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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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. DR Genevisible; Q13277; HS. 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 //