ID STX3_HUMAN Reviewed; 289 AA.
AC Q13277; B4DME0; O43750; O43751; Q15360;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 27-MAR-2024, entry version 205.
DE RecName: Full=Syntaxin-3;
GN Name=STX3; Synonyms=STX3A;
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] (ISOFORM A).
RC TISSUE=Colon;
RA Naren A.P., Bradbury N.A., Bennett M.K., Kirk K.L.;
RT "Syntaxin and n-Sec1 isoforms in colonic epithelial cells: association of
RT syntaxins 1A and 3 with apical endocytic pathway.";
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC TISSUE=Duodenum;
RX PubMed=9378770; DOI=10.1242/jcs.110.18.2207;
RA Delgrossi M.H., Breuza L., Mirre C., Chavrier P., le Bivic A.;
RT "Human syntaxin 3 is localized apically in human intestinal cells.";
RL J. Cell Sci. 110:2207-2214(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RX PubMed=10080545; DOI=10.1002/jlb.65.3.397;
RA Martin-Martin B., Nabokina S.M., Lazo P.A., Mollinedo F.;
RT "Co-expression of several human syntaxin genes in neutrophils and
RT differentiating HL-60 cells: variant isoforms and detection of syntaxin
RT 1.";
RL J. Leukoc. Biol. 65:397-406(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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] (ISOFORM A).
RC TISSUE=Muscle;
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 INVOLVEMENT IN RDMVID, INVOLVEMENT IN DIAR12, VARIANT DIAR12
RP 247-ARG--ASN-289 DEL, CHARACTERIZATIONOF VARIANT DIAR12 247-ARG--ASN-289
RP DEL, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24726755; DOI=10.1053/j.gastro.2014.04.002;
RA Wiegerinck C.L., Janecke A.R., Schneeberger K., Vogel G.F.,
RA van Haaften-Visser D.Y., Escher J.C., Adam R., Thoeni C.E., Pfaller K.,
RA Jordan A.J., Weis C.A., Nijman I.J., Monroe G.R., van Hasselt P.M.,
RA Cutz E., Klumperman J., Clevers H., Nieuwenhuis E.E., Houwen R.H.,
RA van Haaften G., Hess M.W., Huber L.A., Stapelbroek J.M., Mueller T.,
RA Middendorp S.;
RT "Loss of syntaxin 3 causes variant microvillus inclusion disease.";
RL Gastroenterology 147:65.e10-68e.10(2014).
RN [10]
RP ALTERNATIVE SPLICING (ISOFORM 3), FUNCTION (ISOFORM 3), SUBCELLULAR
RP LOCATION (ISOFORM 3), INTERACTION WITH IPO5A (ISOFORM 3), AND TISSUE
RP SPECIFICITY (ISOFORM 3).
RX PubMed=29475951; DOI=10.1074/jbc.ra117.000874;
RA Giovannone A.J., Winterstein C., Bhattaram P., Reales E., Low S.H.,
RA Baggs J.E., Xu M., Lalli M.A., Hogenesch J.B., Weimbs T.;
RT "Soluble syntaxin 3 functions as a transcriptional regulator.";
RL J. Biol. Chem. 293:5478-5491(2018).
RN [11]
RP VARIANT GLY-41.
RX PubMed=25358429; DOI=10.1111/cge.12489;
RA Chograni M., Alkuraya F.S., Ourteni I., Maazoul F., Lariani I.,
RA Chaabouni H.B.;
RT "Autosomal recessive congenital cataract, intellectual disability phenotype
RT linked to STX3 in a consanguineous Tunisian family.";
RL Clin. Genet. 88:283-287(2015).
RN [12]
RP VARIANT RDMVID 247-ARG--ASN-289 DEL.
RX PubMed=29282386; DOI=10.1159/000479624;
RA Alsaleem B.M.R., Ahmed A.B.M., Fageeh M.A.;
RT "Microvillus Inclusion Disease Variant in an Infant with Intractable
RT Diarrhea.";
RL Case Rep. Gastroenterol. 11:647-651(2017).
