Full text data of STX4
STX4
(STX4A)
[Confidence: high (present in two of the MS resources)]
Syntaxin-4 (Renal carcinoma antigen NY-REN-31)
Syntaxin-4 (Renal carcinoma antigen NY-REN-31)
hRBCD
IPI00029730
IPI00029730 Syntaxin 4 Syntaxin 4 membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a 1 n/a n/a 1 n/a 1 n/a n/a n/a n/a Type IV membrane protein NILSSADYVER, CNSMQSEYR, LGSPDEEFFHK found at its expected molecular weight found at molecular weight
IPI00029730 Syntaxin 4 Syntaxin 4 membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a 1 n/a n/a 1 n/a 1 n/a n/a n/a n/a Type IV membrane protein NILSSADYVER, CNSMQSEYR, LGSPDEEFFHK found at its expected molecular weight found at molecular weight
UniProt
Q12846
ID STX4_HUMAN Reviewed; 297 AA.
AC Q12846; Q15525; Q6FHE8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JUL-1998, sequence version 2.
DT 22-JAN-2014, entry version 132.
DE RecName: Full=Syntaxin-4;
DE AltName: Full=Renal carcinoma antigen NY-REN-31;
GN Name=STX4; Synonyms=STX4A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=8206394; DOI=10.1016/0378-1119(94)90117-1;
RA Li H., Hodge D.R., Pei G.K., Seth A.;
RT "Isolation and sequence analysis of the human syntaxin-encoding
RT gene.";
RL Gene 143:303-304(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=8760387;
RA Jagadish M.N., Fernandez C.S., Hewish D.R., Macaulay S.L., Gough K.H.,
RA Grusovin J., Verkuylen A., Cosgrove L., Alafaci A., Frenkel M.J.,
RA Ward C.W.;
RT "Insulin-responsive tissues contain the core complex protein SNAP-25
RT (synaptosomal-associated protein 25) A and B isoforms in addition to
RT syntaxin 4 and synaptobrevins 1 and 2.";
RL Biochem. J. 317:945-954(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Peripheral blood neutrophil;
RX PubMed=10080545;
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
RT syntaxin 1.";
RL J. Leukoc. Biol. 65:397-406(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens epithelium;
RA Rae J.L., Shepard A.R.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang Z., Loh E., Low S.H., Li X., Miura M., An F., Weimbs T.;
RT "Expression of syntaxins in kidney MDCK cells.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-
RT cell carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-15 AND SER-117,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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.,
RA Buerckstuemmer T., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-15, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Plasma membrane t-SNARE that mediates docking of
CC transport vesicles. Necessary for the translocation of SLC2A4 from
CC intracellular vesicles to the plasma membrane. Together with STXB3
CC and VAMP2, may also play a role in docking/fusion of intracellular
CC GLUT4-containing vesicles with the cell surface in adipocytes (By
CC similarity). May also play a role in docking of synaptic vesicles
CC at presynaptic active zones.
CC -!- SUBUNIT: Component of the SNARE complex composed of STX4, SNAP23
CC and VAMP7 that interacts with SYT7 during lysosomal exocytosis.
CC Found in a complex with VAMP8 and SNAP23. Detected in a complex
CC with SNAP23 and STXBP4. Interacts with VAMP2. Interacts with
CC SNAP23 and SNAPIN. Interacts with LLGL1. Interacts (via C-
CC terminus) with CENPF. Interacts with DOC2B. Interacts with STXBP6.
CC Interacts with STXBP3; excludes interaction with DOC2B and SNAP25.
CC Interacts with STXBP4; excludes interaction with VAMP2 (By
CC similarity).
CC -!- INTERACTION:
CC P54920:NAPA; NbExp=2; IntAct=EBI-744942, EBI-749652;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type IV membrane
CC protein (Potential).
CC -!- TISSUE SPECIFICITY: Expressed in neutrophils and neutrophil-
CC differentiated HL-60 cells. Expression in neutrophils increases
CC with differentiation.
CC -!- SIMILARITY: Belongs to the syntaxin family.
CC -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U07158; AAA20967.1; -; mRNA.
DR EMBL; X85784; CAA59769.1; -; mRNA.
DR EMBL; AJ000541; CAA04174.1; -; mRNA.
DR EMBL; AF026007; AAB88810.1; -; mRNA.
DR EMBL; AF318489; AAG40313.1; -; Transcribed_RNA.
