Full text data of STX2
STX2
(EPIM, STX2A, STX2B, STX2C)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Syntaxin-2 (Epimorphin)
Syntaxin-2 (Epimorphin)
UniProt
P32856
ID STX2_HUMAN Reviewed; 288 AA.
AC P32856; Q86VW8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-MAR-2010, sequence version 3.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Syntaxin-2;
DE AltName: Full=Epimorphin;
GN Name=STX2; Synonyms=EPIM, STX2A, STX2B, STX2C;
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] (ISOFORMS 1; 2 AND 3).
RX PubMed=8466509; DOI=10.1006/bbrc.1993.1363;
RA Hirai Y.;
RT "Molecular cloning of human epimorphin: identification of isoforms and
RT their unique properties.";
RL Biochem. Biophys. Res. Commun. 191:1332-1337(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Essential for epithelial morphogenesis. May mediate
CC Ca(2+)-regulation of exocytosis acrosomal reaction in sperm.
CC -!- SUBUNIT: Interacts with SYT6 and SYT8; the interaction is Ca(2+)-
CC dependent (By similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist;
CC Name=3;
CC IsoId=P32856-1; Sequence=Displayed;
CC Name=1;
CC IsoId=P32856-2; Sequence=VSP_006334;
CC Name=2;
CC IsoId=P32856-3; Sequence=VSP_006335;
CC -!- SIMILARITY: Belongs to the syntaxin family.
CC -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA03436.1; Type=Frameshift; Positions=Several;
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; D14582; BAA03436.1; ALT_FRAME; mRNA.
DR EMBL; AC073912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047496; AAH47496.1; -; mRNA.
DR PIR; JN0466; JN0466.
DR RefSeq; NP_001971.2; NM_001980.3.
DR RefSeq; NP_919337.1; NM_194356.2.
DR RefSeq; XP_005253613.1; XM_005253556.1.
DR UniGene; Hs.437585; -.
DR ProteinModelPortal; P32856; -.
DR SMR; P32856; 26-149, 188-283.
DR STRING; 9606.ENSP00000342554; -.
DR PhosphoSite; P32856; -.
DR DMDM; 292495060; -.
DR PaxDb; P32856; -.
DR PRIDE; P32856; -.
DR Ensembl; ENST00000261653; ENSP00000261653; ENSG00000111450.
DR Ensembl; ENST00000392373; ENSP00000376178; ENSG00000111450.
DR GeneID; 2054; -.
DR KEGG; hsa:2054; -.
DR UCSC; uc001uio.4; human.
DR CTD; 2054; -.
DR GeneCards; GC12M131274; -.
DR HGNC; HGNC:3403; STX2.
DR HPA; CAB022658; -.
DR MIM; 132350; gene.
DR neXtProt; NX_P32856; -.
DR PharmGKB; PA27831; -.
DR eggNOG; COG5074; -.
DR HOGENOM; HOG000286023; -.
DR HOVERGEN; HBG000497; -.
DR InParanoid; P32856; -.
DR KO; K08486; -.
DR OMA; DLTACRK; -.
DR OrthoDB; EOG7X9G7R; -.
DR PhylomeDB; P32856; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13685; Neuronal System.
DR ChiTaRS; STX2; human.
DR GeneWiki; STX2; -.
DR GenomeRNAi; 2054; -.
DR NextBio; 8351; -.
DR PRO; PR:P32856; -.
DR Bgee; P32856; -.
DR CleanEx; HS_STX2; -.
DR Genevestigator; P32856; -.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:HGNC.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; TAS:ProtInc.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISS:HGNC.
DR GO; GO:0007340; P:acrosome reaction; ISS:HGNC.
DR GO; GO:0030154; P:cell differentiation; IEA:Ensembl.
DR GO; GO:0007398; P:ectoderm development; TAS:ProtInc.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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 Alternative splicing; Coiled coil; Complete proteome; Membrane;
KW Polymorphism; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 288 Syntaxin-2.
FT /FTId=PRO_0000210196.
FT TOPO_DOM 1 264 Cytoplasmic (Potential).
FT TRANSMEM 265 288 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT DOMAIN 191 253 t-SNARE coiled-coil homology.
FT COILED 35 101 Potential.
FT VAR_SEQ 263 288 KKWIIIAVSVVLVAIIALIIGLSVGK -> QQHCHSNHIPR
FT AIYP (in isoform 2).
