ID   STXB3_HUMAN             Reviewed;         592 AA.
AC   O00186; A8K269; A8K5K7; Q53FW1; Q86YJ3; Q9UPD7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 2.
DT   27-MAR-2024, entry version 191.
DE   RecName: Full=Syntaxin-binding protein 3;
DE   AltName: Full=Platelet Sec1 protein;
DE            Short=PSP;
DE   AltName: Full=Protein unc-18 homolog 3;
DE            Short=Unc18-3;
DE   AltName: Full=Protein unc-18 homolog C;
DE            Short=Unc-18C;
GN   Name=STXBP3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLY-433 AND GLY-546.
RC   TISSUE=Brain;
RX   PubMed=8824310; DOI=10.1523/jneurosci.16-21-06695.1996;
RA   Gengyo-Ando K., Kitayama H., Mukaida M., Ikawa Y.;
RT   "A murine neural-specific homolog corrects cholinergic defects in
RT   Caenorhabditis elegans unc-18 mutants.";
RL   J. Neurosci. 16:6695-6702(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH STX4, SUBCELLULAR LOCATION,
RP   AND PHOSPHORYLATION.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=10194441;
RA   Reed G.L., Houng A.K., Fitzgerald M.L.;
RT   "Human platelets contain SNARE proteins and a Sec1p homologue that
RT   interacts with syntaxin 4 and is phosphorylated after thrombin activation:
RT   implications for platelet secretion.";
RL   Blood 93:2617-2626(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thalamus, and Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Together with STX4 and VAMP2, may play a role in insulin-
CC       dependent movement of GLUT4 and in docking/fusion of intracellular
CC       GLUT4-containing vesicles with the cell surface in adipocytes.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with DOC2B; the interaction is direct, occurs at the
CC       cell membrane, excludes interaction with STX4 and regulates glucose-
CC       stimulated insulin secretion (By similarity). Interacts with STX4.
CC       {ECO:0000250, ECO:0000269|PubMed:10194441}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10194441}.
CC       Cell membrane {ECO:0000269|PubMed:10194441}. Note=In platelets,
CC       predominantly cytosolic. Low amounts membrane-associated.
CC   -!- TISSUE SPECIFICITY: Megakaryocytes and platelets.
CC   -!- PTM: Phosphorylated by PKC in platelets in response to thrombin
CC       stimulation; phosphorylation inhibits binding to STX4.
CC       {ECO:0000269|PubMed:10194441}.
CC   -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
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DR   EMBL; D63506; BAA19482.1; -; mRNA.
DR   EMBL; AF032922; AAC69606.1; -; mRNA.
DR   EMBL; AK290134; BAF82823.1; -; mRNA.
DR   EMBL; AK291322; BAF84011.1; -; mRNA.
DR   EMBL; AK312910; BAG35756.1; -; mRNA.
DR   EMBL; AK223170; BAD96890.1; -; mRNA.
DR   EMBL; AL591719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL449266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471122; EAW56330.1; -; Genomic_DNA.
DR   EMBL; BC038099; AAH38099.1; -; mRNA.
DR   EMBL; BC047764; AAH47764.1; -; mRNA.
DR   CCDS; CCDS790.1; -.
DR   RefSeq; NP_009200.2; NM_007269.3.
DR   AlphaFoldDB; O00186; -.
DR   SMR; O00186; -.
DR   BioGRID; 112683; 92.
DR   IntAct; O00186; 28.
DR   MINT; O00186; -.
DR   STRING; 9606.ENSP00000359025; -.
DR   iPTMnet; O00186; -.
DR   MetOSite; O00186; -.
DR   PhosphoSitePlus; O00186; -.
DR   SwissPalm; O00186; -.
DR   BioMuta; STXBP3; -.
DR   EPD; O00186; -.
DR   jPOST; O00186; -.
DR   MassIVE; O00186; -.
DR   MaxQB; O00186; -.
DR   PaxDb; 9606-ENSP00000359025; -.
DR   PeptideAtlas; O00186; -.
DR   ProteomicsDB; 47766; -.
DR   Pumba; O00186; -.
DR   Antibodypedia; 20045; 260 antibodies from 30 providers.
DR   DNASU; 6814; -.
DR   Ensembl; ENST00000370008.4; ENSP00000359025.3; ENSG00000116266.11.
DR   GeneID; 6814; -.
DR   KEGG; hsa:6814; -.
DR   MANE-Select; ENST00000370008.4; ENSP00000359025.3; NM_007269.4; NP_009200.2.
DR   UCSC; uc001dvy.4; human.
DR   AGR; HGNC:11446; -.
DR   CTD; 6814; -.
DR   DisGeNET; 6814; -.
DR   GeneCards; STXBP3; -.
DR   HGNC; HGNC:11446; STXBP3.
DR   HPA; ENSG00000116266; Low tissue specificity.
DR   MIM; 608339; gene.
DR   neXtProt; NX_O00186; -.
DR   OpenTargets; ENSG00000116266; -.
DR   PharmGKB; PA36243; -.
DR   VEuPathDB; HostDB:ENSG00000116266; -.
DR   eggNOG; KOG1300; Eukaryota.