DR EMBL; BT007326; AAP35990.1; -; mRNA.
DR EMBL; CR541806; CAG46605.1; -; mRNA.
DR EMBL; AK315716; BAG38075.1; -; mRNA.
DR EMBL; CH471192; EAW52176.1; -; Genomic_DNA.
DR EMBL; BC002436; AAH02436.1; -; mRNA.
DR PIR; I38517; I38517.
DR PIR; S52726; S52726.
DR RefSeq; NP_004595.2; NM_004604.4.
DR UniGene; Hs.83734; -.
DR ProteinModelPortal; Q12846; -.
DR SMR; Q12846; 39-292.
DR IntAct; Q12846; 11.
DR MINT; MINT-1454763; -.
DR STRING; 9606.ENSP00000317714; -.
DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
DR PhosphoSite; Q12846; -.
DR DMDM; 3041737; -.
DR OGP; Q12846; -.
DR PaxDb; Q12846; -.
DR PRIDE; Q12846; -.
DR DNASU; 6810; -.
DR Ensembl; ENST00000313843; ENSP00000317714; ENSG00000103496.
DR GeneID; 6810; -.
DR KEGG; hsa:6810; -.
DR UCSC; uc002eal.4; human.
DR CTD; 6810; -.
DR GeneCards; GC16P031044; -.
DR HGNC; HGNC:11439; STX4.
DR HPA; HPA001330; -.
DR MIM; 186591; gene.
DR neXtProt; NX_Q12846; -.
DR PharmGKB; PA36236; -.
DR eggNOG; COG5074; -.
DR HOGENOM; HOG000286023; -.
DR HOVERGEN; HBG000497; -.
DR InParanoid; Q12846; -.
DR KO; K13502; -.
DR OMA; LMQSEYR; -.
DR PhylomeDB; Q12846; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; STX4; human.
DR GeneWiki; STX4; -.
DR GenomeRNAi; 6810; -.
DR NextBio; 26573; -.
DR PRO; PR:Q12846; -.
DR ArrayExpress; Q12846; -.
DR Bgee; Q12846; -.
DR CleanEx; HS_STX4; -.
DR Genevestigator; Q12846; -.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:HGNC.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0043219; C:lateral loop; IEA:Ensembl.
DR GO; GO:0035749; C:myelin sheath adaxonal region; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0005773; C:vacuole; TAS:HGNC.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR010989; t-SNARE.
DR InterPro; IPR000727; T_SNARE_dom.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF00804; Syntaxin; 1.
DR SMART; SM00503; SynN; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Complete proteome; Membrane;
KW Neurotransmitter transport; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 297 Syntaxin-4.
FT /FTId=PRO_0000210202.
FT TOPO_DOM 1 275 Cytoplasmic (Potential).
FT TRANSMEM 276 296 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT TOPO_DOM 297 297 Extracellular (Potential).
FT DOMAIN 200 262 t-SNARE coiled-coil homology.
FT REGION 154 297 Interaction with CENPF (By similarity).
FT COILED 43 163 Potential.
FT MOD_RES 14 14 Phosphoserine.
FT MOD_RES 15 15 Phosphoserine.
FT MOD_RES 117 117 Phosphoserine.
FT MOD_RES 248 248 Phosphoserine (By similarity).
FT CONFLICT 174 174 E -> D (in Ref. 1; AAA20967).
FT CONFLICT 269 269 A -> V (in Ref. 1; AAA20967).
SQ SEQUENCE 297 AA; 34180 MW; 5084FD1C49A86BAA CRC64;
MRDRTHELRQ GDDSSDEEDK ERVALVVHPG TARLGSPDEE FFHKVRTIRQ TIVKLGNKVQ
ELEKQQVTIL ATPLPEESMK QELQNLRDEI KQLGREIRLQ LKAIEPQKEE ADENYNSVNT
RMRKTQHGVL SQQFVELINK CNSMQSEYRE KNVERIRRQL KITNAGMVSD EELEQMLDSG
QSEVFVSNIL KDTQVTRQAL NEISARHSEI QQLERSIREL HDIFTFLATE VEMQGEMINR
IEKNILSSAD YVERGQEHVK TALENQKKAR KKKVLIAICV SITVVLLAVI IGVTVVG
//
ID STX4_HUMAN Reviewed; 297 AA.
AC Q12846; Q15525; Q6FHE8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JUL-1998, sequence version 2.
