STX2_HUMAN
ID STX2_HUMAN Reviewed; 288 AA.
AC P32856; Q86VW8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 195.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., 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., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., 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., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Essential for epithelial morphogenesis. May mediate Ca(2+)-
CC regulation of exocytosis acrosomal reaction in sperm.
CC -!- SUBUNIT: Interacts with SYT6 and SYT8; the interaction is Ca(2+)-
CC dependent. {ECO:0000250}.
CC -!- INTERACTION:
CC P32856-2; Q4LEZ3: AARD; NbExp=3; IntAct=EBI-11956649, EBI-5463075;
CC P32856-2; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-11956649, EBI-742038;
CC P32856-2; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-11956649, EBI-12109402;
CC P32856-2; Q9BQE5: APOL2; NbExp=3; IntAct=EBI-11956649, EBI-4290634;
CC P32856-2; O15155: BET1; NbExp=3; IntAct=EBI-11956649, EBI-749204;
CC P32856-2; Q6QNY1: BLOC1S2; NbExp=3; IntAct=EBI-11956649, EBI-465872;
CC P32856-2; P19397: CD53; NbExp=3; IntAct=EBI-11956649, EBI-6657396;
CC P32856-2; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-11956649, EBI-396137;
CC P32856-2; Q9Y5P4-2: CERT1; NbExp=3; IntAct=EBI-11956649, EBI-11156432;
CC P32856-2; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-11956649, EBI-2680384;
CC P32856-2; O00559: EBAG9; NbExp=3; IntAct=EBI-11956649, EBI-8787095;
CC P32856-2; O75355-2: ENTPD3; NbExp=3; IntAct=EBI-11956649, EBI-12279764;
CC P32856-2; P02671-2: FGA; NbExp=3; IntAct=EBI-11956649, EBI-9640259;
CC P32856-2; O00258: GET1; NbExp=3; IntAct=EBI-11956649, EBI-18908258;
CC P32856-2; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-11956649, EBI-6166686;
CC P32856-2; P30301: MIP; NbExp=3; IntAct=EBI-11956649, EBI-8449636;
CC P32856-2; Q9Y3B7: MRPL11; NbExp=3; IntAct=EBI-11956649, EBI-5453723;
CC P32856-2; Q9BT17: MTG1; NbExp=3; IntAct=EBI-11956649, EBI-2602570;
CC P32856-2; Q9H115: NAPB; NbExp=3; IntAct=EBI-11956649, EBI-3921185;
CC P32856-2; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-11956649, EBI-10317425;
CC P32856-2; P35227: PCGF2; NbExp=3; IntAct=EBI-11956649, EBI-2129767;
CC P32856-2; P26678: PLN; NbExp=3; IntAct=EBI-11956649, EBI-692836;
CC P32856-2; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-11956649, EBI-10485931;
CC P32856-2; Q59EV6: PPGB; NbExp=3; IntAct=EBI-11956649, EBI-14210385;
CC P32856-2; Q96TC7: RMDN3; NbExp=3; IntAct=EBI-11956649, EBI-1056589;
CC P32856-2; P78317: RNF4; NbExp=3; IntAct=EBI-11956649, EBI-2340927;
CC P32856-2; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-11956649, EBI-10244780;
CC P32856-2; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-11956649, EBI-8652744;
CC P32856-2; O75396: SEC22B; NbExp=3; IntAct=EBI-11956649, EBI-1058865;
CC P32856-2; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-11956649, EBI-10329948;