DR   GeneTree; ENSGT00940000157607; -.
DR   HOGENOM; CLU_009210_2_0_1; -.
DR   InParanoid; O00186; -.
DR   OMA; LSTCVRM; -.
DR   OrthoDB; 4609640at2759; -.
DR   PhylomeDB; O00186; -.
DR   TreeFam; TF313242; -.
DR   PathwayCommons; O00186; -.
DR   Reactome; R-HSA-114516; Disinhibition of SNARE formation.
DR   Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR   SignaLink; O00186; -.
DR   BioGRID-ORCS; 6814; 151 hits in 1165 CRISPR screens.
DR   ChiTaRS; STXBP3; human.
DR   GeneWiki; Syntaxin_binding_protein_3; -.
DR   GenomeRNAi; 6814; -.
DR   Pharos; O00186; Tbio.
DR   PRO; PR:O00186; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O00186; Protein.
DR   Bgee; ENSG00000116266; Expressed in corpus callosum and 202 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0031091; C:platelet alpha granule; IDA:UniProtKB.
DR   GO; GO:0098793; C:presynapse; IDA:SynGO.
DR   GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR   GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR   GO; GO:0070820; C:tertiary granule; IDA:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
DR   GO; GO:0017075; F:syntaxin-1 binding; IBA:GO_Central.
DR   GO; GO:0007420; P:brain development; IEA:Ensembl.
DR   GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl.
DR   GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IMP:UniProtKB.
DR   GO; GO:0046325; P:negative regulation of glucose import; IEA:Ensembl.
DR   GO; GO:0007269; P:neurotransmitter secretion; IBA:GO_Central.
DR   GO; GO:0043312; P:neutrophil degranulation; IEP:UniProtKB.
DR   GO; GO:0070527; P:platelet aggregation; IMP:UniProtKB.
DR   GO; GO:0022615; P:protein to membrane docking; IEA:Ensembl.
DR   GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 1.25.40.60; -; 1.
DR   Gene3D; 3.40.50.1910; -; 1.
DR   Gene3D; 3.40.50.2060; -; 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:SF33; SYNTAXIN-BINDING PROTEIN 3; 1.
DR   PANTHER; PTHR11679; VESICLE PROTEIN SORTING-ASSOCIATED; 1.
DR   Pfam; PF00995; Sec1; 1.
DR   PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR   SUPFAM; SSF56815; Sec1/munc18-like (SM) proteins; 1.
DR   Genevisible; O00186; HS.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..592
FT                   /note="Syntaxin-binding protein 3"
FT                   /id="PRO_0000206285"
FT   REGION          1..255
FT                   /note="Mediates interaction with DOC2B"
FT                   /evidence="ECO:0000250"
FT   VARIANT         295
FT                   /note="R -> Q (in dbSNP:rs2275344)"
FT                   /id="VAR_052470"
FT   VARIANT         433
FT                   /note="E -> G (in dbSNP:rs1044136)"
FT                   /evidence="ECO:0000269|PubMed:8824310"
FT                   /id="VAR_017570"
FT   VARIANT         546
FT                   /note="C -> G (in dbSNP:rs1044137)"
FT                   /evidence="ECO:0000269|PubMed:8824310"
FT                   /id="VAR_017571"
FT   CONFLICT        104
FT                   /note="K -> R (in Ref. 7; AAH38099)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        150
FT                   /note="L -> R (in Ref. 7; AAH38099)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        242
FT                   /note="F -> I (in Ref. 4; BAD96890)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        277
FT                   /note="E -> G (in Ref. 1; BAA19482)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        285
FT                   /note="E -> D (in Ref. 3; BAF84011)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   592 AA;  67764 MW;  AAFA268E2D328EC7 CRC64;
     MAPPVAERGL KSVVWQKIKA TVFDDCKKEG EWKIMLLDEF TTKLLASCCK MTDLLEEGIT
     VVENIYKNRE PVRQMKALYF ITPTSKSVDC FLHDFASKSE NKYKAAYIYF TDFCPDNLFN
     KIKASCSKSI RRCKEINISF IPHESQVYTL DVPDAFYYCY SPDPGNAKGK DAIMETMADQ
     IVTVCATLDE NPGVRYKSKP LDNASKLAQL VEKKLEDYYK IDEKSLIKGK THSQLLIIDR
     GFDPVSTVLH ELTFQAMAYD LLPIENDTYK YKTDGKEKEA ILEEEDDLWV RIRHRHIAVV
     LEEIPKLMKE ISSTKKATEG KTSLSALTQL MKKMPHFRKQ ITKQVVHLNL AEDCMNKFKL
     NIEKLCKTEQ DLALGTDAEG QKVKDSMRVL LPVLLNKNHD NCDKIRAILL YIFSINGTTE
     ENLDRLIQNV KIENESDMIR NWSYLGVPIV PQSQQGKPLR KDRSAEETFQ LSRWTPFIKD
     IMEDAIDNRL DSKEWPYCSQ CPAVWNGSGA VSARQKPRAN YLEDRKNGSK LIVFVIGGIT
     YSEVRCAYEV SQAHKSCEVI IGSTHVLTPK KLLDDIKMLN KPKDKVSLIK DE
//