DT 22-JAN-2014, entry version 132.
DE RecName: Full=Syntaxin-4;
DE AltName: Full=Renal carcinoma antigen NY-REN-31;
GN Name=STX4; Synonyms=STX4A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=8206394; DOI=10.1016/0378-1119(94)90117-1;
RA Li H., Hodge D.R., Pei G.K., Seth A.;
RT "Isolation and sequence analysis of the human syntaxin-encoding
RT gene.";
RL Gene 143:303-304(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=8760387;
RA Jagadish M.N., Fernandez C.S., Hewish D.R., Macaulay S.L., Gough K.H.,
RA Grusovin J., Verkuylen A., Cosgrove L., Alafaci A., Frenkel M.J.,
RA Ward C.W.;
RT "Insulin-responsive tissues contain the core complex protein SNAP-25
RT (synaptosomal-associated protein 25) A and B isoforms in addition to
RT syntaxin 4 and synaptobrevins 1 and 2.";
RL Biochem. J. 317:945-954(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Peripheral blood neutrophil;
RX PubMed=10080545;
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
RT syntaxin 1.";
RL J. Leukoc. Biol. 65:397-406(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens epithelium;
RA Rae J.L., Shepard A.R.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang Z., Loh E., Low S.H., Li X., Miura M., An F., Weimbs T.;
RT "Expression of syntaxins in kidney MDCK cells.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-
RT cell carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-15 AND SER-117,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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.,
RA Buerckstuemmer T., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-15, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Plasma membrane t-SNARE that mediates docking of
CC transport vesicles. Necessary for the translocation of SLC2A4 from
CC intracellular vesicles to the plasma membrane. Together with STXB3
CC and VAMP2, may also play a role in docking/fusion of intracellular
CC GLUT4-containing vesicles with the cell surface in adipocytes (By
CC similarity). May also play a role in docking of synaptic vesicles
CC at presynaptic active zones.
CC -!- SUBUNIT: Component of the SNARE complex composed of STX4, SNAP23
CC and VAMP7 that interacts with SYT7 during lysosomal exocytosis.
CC Found in a complex with VAMP8 and SNAP23. Detected in a complex
CC with SNAP23 and STXBP4. Interacts with VAMP2. Interacts with
CC SNAP23 and SNAPIN. Interacts with LLGL1. Interacts (via C-
CC terminus) with CENPF. Interacts with DOC2B. Interacts with STXBP6.
CC Interacts with STXBP3; excludes interaction with DOC2B and SNAP25.
CC Interacts with STXBP4; excludes interaction with VAMP2 (By
CC similarity).
CC -!- INTERACTION:
CC P54920:NAPA; NbExp=2; IntAct=EBI-744942, EBI-749652;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type IV membrane
CC protein (Potential).
CC -!- TISSUE SPECIFICITY: Expressed in neutrophils and neutrophil-
CC differentiated HL-60 cells. Expression in neutrophils increases
CC with differentiation.
CC -!- SIMILARITY: Belongs to the syntaxin family.
CC -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U07158; AAA20967.1; -; mRNA.
DR EMBL; X85784; CAA59769.1; -; mRNA.
DR EMBL; AJ000541; CAA04174.1; -; mRNA.
DR EMBL; AF026007; AAB88810.1; -; mRNA.
DR EMBL; AF318489; AAG40313.1; -; Transcribed_RNA.
DR EMBL; BT007326; AAP35990.1; -; mRNA.
DR EMBL; CR541806; CAG46605.1; -; mRNA.
DR EMBL; AK315716; BAG38075.1; -; mRNA.
DR EMBL; CH471192; EAW52176.1; -; Genomic_DNA.
DR EMBL; BC002436; AAH02436.1; -; mRNA.
DR PIR; I38517; I38517.
DR PIR; S52726; S52726.
DR RefSeq; NP_004595.2; NM_004604.4.
DR UniGene; Hs.83734; -.
DR ProteinModelPortal; Q12846; -.
DR SMR; Q12846; 39-292.
DR IntAct; Q12846; 11.
DR MINT; MINT-1454763; -.
DR STRING; 9606.ENSP00000317714; -.
DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
DR PhosphoSite; Q12846; -.
DR DMDM; 3041737; -.
DR OGP; Q12846; -.
DR PaxDb; Q12846; -.
DR PRIDE; Q12846; -.
DR DNASU; 6810; -.
