SNPH_RAT
ID SNPH_RAT Reviewed; 504 AA.
AC B5DF41;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Syntaphilin;
GN Name=Snph;
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;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-204 AND THR-235, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
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DR EMBL; CH474050; EDL86108.1; -; Genomic_DNA.
DR EMBL; CH474050; EDL86111.1; -; Genomic_DNA.
DR EMBL; BC168917; AAI68917.1; -; mRNA.
DR RefSeq; NP_001099995.1; NM_001106525.3.
DR AlphaFoldDB; B5DF41; -.
DR BioGRID; 255298; 1.
DR STRING; 10116.ENSRNOP00000012727; -.
DR iPTMnet; B5DF41; -.
DR PaxDb; B5DF41; -.
DR PRIDE; B5DF41; -.
DR GeneID; 296267; -.
DR KEGG; rno:296267; -.
DR UCSC; RGD:1305867; rat.
DR CTD; 9751; -.
DR RGD; 1305867; Snph.
DR VEuPathDB; HostDB:ENSRNOG00000009588; -.
DR eggNOG; ENOG502QUYH; Eukaryota.
DR InParanoid; B5DF41; -.
DR OMA; NSLCPIP; -.
DR OrthoDB; 391092at2759; -.
DR PhylomeDB; B5DF41; -.
DR PRO; PR:B5DF41; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000009588; Expressed in frontal cortex and 14 other tissues.
DR Genevisible; B5DF41; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0042734; C:presynaptic membrane; IDA:RGD.
DR GO; GO:0017075; F:syntaxin-1 binding; IEA:InterPro.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
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 Coiled coil; Membrane; Phosphoprotein; Reference proteome; Synapse;
KW Synaptosome; Transmembrane; Transmembrane helix.
FT CHAIN 1..504
FT /note="Syntaphilin"
FT /id="PRO_0000376936"
FT TRANSMEM 437..456
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..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..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:22673903"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80U23"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80U23"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 504 AA; 54494 MW; CED9AE656A7A6C58 CRC64;
MAMSLQGSRR ASAGSRRRTS PPVSVRDAYG TASLSSSSNS GSCKGSDSSP TPRRSMKYTL
CSDNHGIKPP TPEQYLTPLQ QKEVCIRHLK ARLKDTQDRL QDRDTEIDDL KTQLSRMQED
WIEEECHRVE AQLALKEARK EIRQLKQVID TVKNNLIDKD KGLQKYFVDI NIQNKKLETL
LHSMEVAQNG VAKEEGTGES AGGSPARSLT RSSTYTKLSD PAVCGDRQAG DPSNTPAEDR
ADSGFVAADD TLSRTEALEA SSLLSSGVDC GFEEASLHSS FNLGPRFPAS NTYEKLLCGM
EAAVQASCMQ ERAIQTDFVQ YQPDLNTILE KVGQAQGCSS VLKDRHSELD LHPSGPRDPD
SAVVVTVGDE PEAPEPITRG PAIHRPAVNS NPGLPVSVVC PVEEEEEAAA AAAAAAAATT
TTTTTEKEPK SYWSRHYIVD LLAVVVPAVP TVAWLCRSQR RQGQPIYNIS SLLRGCCTVA
LHSIRRISCS LSQPSAGSSG GSQL