FT /FTId=VSP_006335.
FT VAR_SEQ 264 288 KWIIIAVSVVLVAIIALIIGLSVGK -> LMFIIICVIVLL
FT VILGIILATTLS (in isoform 1).
FT /FTId=VSP_006334.
FT VARIANT 42 42 S -> T (in dbSNP:rs6486602).
FT /FTId=VAR_014850.
FT VARIANT 54 54 K -> R (in dbSNP:rs7301926).
FT /FTId=VAR_057259.
FT CONFLICT 89 89 R -> A (in Ref. 1; BAA03436).
FT CONFLICT 276 276 A -> V (in Ref. 1; BAA03436).
FT CONFLICT 288 288 K -> I (in Ref. 1; BAA03436).
SQ SEQUENCE 288 AA; 33341 MW; 5668E6BF891360B4 CRC64;
MRDRLPDLTA CRKNDDGDTV VVVEKDHFMD DFFHQVEEIR NSIDKITQYV EEVKKNHSII
LSAPNPEGKI KEELEDLNKE IKKTANKIRA KLKAIEQSFD QDESGNRTSV DLRIRRTQHS
VLSRKFVEAM AEYNEAQTLF RERSKGRIQR QLEITGRTTT DDELEEMLES GKPSIFTSDI
ISDSQITRQA LNEIESRHKD IMKLETSIRE LHEMFMDMAM FVETQGEMIN NIERNVMNAT
DYVEHAKEET KKAIKYQSKA RRKKWIIIAV SVVLVAIIAL IIGLSVGK
//
ID STX2_HUMAN Reviewed; 288 AA.
AC P32856; Q86VW8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-MAR-2010, sequence version 3.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Syntaxin-2;
DE AltName: Full=Epimorphin;
GN Name=STX2; Synonyms=EPIM, STX2A, STX2B, STX2C;
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] (ISOFORMS 1; 2 AND 3).
RX PubMed=8466509; DOI=10.1006/bbrc.1993.1363;
RA Hirai Y.;
RT "Molecular cloning of human epimorphin: identification of isoforms and
RT their unique properties.";
RL Biochem. Biophys. Res. Commun. 191:1332-1337(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Essential for epithelial morphogenesis. May mediate
CC Ca(2+)-regulation of exocytosis acrosomal reaction in sperm.
CC -!- SUBUNIT: Interacts with SYT6 and SYT8; the interaction is Ca(2+)-
CC dependent (By similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist;
CC Name=3;
CC IsoId=P32856-1; Sequence=Displayed;
CC Name=1;
CC IsoId=P32856-2; Sequence=VSP_006334;
CC Name=2;
CC IsoId=P32856-3; Sequence=VSP_006335;
CC -!- SIMILARITY: Belongs to the syntaxin family.
CC -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA03436.1; Type=Frameshift; Positions=Several;
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; D14582; BAA03436.1; ALT_FRAME; mRNA.
DR EMBL; AC073912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047496; AAH47496.1; -; mRNA.
DR PIR; JN0466; JN0466.
DR RefSeq; NP_001971.2; NM_001980.3.
DR RefSeq; NP_919337.1; NM_194356.2.
DR RefSeq; XP_005253613.1; XM_005253556.1.
DR UniGene; Hs.437585; -.
DR ProteinModelPortal; P32856; -.
DR SMR; P32856; 26-149, 188-283.
DR STRING; 9606.ENSP00000342554; -.
DR PhosphoSite; P32856; -.
DR DMDM; 292495060; -.
DR PaxDb; P32856; -.
DR PRIDE; P32856; -.
DR Ensembl; ENST00000261653; ENSP00000261653; ENSG00000111450.
DR Ensembl; ENST00000392373; ENSP00000376178; ENSG00000111450.
DR GeneID; 2054; -.
DR KEGG; hsa:2054; -.
DR UCSC; uc001uio.4; human.
DR CTD; 2054; -.
DR GeneCards; GC12M131274; -.
DR HGNC; HGNC:3403; STX2.
DR HPA; CAB022658; -.
DR MIM; 132350; gene.
DR neXtProt; NX_P32856; -.
DR PharmGKB; PA27831; -.
DR eggNOG; COG5074; -.
DR HOGENOM; HOG000286023; -.
DR HOVERGEN; HBG000497; -.
DR InParanoid; P32856; -.
DR KO; K08486; -.