DR Ensembl; ENST00000313843; ENSP00000317714; ENSG00000103496.
DR GeneID; 6810; -.
DR KEGG; hsa:6810; -.
DR UCSC; uc002eal.4; human.
DR CTD; 6810; -.
DR GeneCards; GC16P031044; -.
DR HGNC; HGNC:11439; STX4.
DR HPA; HPA001330; -.
DR MIM; 186591; gene.
DR neXtProt; NX_Q12846; -.
DR PharmGKB; PA36236; -.
DR eggNOG; COG5074; -.
DR HOGENOM; HOG000286023; -.
DR HOVERGEN; HBG000497; -.
DR InParanoid; Q12846; -.
DR KO; K13502; -.
DR OMA; LMQSEYR; -.
DR PhylomeDB; Q12846; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; STX4; human.
DR GeneWiki; STX4; -.
DR GenomeRNAi; 6810; -.
DR NextBio; 26573; -.
DR PRO; PR:Q12846; -.
DR ArrayExpress; Q12846; -.
DR Bgee; Q12846; -.
DR CleanEx; HS_STX4; -.
DR Genevestigator; Q12846; -.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:HGNC.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0043219; C:lateral loop; IEA:Ensembl.
DR GO; GO:0035749; C:myelin sheath adaxonal region; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0005773; C:vacuole; TAS:HGNC.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR010989; t-SNARE.
DR InterPro; IPR000727; T_SNARE_dom.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF00804; Syntaxin; 1.
DR SMART; SM00503; SynN; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Complete proteome; Membrane;
KW Neurotransmitter transport; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 297 Syntaxin-4.
FT /FTId=PRO_0000210202.
FT TOPO_DOM 1 275 Cytoplasmic (Potential).
FT TRANSMEM 276 296 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT TOPO_DOM 297 297 Extracellular (Potential).
FT DOMAIN 200 262 t-SNARE coiled-coil homology.
FT REGION 154 297 Interaction with CENPF (By similarity).
FT COILED 43 163 Potential.
FT MOD_RES 14 14 Phosphoserine.
FT MOD_RES 15 15 Phosphoserine.
FT MOD_RES 117 117 Phosphoserine.
FT MOD_RES 248 248 Phosphoserine (By similarity).
FT CONFLICT 174 174 E -> D (in Ref. 1; AAA20967).
FT CONFLICT 269 269 A -> V (in Ref. 1; AAA20967).
SQ SEQUENCE 297 AA; 34180 MW; 5084FD1C49A86BAA CRC64;
MRDRTHELRQ GDDSSDEEDK ERVALVVHPG TARLGSPDEE FFHKVRTIRQ TIVKLGNKVQ
ELEKQQVTIL ATPLPEESMK QELQNLRDEI KQLGREIRLQ LKAIEPQKEE ADENYNSVNT
RMRKTQHGVL SQQFVELINK CNSMQSEYRE KNVERIRRQL KITNAGMVSD EELEQMLDSG
QSEVFVSNIL KDTQVTRQAL NEISARHSEI QQLERSIREL HDIFTFLATE VEMQGEMINR
IEKNILSSAD YVERGQEHVK TALENQKKAR KKKVLIAICV SITVVLLAVI IGVTVVG
//
MIM
186591
*RECORD*
*FIELD* NO
186591
*FIELD* TI
*186591 SYNTAXIN 4; STX4
;;STX4A;;
SYNTAXIN, PLACENTAL;;
p35-2
*FIELD* TX
CLONING
read more
Li et al. (1994) described the nucleotide sequence of STX4A, a syntaxin
gene isolated from a placenta library. (The gene was previously
symbolized STX2.) It encodes a predicted 297-amino acid protein that is
89% identical to the amino acid sequence of rat Stx4a.
By immunohistochemical analysis of rat brain sections, Kennedy et al.
(2010) showed that Stx4 was expressed throughout brain. In rat
hippocampal neurons, Stx4 showed a punctate distribution in the
somatodendritic compartment, and Stx4 clusters often localized to
dendritic spines. Immunogold electron microscopy of CA1 rat hippocampus
revealed frequent Stx4 labeling near spine membranes at sites lateral to
postsynaptic densities, with occasional labeling of presynaptic
membranes. Biochemical fractionation of mouse brain revealed Stx4 in
synaptosome fractions, but not in synaptic vesicle fractions.
