STXB1_PONAB
ID STXB1_PONAB Reviewed; 594 AA.
AC Q5R6D2;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Syntaxin-binding protein 1;
DE AltName: Full=N-Sec1;
DE AltName: Full=Protein unc-18 homolog 1;
DE Short=Unc18-1;
DE AltName: Full=Protein unc-18 homolog A;
DE Short=Unc-18A;
GN Name=STXBP1; Synonyms=UNC18A;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May participate in the regulation of synaptic vesicle docking
CC and fusion, possibly through interaction with GTP-binding proteins.
CC Essential for neurotransmission and binds syntaxin, a component of the
CC synaptic vesicle fusion machinery probably in a 1:1 ratio. Can interact
CC with syntaxins 1, 2, and 3 but not syntaxin 4. May play a role in
CC determining the specificity of intracellular fusion reactions (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds SYTL4 (By similarity). Interacts with STX1A (By
CC similarity). Interacts with alpha-synuclein/SNCA; this interaction
CC controls SNCA self-replicating aggregation (By similarity). Interacts
CC with CABP5 (By similarity). {ECO:0000250|UniProtKB:P61763,
CC ECO:0000250|UniProtKB:P61764, ECO:0000250|UniProtKB:P61765}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P61764}. Membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
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DR EMBL; CR860559; CAH92684.1; -; mRNA.
DR RefSeq; NP_001126572.1; NM_001133100.1.
DR AlphaFoldDB; Q5R6D2; -.
DR SMR; Q5R6D2; -.
DR STRING; 9601.ENSPPYP00000021991; -.
DR Ensembl; ENSPPYT00000022898; ENSPPYP00000021991; ENSPPYG00000019625.
DR GeneID; 100173563; -.
DR KEGG; pon:100173563; -.
DR CTD; 6812; -.
DR eggNOG; KOG1300; Eukaryota.
DR GeneTree; ENSGT00940000155127; -.
DR HOGENOM; CLU_009210_2_0_1; -.
DR InParanoid; Q5R6D2; -.
DR OrthoDB; 725424at2759; -.
DR Proteomes; UP000001595; Chromosome 9.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR Gene3D; 3.40.50.1910; -; 1.
DR Gene3D; 3.40.50.2060; -; 1.
DR Gene3D; 3.90.830.10; -; 1.
DR InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR Pfam; PF00995; Sec1; 1.
DR PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..594
FT /note="Syntaxin-binding protein 1"
FT /id="PRO_0000291775"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61765"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08599"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08599"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08599"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61765"
SQ SEQUENCE 594 AA; 67569 MW; 2DD0715F875CE0F3 CRC64;
MAPIGLKAVV GEKIMHDVIK KVKKKGEWKV LVVDQLSMRM LSSCCKMTDI MTEGITIVED
INKRREPLPS LEAVYLITPS EKSVHSLISD FKDPPTAKYR AAHVFFTDSC PDALFNELVK
SRAAKVIKTL TEINIAFLPY ESQVYSLDSA DSFQSFYSPH KAQMKNPILE RLAEQIATLC
ATLKEYPAVR YRGEYKDNAL LAQLIQDKLD AYKADDPTMG EGPDKARSQL LILDRGFDPS
SPVLHELTFQ AMSYDLLPIE NDVYKYETSG IGEARVKEVL LDEDDDLWIA LRHKHIAEVS
QEVTRSLKDF SSSKRMNTGE KTTMRDLSQM LKKMPQYQKE LSKYSTHLHL AEDCMKHYQG
TVDKLCRVEQ DLAMGTDAEG EKIKDPMRAI VPILLDANVS TYDKIRIILL YIFLKNGITE
ENLNKLIQHA QIPPEDSEII TNMAHLGVPI VTDSTLRRRS KPERKERISE QTYQLSRWTP
IIKDIMEDTI EDKLDTKHYP YISTRSSASF STTAVSARYG HWHKNKAPGE YRSGPRLIIF
ILGGVSLNEM RCAYEVTQAN GKWEVLIGST HILTPQKLLD TLKKLNKTDE EISS