CC P32856-2; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-11956649, EBI-17595455;
CC P32856-2; O95721: SNAP29; NbExp=3; IntAct=EBI-11956649, EBI-490676;
CC P32856-2; P0DN84: STRIT1; NbExp=3; IntAct=EBI-11956649, EBI-12200293;
CC P32856-2; Q86Y82: STX12; NbExp=3; IntAct=EBI-11956649, EBI-2691717;
CC P32856-2; O14662-5: STX16; NbExp=3; IntAct=EBI-11956649, EBI-9089968;
CC P32856-2; Q16623: STX1A; NbExp=3; IntAct=EBI-11956649, EBI-712466;
CC P32856-2; P61266: STX1B; NbExp=3; IntAct=EBI-11956649, EBI-9071709;
CC P32856-2; P32856-2: STX2; NbExp=3; IntAct=EBI-11956649, EBI-11956649;
CC P32856-2; Q13277: STX3; NbExp=3; IntAct=EBI-11956649, EBI-1394295;
CC P32856-2; Q12846: STX4; NbExp=4; IntAct=EBI-11956649, EBI-744942;
CC P32856-2; Q13190: STX5; NbExp=3; IntAct=EBI-11956649, EBI-714206;
CC P32856-2; O43752: STX6; NbExp=3; IntAct=EBI-11956649, EBI-2695795;
CC P32856-2; O15400: STX7; NbExp=3; IntAct=EBI-11956649, EBI-3221827;
CC P32856-2; Q9UNK0: STX8; NbExp=3; IntAct=EBI-11956649, EBI-727240;
CC P32856-2; Q9Y2K9: STXBP5L; NbExp=3; IntAct=EBI-11956649, EBI-11294039;
CC P32856-2; Q9BXJ8: TMEM120A; NbExp=3; IntAct=EBI-11956649, EBI-727322;
CC P32856-2; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-11956649, EBI-10171534;
CC P32856-2; P19075: TSPAN8; NbExp=3; IntAct=EBI-11956649, EBI-4289938;
CC P32856-2; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-11956649, EBI-10180829;
CC P32856-2; P63027: VAMP2; NbExp=3; IntAct=EBI-11956649, EBI-520113;
CC P32856-2; Q15836: VAMP3; NbExp=3; IntAct=EBI-11956649, EBI-722343;
CC P32856-2; O95183: VAMP5; NbExp=3; IntAct=EBI-11956649, EBI-10191195;
CC P32856-2; Q9UEU0: VTI1B; NbExp=3; IntAct=EBI-11956649, EBI-723716;
CC P32856-2; Q6PEW1: ZCCHC12; NbExp=3; IntAct=EBI-11956649, EBI-748373;
CC P32856-2; O95159: ZFPL1; NbExp=3; IntAct=EBI-11956649, EBI-718439;
CC P32856-2; A8K8V0: ZNF785; NbExp=3; IntAct=EBI-11956649, EBI-3925400;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane 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. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA03436.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D14582; BAA03436.1; ALT_FRAME; mRNA.
DR EMBL; AC073912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047496; AAH47496.1; -; mRNA.
DR CCDS; CCDS9269.1; -. [P32856-2]
DR CCDS; CCDS9270.1; -. [P32856-1]
DR PIR; JN0466; JN0466.
DR RefSeq; NP_001971.2; NM_001980.3. [P32856-2]
DR RefSeq; NP_919337.1; NM_194356.2. [P32856-1]
DR AlphaFoldDB; P32856; -.
DR SMR; P32856; -.
DR BioGRID; 108368; 76.
DR CORUM; P32856; -.
DR IntAct; P32856; 58.
DR MINT; P32856; -.
DR STRING; 9606.ENSP00000376178; -.
DR MoonDB; P32856; Curated.
DR MoonProt; P32856; -.
DR iPTMnet; P32856; -.
DR PhosphoSitePlus; P32856; -.
DR SwissPalm; P32856; -.
DR BioMuta; STX2; -.
DR DMDM; 292495060; -.
DR EPD; P32856; -.
DR jPOST; P32856; -.
DR MassIVE; P32856; -.
DR MaxQB; P32856; -.
DR PaxDb; P32856; -.
DR PeptideAtlas; P32856; -.
DR PRIDE; P32856; -.