GENE FUNCTION
Mandon et al. (1996) stated that vesicle-associated membrane proteins
(VAMPs) or synaptobrevins (see 185880) are proposed to bind to cognate
vesicle-targeting receptors in target membranes, which include several
members of the syntaxin family. The molecular mechanisms responsible for
targeting of vesicles containing aquaporin-2 (AQP2; 107777) to the
apical plasma membrane of renal collecting duct cells may involve the
vesicle-targeting protein STX4. Among the known syntaxin isoforms, only
STX1 (STX1A; 186590) and STX4 bind VAMP2 (185881) with high affinity.
Thus, STX1 and STX4 could be considered candidates for a role in
targeting of the AQP2/VAMP2-containing vesicles to the apical plasma
membrane in collecting duct cells. In contrast to STX1, which is
expressed predominantly in the central nervous system, STX4 is expressed
in a variety of tissues including the kidney. Mandon et al. (1996) used
sequence data for rat Stx1a, Stx1b (601485), and Stx4 from Bennett et
al. (1993) to design PCR primers for RT-PCR analysis of rat tissues.
They detected Stx4 mRNA in the apical plasma membrane of collecting duct
principal cells. They also demonstrated in the rat kidney the presence
of a protein with the characteristics of Stx4 in the apical plasma
membrane of inner medullary-collecting duct cells.
To clarify the physiologic function of STXBP3 (608339) in
insulin-stimulated GLUT4 (SLC2A4; 138190) exocytosis, Kanda et al.
(2005) generated mouse embryos deficient in the Stx4-binding protein
Stxbp3 and developed Stxbp3 -/- adipocytes from their mesenchymal
fibroblasts. The insulin-induced appearance of Glut4 at the cell surface
was enhanced in Stxbp3 -/- adipocytes compared to +/+ cells. Wortmannin,
an inhibitor of PI3K, inhibited insulin-stimulated Glut4 externalization
in +/+ but not -/- adipocytes. Kanda et al. (2005) suggested that
disruption of the interaction between STX4 and STXBP3 in adipocytes
might result in enhancement of insulin-stimulated GLUT4 externalization.
Using RT-PCR, immunoblot analysis, and immunofluorescence microscopy,
Sander et al. (2008) demonstrated that human intestinal mast cells (MCs)
expressed SNAP23 (602534), STX1B, STX2 (132350), STX3 (STX3A; 600876),
STX4, and STX6 (603944), but not SNAP25 (600322). MCs also expressed
VAMP3 (603657), VAMP7 (300053), and VAMP8 (603177), but, in contrast
with rodent MCs, they expressed only low levels of VAMP2 (185881). VAMP7
and VAMP8 translocated to the plasma membrane and interacted with SNAP23
and STX4 upon activation. Inhibition of STX4, SNAP23, VAMP7, or VAMP8,
but not VAMP2 or VAMP3, resulted in markedly reduced high-affinity IgE
receptor-mediated histamine release. Sander et al. (2008) concluded that
human MCs express a specific pattern of SNAREs and that VAMP7 and VAMP8,
but not VAMP2, are required for rapid degranulation.
Using rat hippocampal neurons, Kennedy et al. (2010) showed that
exocytosis of recycling endosomes at dendritic spines occurred at
Stx4-enriched sites immediately lateral to postsynaptic densities.
Disruption of Stx4 either acutely or chronically blocked membrane fusion
and cargo delivery triggered by synaptic activation, and acute
inhibition of Stx4 abolished long-term potentiation. Kennedy et al.
(2010) concluded that STX4 is a central component of the SNARE machinery
that mediates rapid, activity-dependent fusion of recycling endosomes in
dendritic spines.
*FIELD* RF
1. Bennett, M. K.; Garcia-Arraras, J. E.; Elferink, L. A.; Peterson,
K.; Fleming, A. M.; Hazuka, C. D.; Scheller, R. H.: The syntaxin
family of vesicular transport receptors. Cell 74: 863-873, 1993.
2. Kanda, H.; Tamori, Y.; Shinoda, H.; Yoshikawa, M.; Sakaue, M.;
Udagawa, J.; Otani, H.; Tashiro, F.; Miyazaki, J.; Kasuga, M.: Adipocytes
from Munc18c-null mice show increased sensitivity to insulin-stimulated
GLUT4 externalization. J. Clin. Invest. 115: 291-301, 2005.
