Full text data of STX7
STX7
[Confidence: high (present in two of the MS resources)]
Syntaxin-7
Syntaxin-7
hRBCD
IPI00289876
IPI00289876 Syntaxin 7 Syntaxin 7 membrane n/a 2 n/a n/a n/a n/a n/a n/a 1 n/a 4 1 n/a 3 1 1 3 2 1 1 Type IV membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00289876 Syntaxin 7 Syntaxin 7 membrane n/a 2 n/a n/a n/a n/a n/a n/a 1 n/a 4 1 n/a 3 1 1 3 2 1 1 Type IV membrane protein n/a found at its expected molecular weight found at molecular weight
Comments
Isoform O15400-2 was detected.
Isoform O15400-2 was detected.
UniProt
O15400
ID STX7_HUMAN Reviewed; 261 AA.
AC O15400; E1P579; Q5SZW2; Q96ES9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Syntaxin-7;
GN Name=STX7;
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] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=9358037; DOI=10.1016/S0378-1119(97)00343-0;
RA Wang H., Frelin L., Pevsner J.;
RT "Human syntaxin 7: a Pep12p/Vps6p homologue implicated in vesicle
RT trafficking to lysosomes.";
RL Gene 199:39-48(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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 [5]
RP PROTEIN SEQUENCE OF 2-17, AND ACETYLATION AT SER-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP CHARACTERIZATION.
RX PubMed=10564279; DOI=10.1091/mbc.10.11.3891;
RA Prekeris R., Yang B., Oorschot V., Klumperman J., Scheller R.H.;
RT "Differential roles of syntaxin 7 and syntaxin 8 in endosomal
RT trafficking.";
RL Mol. Biol. Cell 10:3891-3908(1999).
RN [7]
RP CHARACTERIZATION.
RX PubMed=10692457; DOI=10.1074/jbc.275.9.6523;
RA Nakamura N., Yamamoto A., Wada Y., Futai M.;
RT "Syntaxin 7 mediates endocytic trafficking to late endosomes.";
RL J. Biol. Chem. 275:6523-6529(2000).
RN [8]
RP INTERACTION WITH VPS11; VPS16; VPS18 AND VPS33A.
RX PubMed=11382755; DOI=10.1074/jbc.M101778200;
RA Kim B.Y., Kraemer H., Yamamoto A., Kominami E., Kohsaka S.,
RA Akazawa C.;
RT "Molecular characterization of mammalian homologues of class C Vps
RT proteins that interact with syntaxin-7.";
RL J. Biol. Chem. 276:29393-29402(2001).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND MASS
RP 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, 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).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May be involved in protein trafficking from the plasma
CC membrane to the early endosome (EE) as well as in homotypic fusion
CC of endocytic organelles. Mediates the endocytic trafficking from
CC early endosomes to late endosomes and lysosomes.
CC -!- SUBUNIT: Forms a SNARE complex with VTI1B, STX8 and VAMP8 which
CC functions in the homotypic fusion of late endosomes. Component of
CC the SNARE complex composed of STX7, STX8, VAMP7 and VTI1B that is
CC required for heterotypic fusion of late endosomes with lysosomes
CC (By similarity). Interacts with VPS11, VPS16 and VPS18. Interacts
CC with VPS33A.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane; Single-pass type IV
CC membrane protein (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15400-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15400-2; Sequence=VSP_012938;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highest expression is found in placenta
CC followed by heart, skeletal muscle, kidney and brain. Low
CC expression is found in pancreas, lung and liver.
CC -!- SIMILARITY: Belongs to the syntaxin family.
CC -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
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DR EMBL; U77942; AAC51851.1; -; mRNA.
DR EMBL; AL357034; CAI15716.1; -; Genomic_DNA.
DR EMBL; AL357034; CAI15717.1; -; Genomic_DNA.
DR EMBL; AL589691; CAI16816.1; -; Genomic_DNA.
DR EMBL; AL589691; CAI16817.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48029.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48030.1; -; Genomic_DNA.
DR EMBL; BC011975; AAH11975.1; -; mRNA.
DR RefSeq; NP_003560.2; NM_003569.2.
DR UniGene; Hs.593148; -.
DR UniGene; Hs.605992; -.
DR ProteinModelPortal; O15400; -.
DR SMR; O15400; 10-227.
DR DIP; DIP-57384N; -.
DR IntAct; O15400; 8.
DR MINT; MINT-5002218; -.
DR STRING; 9606.ENSP00000356918; -.
DR PhosphoSite; O15400; -.
DR OGP; O15400; -.
DR PaxDb; O15400; -.
DR PRIDE; O15400; -.
DR DNASU; 8417; -.
DR Ensembl; ENST00000367937; ENSP00000356914; ENSG00000079950.
DR Ensembl; ENST00000367941; ENSP00000356918; ENSG00000079950.
DR GeneID; 8417; -.
DR KEGG; hsa:8417; -.
DR UCSC; uc003qdg.2; human.
DR CTD; 8417; -.
DR GeneCards; GC06M132822; -.
DR HGNC; HGNC:11442; STX7.
DR HPA; HPA001467; -.
DR MIM; 603217; gene.
DR neXtProt; NX_O15400; -.
DR PharmGKB; PA36239; -.
DR eggNOG; COG5325; -.
DR HOGENOM; HOG000188453; -.
DR HOVERGEN; HBG053083; -.
DR InParanoid; O15400; -.
DR KO; K08488; -.
DR OMA; ADVHVQQ; -.
DR OrthoDB; EOG7B31PS; -.
DR PhylomeDB; O15400; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13685; Neuronal System.
DR ChiTaRS; STX7; human.