DR OMA; DLTACRK; -.
DR OrthoDB; EOG7X9G7R; -.
DR PhylomeDB; P32856; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13685; Neuronal System.
DR ChiTaRS; STX2; human.
DR GeneWiki; STX2; -.
DR GenomeRNAi; 2054; -.
DR NextBio; 8351; -.
DR PRO; PR:P32856; -.
DR Bgee; P32856; -.
DR CleanEx; HS_STX2; -.
DR Genevestigator; P32856; -.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:HGNC.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; TAS:ProtInc.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISS:HGNC.
DR GO; GO:0007340; P:acrosome reaction; ISS:HGNC.
DR GO; GO:0030154; P:cell differentiation; IEA:Ensembl.
DR GO; GO:0007398; P:ectoderm development; TAS:ProtInc.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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 Alternative splicing; Coiled coil; Complete proteome; Membrane;
KW Polymorphism; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 288 Syntaxin-2.
FT /FTId=PRO_0000210196.
FT TOPO_DOM 1 264 Cytoplasmic (Potential).
FT TRANSMEM 265 288 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT DOMAIN 191 253 t-SNARE coiled-coil homology.
FT COILED 35 101 Potential.
FT VAR_SEQ 263 288 KKWIIIAVSVVLVAIIALIIGLSVGK -> QQHCHSNHIPR
FT AIYP (in isoform 2).
FT /FTId=VSP_006335.
FT VAR_SEQ 264 288 KWIIIAVSVVLVAIIALIIGLSVGK -> LMFIIICVIVLL
FT VILGIILATTLS (in isoform 1).
FT /FTId=VSP_006334.
FT VARIANT 42 42 S -> T (in dbSNP:rs6486602).
FT /FTId=VAR_014850.
FT VARIANT 54 54 K -> R (in dbSNP:rs7301926).
FT /FTId=VAR_057259.
FT CONFLICT 89 89 R -> A (in Ref. 1; BAA03436).
FT CONFLICT 276 276 A -> V (in Ref. 1; BAA03436).
FT CONFLICT 288 288 K -> I (in Ref. 1; BAA03436).
SQ SEQUENCE 288 AA; 33341 MW; 5668E6BF891360B4 CRC64;
MRDRLPDLTA CRKNDDGDTV VVVEKDHFMD DFFHQVEEIR NSIDKITQYV EEVKKNHSII
LSAPNPEGKI KEELEDLNKE IKKTANKIRA KLKAIEQSFD QDESGNRTSV DLRIRRTQHS
VLSRKFVEAM AEYNEAQTLF RERSKGRIQR QLEITGRTTT DDELEEMLES GKPSIFTSDI
ISDSQITRQA LNEIESRHKD IMKLETSIRE LHEMFMDMAM FVETQGEMIN NIERNVMNAT
DYVEHAKEET KKAIKYQSKA RRKKWIIIAV SVVLVAIIAL IIGLSVGK
//
MIM
132350
*RECORD*
*FIELD* NO
132350
*FIELD* TI
*132350 SYNTAXIN 2; STX2
;;EPIMORPHIN; EPIM;;
SYNTAXIN 2A; STX2A;;
SYNTAXIN 2B; STX2B;;
read moreSYNTAXIN 2C; STX2C
*FIELD* TX
CLONING
Hirai et al. (1992) identified a novel 150-kD protein expressed on the
surface of mesenchymal cells of mouse embryonic tissues. A monoclonal
antibody to this molecule inhibited various processes of epithelial
morphogenesis, such as hair follicle growth and lung epithelial tubular
formation, in organ cultures of these tissues. Sequence analysis of cDNA
encoding this protein showed that it had 289 amino acids with a
hydrophobic stretch at the C terminus. NIH-3T3 cells transfected with
the cDNA expressed the exogenous 150-kD protein on their surface. When
lung epithelial cells were cocultured with these transfected cells, they
showed normal tubular morphogenesis, but not when cocultured with
untransfected NIH-3T3 cells. Hirai et al. (1992) interpreted these
results as indicating that the protein, termed epimorphin, plays a
central role in epithelial-mesenchymal interactions.
GENE FUNCTION
Low et al. (2003) found that 2 members of the SNARE membrane fusion
machinery, syntaxin-2 and Vamp8 (603177), localized to the midbody
during cytokinesis in rat and canine kidney cell lines. Inhibition of
syntaxin-2 and Vamp8 function by overexpression of nonmembrane-anchored
mutants caused failure of cytokinesis leading to the formation of
binucleated cells. Time-lapse microscopy showed that only midbody
abscission and not further upstream events, such as furrowing, were
affected.