3. Kennedy, M. J.; Davison, I. G.; Robinson, C. G.; Ehlers, M. D.
: Syntaxin-4 defines a domain for activity-dependent exocytosis in
dendritic spines. Cell 141: 524-535, 2010.
4. Li, H.; Hodge, D. R.; Pei, G. K.; Seth, A.: Isolation and sequence
analysis of the human syntaxin-encoding gene. Gene 143: 303-304,
1994.
5. Mandon, B.; Chou, C.-L.; Nielsen, S.; Knepper, M. A.: Syntaxin-4
is localized to the apical plasma membrane of rat renal collecting
duct cells: possible role in aquaporin-2 trafficking. J. Clin. Invest. 98:
906-913, 1996.
6. Sander, L. E.; Frank, S. P. C.; Bolat, S.; Blank, U.; Galli, T.;
Bigalke, H.; Bischoff, S. C.; Lorentz, A.: Vesicle associated membrane
protein (VAMP)-7 and VAMP-8, but not VAMP-2 or VAMP-3, are required
for activation-induced degranulation of mature human mast cells. Europ.
J. Immun. 38: 855-863, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 12/20/2010
Paul J. Converse - updated: 10/9/2009
Marla J. F. O'Neill - updated: 4/12/2005
Mark H. Paalman - updated: 10/25/1996
Alan F. Scott - updated: 9/20/1995
*FIELD* CD
Victor A. McKusick: 9/10/1992
*FIELD* ED
mgross: 01/03/2011
terry: 12/20/2010
mgross: 10/12/2009
mgross: 10/9/2009
tkritzer: 4/12/2005
psherman: 10/27/1998
mark: 10/25/1996
carol: 9/10/1992
*RECORD*
*FIELD* NO
186591
*FIELD* TI
*186591 SYNTAXIN 4; STX4
;;STX4A;;
SYNTAXIN, PLACENTAL;;
p35-2
*FIELD* TX
CLONING
read more
Li et al. (1994) described the nucleotide sequence of STX4A, a syntaxin
gene isolated from a placenta library. (The gene was previously
symbolized STX2.) It encodes a predicted 297-amino acid protein that is
89% identical to the amino acid sequence of rat Stx4a.
By immunohistochemical analysis of rat brain sections, Kennedy et al.
(2010) showed that Stx4 was expressed throughout brain. In rat
hippocampal neurons, Stx4 showed a punctate distribution in the
somatodendritic compartment, and Stx4 clusters often localized to
dendritic spines. Immunogold electron microscopy of CA1 rat hippocampus
revealed frequent Stx4 labeling near spine membranes at sites lateral to
postsynaptic densities, with occasional labeling of presynaptic
membranes. Biochemical fractionation of mouse brain revealed Stx4 in
synaptosome fractions, but not in synaptic vesicle fractions.
GENE FUNCTION
Mandon et al. (1996) stated that vesicle-associated membrane proteins
(VAMPs) or synaptobrevins (see 185880) are proposed to bind to cognate
vesicle-targeting receptors in target membranes, which include several
members of the syntaxin family. The molecular mechanisms responsible for
targeting of vesicles containing aquaporin-2 (AQP2; 107777) to the
apical plasma membrane of renal collecting duct cells may involve the
vesicle-targeting protein STX4. Among the known syntaxin isoforms, only
STX1 (STX1A; 186590) and STX4 bind VAMP2 (185881) with high affinity.
Thus, STX1 and STX4 could be considered candidates for a role in
targeting of the AQP2/VAMP2-containing vesicles to the apical plasma
membrane in collecting duct cells. In contrast to STX1, which is
expressed predominantly in the central nervous system, STX4 is expressed
in a variety of tissues including the kidney. Mandon et al. (1996) used
sequence data for rat Stx1a, Stx1b (601485), and Stx4 from Bennett et
al. (1993) to design PCR primers for RT-PCR analysis of rat tissues.
They detected Stx4 mRNA in the apical plasma membrane of collecting duct
principal cells. They also demonstrated in the rat kidney the presence
of a protein with the characteristics of Stx4 in the apical plasma
membrane of inner medullary-collecting duct cells.
To clarify the physiologic function of STXBP3 (608339) in
insulin-stimulated GLUT4 (SLC2A4; 138190) exocytosis, Kanda et al.