RN [13]
RP VARIANT RDMVID 247-ARG--ASN-289 DEL, FUNCTION (ISOFORM B), AND TISSUE
RP SPECIFICITY (ISOFORM B).
RX PubMed=33974130; DOI=10.1007/s00439-021-02284-1;
RA Janecke A.R., Liu X., Adam R., Punuru S., Viestenz A., Strauss V.,
RA Laass M., Sanchez E., Adachi R., Schatz M.P., Saboo U.S., Mittal N.,
RA Rohrschneider K., Escher J., Ganesh A., Al Zuhaibi S., Al Murshedi F.,
RA AlSaleem B., Alfadhel M., Al Sinani S., Alkuraya F.S., Huber L.A.,
RA Mueller T., Heidelberger R., Janz R.;
RT "Pathogenic STX3 variants affecting the retinal and intestinal transcripts
RT cause an early-onset severe retinal dystrophy in microvillus inclusion
RT disease subjects.";
RL Hum. Genet. 140:1143-1156(2021).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Potentially involved in docking of synaptic vesicles at
CC presynaptic active zones. Apical receptor involved in membrane fusion
CC of apical vesicles. {ECO:0000269|PubMed:24726755}.
CC -!- FUNCTION: [Isoform B]: Essential for survival of retinal
CC photoreceetors. {ECO:0000269|PubMed:33974130}.
CC -!- FUNCTION: [Isoform 3]: Functions as a regulator of gene expression.
CC {ECO:0000269|PubMed:29475951}.
CC -!- SUBUNIT: Interacts with REEP6 (By similarity). Interacts with PRPH2 in
CC rod and cone photoreceptors (By similarity). Interacts with ROM1 (By
CC similarity). Interacts with SNAP25 (By similarity). Interacts with
CC VAMP2 (By similarity). {ECO:0000250|UniProtKB:Q64704}.
CC -!- SUBUNIT: [Isoform 3]: Interacts with IPO5.
CC {ECO:0000269|PubMed:29475951}.
CC -!- INTERACTION:
CC Q13277; Q13520: AQP6; NbExp=3; IntAct=EBI-1394295, EBI-13059134;
CC Q13277; P11912: CD79A; NbExp=3; IntAct=EBI-1394295, EBI-7797864;
CC Q13277; O75208: COQ9; NbExp=3; IntAct=EBI-1394295, EBI-724524;
CC Q13277; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-1394295, EBI-18013275;
CC Q13277; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-1394295, EBI-6942903;
CC Q13277; P49447: CYB561; NbExp=3; IntAct=EBI-1394295, EBI-8646596;
CC Q13277; O00559: EBAG9; NbExp=3; IntAct=EBI-1394295, EBI-8787095;
CC Q13277; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-1394295, EBI-18535450;
CC Q13277; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-1394295, EBI-781551;
CC Q13277; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-1394295, EBI-18304435;
CC Q13277; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-1394295, EBI-12175685;
CC Q13277; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-1394295, EBI-13345167;
CC Q13277; Q8TED1: GPX8; NbExp=3; IntAct=EBI-1394295, EBI-11721746;
CC Q13277; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-1394295, EBI-10266796;
CC Q13277; Q9NQG1: MANBAL; NbExp=3; IntAct=EBI-1394295, EBI-3867271;
CC Q13277; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-1394295, EBI-373355;
CC Q13277; O14880: MGST3; NbExp=3; IntAct=EBI-1394295, EBI-724754;
CC Q13277; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-1394295, EBI-6163737;
CC Q13277; Q15800: MSMO1; NbExp=3; IntAct=EBI-1394295, EBI-949102;
CC Q13277; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-1394295, EBI-3923617;
CC Q13277; Q9H115: NAPB; NbExp=8; IntAct=EBI-1394295, EBI-3921185;
CC Q13277; O15173: PGRMC2; NbExp=3; IntAct=EBI-1394295, EBI-1050125;
CC Q13277; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-1394295, EBI-7545592;