DR ProteomicsDB; 54883; -. [P32856-1]
DR ProteomicsDB; 54884; -. [P32856-2]
DR ProteomicsDB; 54885; -. [P32856-3]
DR Antibodypedia; 19407; 269 antibodies from 30 providers.
DR DNASU; 2054; -.
DR Ensembl; ENST00000261653.10; ENSP00000261653.6; ENSG00000111450.14. [P32856-2]
DR Ensembl; ENST00000392373.7; ENSP00000376178.2; ENSG00000111450.14. [P32856-1]
DR GeneID; 2054; -.
DR KEGG; hsa:2054; -.
DR MANE-Select; ENST00000392373.7; ENSP00000376178.2; NM_194356.4; NP_919337.1.
DR UCSC; uc001uio.6; human. [P32856-1]
DR CTD; 2054; -.
DR DisGeNET; 2054; -.
DR GeneCards; STX2; -.
DR HGNC; HGNC:3403; STX2.
DR HPA; ENSG00000111450; Low tissue specificity.
DR MIM; 132350; gene.
DR neXtProt; NX_P32856; -.
DR OpenTargets; ENSG00000111450; -.
DR PharmGKB; PA27831; -.
DR VEuPathDB; HostDB:ENSG00000111450; -.
DR eggNOG; KOG0810; Eukaryota.
DR GeneTree; ENSGT01030000234627; -.
DR HOGENOM; CLU_042423_2_2_1; -.
DR InParanoid; P32856; -.
DR OMA; FMESYFR; -.
DR OrthoDB; 1033833at2759; -.
DR PhylomeDB; P32856; -.
DR TreeFam; TF313763; -.
DR PathwayCommons; P32856; -.
DR SignaLink; P32856; -.
DR BioGRID-ORCS; 2054; 10 hits in 1077 CRISPR screens.
DR ChiTaRS; STX2; human.
DR GeneWiki; STX2; -.
DR GenomeRNAi; 2054; -.
DR Pharos; P32856; Tbio.
DR PRO; PR:P32856; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P32856; protein.
DR Bgee; ENSG00000111450; Expressed in secondary oocyte and 180 other tissues.
DR ExpressionAtlas; P32856; baseline and differential.
DR Genevisible; P32856; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:HGNC-UCL.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; TAS:ProtInc.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0048787; C:presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISS:HGNC-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
DR GO; GO:0007340; P:acrosome reaction; ISS:HGNC-UCL.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR GO; GO:0030154; P:cell differentiation; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
DR GO; GO:1903575; P:cornified envelope assembly; IDA:UniProtKB.
DR GO; GO:0007398; P:ectoderm development; TAS:ProtInc.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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 GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR CDD; cd00179; SynN; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR028671; STX2.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR PANTHER; PTHR19957:SF36; PTHR19957:SF36; 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; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..288
FT /note="Syntaxin-2"
FT /id="PRO_0000210196"
FT TOPO_DOM 1..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..288
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 191..253
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT COILED 35..101
FT /evidence="ECO:0000255"
FT VAR_SEQ 263..288
FT /note="KKWIIIAVSVVLVAIIALIIGLSVGK -> QQHCHSNHIPRAIYP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:8466509"
FT /id="VSP_006335"
FT VAR_SEQ 264..288
FT /note="KWIIIAVSVVLVAIIALIIGLSVGK -> LMFIIICVIVLLVILGIILATTL
FT S (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8466509"
FT /id="VSP_006334"
FT VARIANT 42
FT /note="S -> T (in dbSNP:rs17564)"
FT /id="VAR_014850"
FT VARIANT 54
FT /note="K -> R (in dbSNP:rs7301926)"
FT /id="VAR_057259"
FT CONFLICT 89
FT /note="R -> A (in Ref. 1; BAA03436)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="A -> V (in Ref. 1; BAA03436)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="K -> I (in Ref. 1; BAA03436)"
FT /evidence="ECO:0000305"
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