MAPPING
Zha et al. (1996) mapped the rat, mouse, and human epimorphin genes.
They used a rat epimorphin DNA probe, mouse rat somatic cell hybrids,
and fluorescence in situ hybridization to map epimorphin to rat
chromosome 12q16. By analyzing epimorphin RFLPs segregating in 2 genetic
crosses, Zha et al. (1996) mapped epimorphin to mouse chromosome 5, a
region homologous to parts of human chromosomes 7 and 12. They
determined that epimorphin is a new member of the synteny group
conserved between mouse chromosome 5 and rat chromosome 5 that also
includes Tcf1 (142410), Mdh2 (154100), and Gus. Zha et al. (1996) noted
that mouse epimorphin maps near the developmental mutation bf (buff),
which is characterized by alteration of coat color in non-agouti mice.
Zha et al. (1996) mapped the epimorphin gene to human chromosome 7 by in
situ hybridization.
ANIMAL MODEL
Wang et al. (2006) found that male Epim -/- mice were sterile due to
abnormal testicular development and impaired spermatogenesis. Intestinal
growth was increased in Epim -/- mice due to augmented crypt cell
proliferation and crypt fission during the suckling period that was
mediated, at least in part, by changes in Bmp (see BMP1; 112264) and Wnt
(see WNT1; 164820) signaling pathways. Colonic mucosal injury and
colitis induced by dextran sodium sulfate were ameliorated in Epim -/-
mice, likely due to the increased proliferative capacity of the Epim -/-
colon.
*FIELD* RF
1. Hirai, Y.; Takebe, K.; Takashina, M.; Kobayashi, S.; Takeichi,
M.: Epimorhpin: a mesenchymal protein essential for epithelial morphogenesis. Cell 69:
471-481, 1992.
2. Low, S. H.; Li, X.; Miura, M.; Kudo, N.; Quinones, B.; Weimbs,
T.: Syntaxin 2 and endobrevin are required for the terminal step
of cytokinesis in mammalian cells. Dev. Cell 4: 753-759, 2003.
3. Wang, Y.; Wang, L.; Iordanov, H.; Swietlicki, E. A.; Zheng, Q.;
Jiang, S.; Tang, Y.; Levin, M. S.; Rubin, D. C.: Epimorphin-/- mice
have increased intestinal growth, decreased susceptibility to dextran
sodium sulfate colitis, and impaired spermatogenesis. J. Clin. Invest. 116:
1535-1546, 2006.
4. Zha, H.; Remmers, E. F.; Szpirer, C.; Szpirer, J.; Zhang, H.; Kozak,
C. A.; Wilder, R. L.: The epimorphin gene is highly conserved among
humans, mice, and rats and maps to human chromosome 7, mouse chromosome
5, and rat chromosome 12. Genomics 37: 386-389, 1996.
*FIELD* CN
Patricia A. Hartz - updated: 7/20/2006
Patricia A. Hartz - updated: 9/2/2005
Moyra Smith - updated: 12/19/1996
*FIELD* CD
Victor A. McKusick: 5/29/1992
*FIELD* ED
mgross: 01/03/2011
mgross: 10/1/2009
mgross: 8/2/2006
terry: 7/20/2006
mgross: 9/7/2005
terry: 9/2/2005
carol: 3/13/2000
mark: 12/19/1996
jamie: 12/18/1996
jamie: 12/17/1996
carol: 8/10/1992
carol: 5/29/1992
*RECORD*
*FIELD* NO
132350
*FIELD* TI
*132350 SYNTAXIN 2; STX2
;;EPIMORPHIN; EPIM;;
SYNTAXIN 2A; STX2A;;
SYNTAXIN 2B; STX2B;;
read moreSYNTAXIN 2C; STX2C
*FIELD* TX
CLONING
Hirai et al. (1992) identified a novel 150-kD protein expressed on the
surface of mesenchymal cells of mouse embryonic tissues. A monoclonal
antibody to this molecule inhibited various processes of epithelial
morphogenesis, such as hair follicle growth and lung epithelial tubular
formation, in organ cultures of these tissues. Sequence analysis of cDNA
encoding this protein showed that it had 289 amino acids with a
hydrophobic stretch at the C terminus. NIH-3T3 cells transfected with
the cDNA expressed the exogenous 150-kD protein on their surface. When
lung epithelial cells were cocultured with these transfected cells, they
showed normal tubular morphogenesis, but not when cocultured with
untransfected NIH-3T3 cells. Hirai et al. (1992) interpreted these
results as indicating that the protein, termed epimorphin, plays a
central role in epithelial-mesenchymal interactions.
