT_INIT; mRNA.
DR EMBL; AL928719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC072567; AAH72567.1; ALT_INIT; mRNA.
DR EMBL; BC096541; AAH96541.1; ALT_INIT; mRNA.
DR EMBL; BC117896; AAI17897.1; -; mRNA.
DR EMBL; BC117897; AAI17898.1; -; mRNA.
DR EMBL; BC139792; AAI39793.1; ALT_INIT; mRNA.
DR CCDS; CCDS16871.1; -. [Q80U23-2]
DR CCDS; CCDS71161.1; -. [Q80U23-3]
DR CCDS; CCDS71162.1; -. [Q80U23-1]
DR RefSeq; NP_001278005.1; NM_001291076.1. [Q80U23-1]
DR RefSeq; NP_001278006.1; NM_001291077.1. [Q80U23-3]
DR RefSeq; NP_937857.1; NM_198214.3. [Q80U23-2]
DR RefSeq; XP_011237840.1; XM_011239538.1. [Q80U23-2]
DR AlphaFoldDB; Q80U23; -.
DR BioGRID; 232344; 1.
DR IntAct; Q80U23; 2.
DR MINT; Q80U23; -.
DR STRING; 10090.ENSMUSP00000028951; -.
DR iPTMnet; Q80U23; -.
DR PhosphoSitePlus; Q80U23; -.
DR SwissPalm; Q80U23; -.
DR MaxQB; Q80U23; -.
DR PeptideAtlas; Q80U23; -.
DR PRIDE; Q80U23; -.
DR ProteomicsDB; 261293; -. [Q80U23-1]
DR ProteomicsDB; 261294; -. [Q80U23-2]
DR ProteomicsDB; 261295; -. [Q80U23-3]
DR Antibodypedia; 34949; 178 antibodies from 31 providers.
DR DNASU; 241727; -.
DR Ensembl; ENSMUST00000028951; ENSMUSP00000028951; ENSMUSG00000027457. [Q80U23-2]
DR Ensembl; ENSMUST00000094456; ENSMUSP00000092026; ENSMUSG00000027457. [Q80U23-1]
DR Ensembl; ENSMUST00000109875; ENSMUSP00000105501; ENSMUSG00000027457. [Q80U23-2]
DR Ensembl; ENSMUST00000109877; ENSMUSP00000105503; ENSMUSG00000027457. [Q80U23-3]
DR GeneID; 241727; -.
DR KEGG; mmu:241727; -.
DR UCSC; uc008ned.2; mouse. [Q80U23-2]
DR UCSC; uc008nee.2; mouse. [Q80U23-1]
DR UCSC; uc008nef.2; mouse. [Q80U23-3]
DR CTD; 9751; -.
DR MGI; MGI:2139270; Snph.
DR VEuPathDB; HostDB:ENSMUSG00000027457; -.
DR eggNOG; ENOG502QUYH; Eukaryota.
DR GeneTree; ENSGT00520000055634; -.
DR HOGENOM; CLU_019458_1_0_1; -.
DR InParanoid; Q80U23; -.
DR OMA; NSLCPIP; -.
DR OrthoDB; 391092at2759; -.
DR PhylomeDB; Q80U23; -.
DR TreeFam; TF332407; -.
DR BioGRID-ORCS; 241727; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q80U23; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80U23; protein.
DR Bgee; ENSMUSG00000027457; Expressed in visual cortex and 101 other tissues.
DR ExpressionAtlas; Q80U23; baseline and differential.
DR Genevisible; Q80U23; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0017075; F:syntaxin-1 binding; IEA:InterPro.
DR GO; GO:0045806; P:negative regulation of endocytosis; ISO:MGI.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; ISO:MGI.
DR InterPro; IPR026196; Syntaphilin.
DR InterPro; IPR028197; Syntaphilin/Syntabulin.
DR PANTHER; PTHR16208:SF1; PTHR16208:SF1; 1.
DR Pfam; PF15290; Syntaphilin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Membrane; Phosphoprotein;
KW Reference proteome; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..495
FT /note="Syntaphilin"
FT /id="PRO_0000284137"
FT TRANSMEM 427..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 79..161
FT /evidence="ECO:0000255"
FT COMPBIAS 1..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:B5DF41"
FT VAR_SEQ 16
FT /note="R -> RSGGTLGRSGLAVFAQCPQVPASQNEQRPLLPAS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_037439"
FT VAR_SEQ 17..52
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037440"
FT CONFLICT 156
FT /note="L -> V (in Ref. 2; BAC33090)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="K -> M (in Ref. 4; AAH96541)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="D -> Y (in Ref. 2; BAC33090)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="I -> V (in Ref. 4; AAI17897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 53753 MW; D1BA1C0702446C97 CRC64;
MAMSLQGSRR ASAGSRRRTS PPVSVRDAYG TSSLSSSSNS GSCKGSDSSP TPRRSMKYTL
CSDNHGIKPP TPEQYLTPLQ QKEVCIRHLK ARLKDTQDRL QDRDTEIDDL KTQLSRMQED
WIEEECHRVE AQLALKEARK EIRQLKQVID TVKNNLIDKD KGLQKYFVDI NIQNKKLETL
LHSMEVAQNG VAKEEGTGES AGGSPARSLT RSSTYTKLSD PAVCGDRQPG DPSNTSAEDG
ADSGYVAADD TLSRTDALEA SSLLSSGVDC GLEEASLHSS FNLGPRFPAS NTYEKLLCGM
EAGVQVSCMQ ERAIQTDFVQ YQPDLNTILE KVGQAQVCGS VLKDRHSELD PHPSGPRDPD
SAVVVTVGDE LEAPEPITCG PATHRPAVNS NPGLPVSVVC PVEEEEEEAA AATTTEKEPK
SYWSRHYIVD LLAVVVPAVP TVAWLCRSQR RQGQPIYNIS SLLRGCCTVA LHSIRRISCR
SLGQPSSSTA GGSQL