CC Q13277; Q96TC7: RMDN3; NbExp=3; IntAct=EBI-1394295, EBI-1056589;
CC Q13277; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-1394295, EBI-17247926;
CC Q13277; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-1394295, EBI-17295964;
CC Q13277; O95721: SNAP29; NbExp=3; IntAct=EBI-1394295, EBI-490676;
CC Q13277; Q16623: STX1A; NbExp=3; IntAct=EBI-1394295, EBI-712466;
CC Q13277; P32856-2: STX2; NbExp=3; IntAct=EBI-1394295, EBI-11956649;
CC Q13277; Q12846: STX4; NbExp=8; IntAct=EBI-1394295, EBI-744942;
CC Q13277; Q13190: STX5; NbExp=3; IntAct=EBI-1394295, EBI-714206;
CC Q13277; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-1394295, EBI-8638294;
CC Q13277; Q6ZT21: TMPPE; NbExp=3; IntAct=EBI-1394295, EBI-11724433;
CC Q13277; Q9Y320: TMX2; NbExp=3; IntAct=EBI-1394295, EBI-6447886;
CC Q13277; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-1394295, EBI-12837904;
CC Q13277; O95405: ZFYVE9; NbExp=3; IntAct=EBI-1394295, EBI-296817;
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Apical cell membrane
CC {ECO:0000269|PubMed:24726755}; Single-pass type IV membrane protein
CC {ECO:0000305}. Note=Localized to the inner and outer plexiform layers,
CC the cell body and the inner segments of photoreceptors.
CC {ECO:0000250|UniProtKB:Q64704}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus
CC {ECO:0000269|PubMed:29475951}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=Q13277-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q13277-2; Sequence=VSP_006340;
CC Name=3; Synonyms=S {ECO:0000303|PubMed:29475951}, Non-membrane-anchored
CC form {ECO:0000303|PubMed:29475951};
CC IsoId=Q13277-3; Sequence=VSP_043187;
CC -!- TISSUE SPECIFICITY: [Isoform A]: Expressed in small intestine, kidney,
CC pancreas, placenta as well as in retina. Weaker expression in lung,
CC liver and heart. Not expressed in brain and skeletal muscle.
CC {ECO:0000269|PubMed:24726755, ECO:0000269|PubMed:33974130}.
CC -!- TISSUE SPECIFICITY: [Isoform B]: Expressed only in the retina.
CC {ECO:0000269|PubMed:33974130}.
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Ubiquitously expressed.
CC {ECO:0000269|PubMed:29475951}.
CC -!- DISEASE: Retinal dystrophy and microvillus inclusion disease (RDMVID)
CC [MIM:619446]: An autosomal recessive disease characterized by early-
CC onset, severe retinal dystrophy associated with intractable congenital
CC diarrhea. Intestinal biopsies show loss of microvilli, microvillus
CC inclusions, and accumulation of subapical vesicles in villus
CC enterocytes. {ECO:0000269|PubMed:24726755, ECO:0000269|PubMed:29282386,
CC ECO:0000269|PubMed:33974130}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Diarrhea 12, with microvillus atrophy (DIAR12) [MIM:619445]:
CC An autosomal recessive congenital enteropathy characterized by
CC intractable secretory diarrhea, resulting in severe dehydration and
CC metabolic acidosis. DIAR12 can be diagnosed based on variable loss of
CC brush-border microvilli, microvillus inclusions, and accumulation of
CC subapical vesicles in villus enterocytes.
CC {ECO:0000269|PubMed:24726755}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; U32315; AAA75303.1; -; mRNA.
DR EMBL; X90581; CAA62209.1; -; mRNA.
DR EMBL; AJ002076; CAA05175.1; -; mRNA.