(2005) generated mouse embryos deficient in the Stx4-binding protein
Stxbp3 and developed Stxbp3 -/- adipocytes from their mesenchymal
fibroblasts. The insulin-induced appearance of Glut4 at the cell surface
was enhanced in Stxbp3 -/- adipocytes compared to +/+ cells. Wortmannin,
an inhibitor of PI3K, inhibited insulin-stimulated Glut4 externalization
in +/+ but not -/- adipocytes. Kanda et al. (2005) suggested that
disruption of the interaction between STX4 and STXBP3 in adipocytes
might result in enhancement of insulin-stimulated GLUT4 externalization.
Using RT-PCR, immunoblot analysis, and immunofluorescence microscopy,
Sander et al. (2008) demonstrated that human intestinal mast cells (MCs)
expressed SNAP23 (602534), STX1B, STX2 (132350), STX3 (STX3A; 600876),
STX4, and STX6 (603944), but not SNAP25 (600322). MCs also expressed
VAMP3 (603657), VAMP7 (300053), and VAMP8 (603177), but, in contrast
with rodent MCs, they expressed only low levels of VAMP2 (185881). VAMP7
and VAMP8 translocated to the plasma membrane and interacted with SNAP23
and STX4 upon activation. Inhibition of STX4, SNAP23, VAMP7, or VAMP8,
but not VAMP2 or VAMP3, resulted in markedly reduced high-affinity IgE
receptor-mediated histamine release. Sander et al. (2008) concluded that
human MCs express a specific pattern of SNAREs and that VAMP7 and VAMP8,
but not VAMP2, are required for rapid degranulation.
Using rat hippocampal neurons, Kennedy et al. (2010) showed that
exocytosis of recycling endosomes at dendritic spines occurred at
Stx4-enriched sites immediately lateral to postsynaptic densities.
Disruption of Stx4 either acutely or chronically blocked membrane fusion
and cargo delivery triggered by synaptic activation, and acute
inhibition of Stx4 abolished long-term potentiation. Kennedy et al.
(2010) concluded that STX4 is a central component of the SNARE machinery
that mediates rapid, activity-dependent fusion of recycling endosomes in
dendritic spines.
*FIELD* RF
1. Bennett, M. K.; Garcia-Arraras, J. E.; Elferink, L. A.; Peterson,
K.; Fleming, A. M.; Hazuka, C. D.; Scheller, R. H.: The syntaxin
family of vesicular transport receptors. Cell 74: 863-873, 1993.
2. Kanda, H.; Tamori, Y.; Shinoda, H.; Yoshikawa, M.; Sakaue, M.;
Udagawa, J.; Otani, H.; Tashiro, F.; Miyazaki, J.; Kasuga, M.: Adipocytes
from Munc18c-null mice show increased sensitivity to insulin-stimulated
GLUT4 externalization. J. Clin. Invest. 115: 291-301, 2005.
3. Kennedy, M. J.; Davison, I. G.; Robinson, C. G.; Ehlers, M. D.
: Syntaxin-4 defines a domain for activity-dependent exocytosis in
dendritic spines. Cell 141: 524-535, 2010.
4. Li, H.; Hodge, D. R.; Pei, G. K.; Seth, A.: Isolation and sequence
analysis of the human syntaxin-encoding gene. Gene 143: 303-304,
1994.
5. Mandon, B.; Chou, C.-L.; Nielsen, S.; Knepper, M. A.: Syntaxin-4
is localized to the apical plasma membrane of rat renal collecting
duct cells: possible role in aquaporin-2 trafficking. J. Clin. Invest. 98:
906-913, 1996.
6. Sander, L. E.; Frank, S. P. C.; Bolat, S.; Blank, U.; Galli, T.;
Bigalke, H.; Bischoff, S. C.; Lorentz, A.: Vesicle associated membrane
protein (VAMP)-7 and VAMP-8, but not VAMP-2 or VAMP-3, are required
for activation-induced degranulation of mature human mast cells. Europ.
J. Immun. 38: 855-863, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 12/20/2010
Paul J. Converse - updated: 10/9/2009
Marla J. F. O'Neill - updated: 4/12/2005
Mark H. Paalman - updated: 10/25/1996
Alan F. Scott - updated: 9/20/1995
*FIELD* CD
Victor A. McKusick: 9/10/1992
*FIELD* ED
mgross: 01/03/2011
terry: 12/20/2010
mgross: 10/12/2009
mgross: 10/9/2009
tkritzer: 4/12/2005
psherman: 10/27/1998
mark: 10/25/1996
carol: 9/10/1992