GENE FUNCTION
Low et al. (2003) found that 2 members of the SNARE membrane fusion
machinery, syntaxin-2 and Vamp8 (603177), localized to the midbody
during cytokinesis in rat and canine kidney cell lines. Inhibition of
syntaxin-2 and Vamp8 function by overexpression of nonmembrane-anchored
mutants caused failure of cytokinesis leading to the formation of
binucleated cells. Time-lapse microscopy showed that only midbody
abscission and not further upstream events, such as furrowing, were
affected.
MAPPING
Zha et al. (1996) mapped the rat, mouse, and human epimorphin genes.
They used a rat epimorphin DNA probe, mouse rat somatic cell hybrids,
and fluorescence in situ hybridization to map epimorphin to rat
chromosome 12q16. By analyzing epimorphin RFLPs segregating in 2 genetic
crosses, Zha et al. (1996) mapped epimorphin to mouse chromosome 5, a
region homologous to parts of human chromosomes 7 and 12. They
determined that epimorphin is a new member of the synteny group
conserved between mouse chromosome 5 and rat chromosome 5 that also
includes Tcf1 (142410), Mdh2 (154100), and Gus. Zha et al. (1996) noted
that mouse epimorphin maps near the developmental mutation bf (buff),
which is characterized by alteration of coat color in non-agouti mice.
Zha et al. (1996) mapped the epimorphin gene to human chromosome 7 by in
situ hybridization.
ANIMAL MODEL
Wang et al. (2006) found that male Epim -/- mice were sterile due to
abnormal testicular development and impaired spermatogenesis. Intestinal
growth was increased in Epim -/- mice due to augmented crypt cell
proliferation and crypt fission during the suckling period that was
mediated, at least in part, by changes in Bmp (see BMP1; 112264) and Wnt
(see WNT1; 164820) signaling pathways. Colonic mucosal injury and
colitis induced by dextran sodium sulfate were ameliorated in Epim -/-
mice, likely due to the increased proliferative capacity of the Epim -/-
colon.
*FIELD* RF
1. Hirai, Y.; Takebe, K.; Takashina, M.; Kobayashi, S.; Takeichi,
M.: Epimorhpin: a mesenchymal protein essential for epithelial morphogenesis. Cell 69:
471-481, 1992.
2. Low, S. H.; Li, X.; Miura, M.; Kudo, N.; Quinones, B.; Weimbs,
T.: Syntaxin 2 and endobrevin are required for the terminal step
of cytokinesis in mammalian cells. Dev. Cell 4: 753-759, 2003.
3. Wang, Y.; Wang, L.; Iordanov, H.; Swietlicki, E. A.; Zheng, Q.;
Jiang, S.; Tang, Y.; Levin, M. S.; Rubin, D. C.: Epimorphin-/- mice
have increased intestinal growth, decreased susceptibility to dextran
sodium sulfate colitis, and impaired spermatogenesis. J. Clin. Invest. 116:
1535-1546, 2006.
4. Zha, H.; Remmers, E. F.; Szpirer, C.; Szpirer, J.; Zhang, H.; Kozak,
C. A.; Wilder, R. L.: The epimorphin gene is highly conserved among
humans, mice, and rats and maps to human chromosome 7, mouse chromosome
5, and rat chromosome 12. Genomics 37: 386-389, 1996.
*FIELD* CN
Patricia A. Hartz - updated: 7/20/2006
Patricia A. Hartz - updated: 9/2/2005
Moyra Smith - updated: 12/19/1996
*FIELD* CD
Victor A. McKusick: 5/29/1992
*FIELD* ED
mgross: 01/03/2011
mgross: 10/1/2009
mgross: 8/2/2006
terry: 7/20/2006
mgross: 9/7/2005
terry: 9/2/2005
carol: 3/13/2000
mark: 12/19/1996
jamie: 12/18/1996
jamie: 12/17/1996
carol: 8/10/1992
carol: 5/29/1992