DR EMBL; AJ002077; CAA05176.1; -; mRNA.
DR EMBL; AK297419; BAG59852.1; -; mRNA.
DR EMBL; AP000640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW73854.1; -; Genomic_DNA.
DR EMBL; BC007405; AAH07405.1; -; mRNA.
DR EMBL; BC007429; AAH07429.1; -; mRNA.
DR CCDS; CCDS53637.1; -. [Q13277-3]
DR CCDS; CCDS7975.1; -. [Q13277-1]
DR PIR; G01969; G01969.
DR RefSeq; NP_001171511.1; NM_001178040.1. [Q13277-3]
DR RefSeq; NP_004168.1; NM_004177.4. [Q13277-1]
DR RefSeq; XP_005274252.1; XM_005274195.3. [Q13277-1]
DR RefSeq; XP_005274257.1; XM_005274200.3.
DR AlphaFoldDB; Q13277; -.
DR SMR; Q13277; -.
DR BioGRID; 112678; 153.
DR CORUM; Q13277; -.
DR IntAct; Q13277; 104.
DR MINT; Q13277; -.
DR STRING; 9606.ENSP00000338562; -.
DR TCDB; 8.A.91.1.6; the syntaxin (syntaxin) family.
DR iPTMnet; Q13277; -.
DR PhosphoSitePlus; Q13277; -.
DR SwissPalm; Q13277; -.
DR BioMuta; STX3; -.
DR DMDM; 116242806; -.
DR EPD; Q13277; -.
DR jPOST; Q13277; -.
DR MassIVE; Q13277; -.
DR MaxQB; Q13277; -.
DR PaxDb; 9606-ENSP00000338562; -.
DR PeptideAtlas; Q13277; -.
DR ProteomicsDB; 59271; -. [Q13277-1]
DR ProteomicsDB; 59272; -. [Q13277-2]
DR ProteomicsDB; 59273; -. [Q13277-3]
DR Pumba; Q13277; -.
DR Antibodypedia; 724; 198 antibodies from 31 providers.
DR DNASU; 6809; -.
DR Ensembl; ENST00000337979.9; ENSP00000338562.4; ENSG00000166900.17. [Q13277-1]
DR Ensembl; ENST00000529177.5; ENSP00000433248.1; ENSG00000166900.17. [Q13277-3]
DR GeneID; 6809; -.
DR KEGG; hsa:6809; -.
DR MANE-Select; ENST00000337979.9; ENSP00000338562.4; NM_004177.5; NP_004168.1.
DR UCSC; uc010rkx.3; human. [Q13277-1]
DR AGR; HGNC:11438; -.
DR CTD; 6809; -.
DR DisGeNET; 6809; -.
DR GeneCards; STX3; -.
DR HGNC; HGNC:11438; STX3.
DR HPA; ENSG00000166900; Tissue enriched (retina).
DR MalaCards; STX3; -.
DR MIM; 600876; gene.
DR MIM; 619445; phenotype.
DR MIM; 619446; phenotype.
DR neXtProt; NX_Q13277; -.
DR OpenTargets; ENSG00000166900; -.
DR Orphanet; 2290; Microvillus inclusion disease.
DR PharmGKB; PA36235; -.
DR VEuPathDB; HostDB:ENSG00000166900; -.
DR eggNOG; KOG0810; Eukaryota.
DR GeneTree; ENSGT01030000234627; -.
DR InParanoid; Q13277; -.
DR OrthoDB; 2876074at2759; -.
DR PhylomeDB; Q13277; -.
DR TreeFam; TF313763; -.
DR PathwayCommons; Q13277; -.
DR Reactome; R-HSA-449836; Other interleukin signaling.
DR SignaLink; Q13277; -.
DR BioGRID-ORCS; 6809; 14 hits in 1155 CRISPR screens.
DR ChiTaRS; STX3; human.
DR GeneWiki; Syntaxin_3; -.
DR GenomeRNAi; 6809; -.
DR Pharos; Q13277; Tbio.
DR PRO; PR:Q13277; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q13277; Protein.
DR Bgee; ENSG00000166900; Expressed in rectum and 179 other cell types or tissues.
DR ExpressionAtlas; Q13277; baseline and differential.
DR Genevisible; Q13277; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:HGNC-UCL.
DR GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0030426; C:growth cone; ISS:HGNC-UCL.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; ISS:HGNC-UCL.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR GO; GO:0048787; C:presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0031201; C:SNARE complex; ISS:HGNC-UCL.
DR GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; TAS:HGNC-UCL.
DR GO; GO:0042589; C:zymogen granule membrane; IEA:Ensembl.
DR GO; GO:0050544; F:arachidonic acid binding; ISS:HGNC-UCL.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; ISS:HGNC-UCL.
DR GO; GO:0090174; P:organelle membrane fusion; IMP:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IMP:UniProtKB.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IMP:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR CDD; cd15881; SNARE_syntaxin3; 1.
DR CDD; cd00179; SynN; 1.
DR Gene3D; 1.20.5.110; -; 1.
DR Gene3D; 1.20.58.70; -; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR031186; STX3_SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; SYNTAXIN; 1.
DR PANTHER; PTHR19957:SF34; SYNTAXIN-3; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF00804; Syntaxin; 1.
DR SMART; SM00503; SynN; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; t-snare proteins; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil; Disease variant;
KW Membrane; Neurotransmitter transport; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..289
FT /note="Syntaxin-3"
FT /id="PRO_0000210199"
FT TOPO_DOM 1..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..289
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 191..253
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT COILED 32..111
FT /evidence="ECO:0000255"
FT VAR_SEQ 226..262
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10080545"
FT /id="VSP_006340"
FT VAR_SEQ 266..289
FT /note="IIIVLVVVLLGILALIIGLSVGLN -> SLQTGVATLVFR (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:29475951"
FT /id="VSP_043187"
FT VARIANT 41
FT /note="E -> G (found in a patient with congenital cataract
FT and developmental delay; uncertain significance;
FT dbSNP:rs797045154)"
FT /evidence="ECO:0000269|PubMed:25358429"
FT /id="VAR_086135"
FT VARIANT 83
FT /note="E -> D (in dbSNP:rs12282741)"
FT /id="VAR_028189"
FT VARIANT 247..289
FT /note="Missing (in DIAR12; loss of expression)"
FT /evidence="ECO:0000269|PubMed:24726755,
FT ECO:0000269|PubMed:33974130"
FT /id="VAR_086136"
FT VARIANT 276
FT /note="G -> S (in dbSNP:rs34563654)"
FT /id="VAR_052246"
FT VARIANT 285
FT /note="S -> P (in dbSNP:rs34753750)"
FT /id="VAR_052247"
FT CONFLICT 2..11
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="T -> S (in Ref. 2; CAA62209)"
FT /evidence="ECO:0000305"
FT CONFLICT 152..153
FT /note="QL -> HV (in Ref. 1; AAA75303)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="T -> S (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 33155 MW; 0E12EBC7CBEDB81E CRC64;
MKDRLEQLKA KQLTQDDDTD AVEIAIDNTA FMDEFFSEIE ETRLNIDKIS EHVEEAKKLY
SIILSAPIPE PKTKDDLEQL TTEIKKRANN VRNKLKSMEK HIEEDEVRSS ADLRIRKSQH
SVLSRKFVEV MTKYNEAQVD FRERSKGRIQ RQLEITGKKT TDEELEEMLE SGNPAIFTSG
IIDSQISKQA LSEIEGRHKD IVRLESSIKE LHDMFMDIAM LVENQGEMLD NIELNVMHTV
DHVEKARDET KKAVKYQSQA RKKLIIIIVL VVVLLGILAL IIGLSVGLN
//