DR GeneWiki; STX7; -.
DR GenomeRNAi; 8417; -.
DR NextBio; 31504; -.
DR PMAP-CutDB; O15400; -.
DR PRO; PR:O15400; -.
DR Bgee; O15400; -.
DR CleanEx; HS_STX7; -.
DR Genevestigator; O15400; -.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0031201; C:SNARE complex; IBA:RefGenome.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:RefGenome.
DR GO; GO:0000149; F:SNARE binding; IBA:RefGenome.
DR GO; GO:0006886; P:intracellular protein transport; IBA:RefGenome.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:ProtInc.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IBA:RefGenome.
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 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 Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Direct protein sequencing; Endosome; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 261 Syntaxin-7.
FT /FTId=PRO_0000210213.
FT TOPO_DOM 2 238 Cytoplasmic (Potential).
FT TRANSMEM 239 259 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT TOPO_DOM 260 261 Vesicular (Potential).
FT DOMAIN 165 227 t-SNARE coiled-coil homology.
FT COILED 47 69 Potential.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 45 45 Phosphoserine (By similarity).
FT MOD_RES 79 79 Phosphothreonine (By similarity).
FT MOD_RES 125 125 Phosphoserine (By similarity).
FT MOD_RES 126 126 Phosphoserine (By similarity).
FT MOD_RES 129 129 Phosphoserine.
FT MOD_RES 205 205 Phosphoserine (By similarity).
FT VAR_SEQ 232 261 RKSRKTLCIIILILVIGVAIISLIIWGLNH -> KKDSCML
FT M (in isoform 2).
FT /FTId=VSP_012938.
FT CONFLICT 12 12 A -> T (in Ref. 1; AAC51851).
SQ SEQUENCE 261 AA; 29816 MW; 42AC173F0233ACDA CRC64;
MSYTPGVGGD PAQLAQRISS NIQKITQCSV EIQRTLNQLG TPQDSPELRQ QLQQKQQYTN
QLAKETDKYI KEFGSLPTTP SEQRQRKIQK DRLVAEFTTS LTNFQKVQRQ AAEREKEFVA
RVRASSRVSG SFPEDSSKER NLVSWESQTQ PQVQVQDEEI TEDDLRLIHE RESSIRQLEA
DIMDINEIFK DLGMMIHEQG DVIDSIEANV ENAEVHVQQA NQQLSRAADY QRKSRKTLCI
IILILVIGVA IISLIIWGLN H
//
ID STX7_HUMAN Reviewed; 261 AA.
AC O15400; E1P579; Q5SZW2; Q96ES9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Syntaxin-7;
GN Name=STX7;
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] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=9358037; DOI=10.1016/S0378-1119(97)00343-0;
RA Wang H., Frelin L., Pevsner J.;
RT "Human syntaxin 7: a Pep12p/Vps6p homologue implicated in vesicle
RT trafficking to lysosomes.";
RL Gene 199:39-48(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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 [5]
RP PROTEIN SEQUENCE OF 2-17, AND ACETYLATION AT SER-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP CHARACTERIZATION.
RX PubMed=10564279; DOI=10.1091/mbc.10.11.3891;
RA Prekeris R., Yang B., Oorschot V., Klumperman J., Scheller R.H.;
RT "Differential roles of syntaxin 7 and syntaxin 8 in endosomal
RT trafficking.";
RL Mol. Biol. Cell 10:3891-3908(1999).
RN [7]
RP CHARACTERIZATION.
RX PubMed=10692457; DOI=10.1074/jbc.275.9.6523;
RA Nakamura N., Yamamoto A., Wada Y., Futai M.;
RT "Syntaxin 7 mediates endocytic trafficking to late endosomes.";
RL J. Biol. Chem. 275:6523-6529(2000).
RN [8]
RP INTERACTION WITH VPS11; VPS16; VPS18 AND VPS33A.
RX PubMed=11382755; DOI=10.1074/jbc.M101778200;
RA Kim B.Y., Kraemer H., Yamamoto A., Kominami E., Kohsaka S.,
RA Akazawa C.;
RT "Molecular characterization of mammalian homologues of class C Vps
RT proteins that interact with syntaxin-7.";
RL J. Biol. Chem. 276:29393-29402(2001).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND MASS
RP 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, 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).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May be involved in protein trafficking from the plasma
CC membrane to the early endosome (EE) as well as in homotypic fusion
CC of endocytic organelles. Mediates the endocytic trafficking from
CC early endosomes to late endosomes and lysosomes.
CC -!- SUBUNIT: Forms a SNARE complex with VTI1B, STX8 and VAMP8 which
CC functions in the homotypic fusion of late endosomes. Component of
CC the SNARE complex composed of STX7, STX8, VAMP7 and VTI1B that is
CC required for heterotypic fusion of late endosomes with lysosomes
CC (By similarity). Interacts with VPS11, VPS16 and VPS18. Interacts
CC with VPS33A.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane; Single-pass type IV
CC membrane protein (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15400-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15400-2; Sequence=VSP_012938;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highest expression is found in placenta
CC followed by heart, skeletal muscle, kidney and brain. Low
CC expression is found in pancreas, lung and liver.
CC -!- SIMILARITY: Belongs to the syntaxin family.
CC -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
CC -----------------------------------------------------------------------
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DR EMBL; U77942; AAC51851.1; -; mRNA.
DR EMBL; AL357034; CAI15716.1; -; Genomic_DNA.
DR EMBL; AL357034; CAI15717.1; -; Genomic_DNA.
DR EMBL; AL589691; CAI16816.1; -; Genomic_DNA.
DR EMBL; AL589691; CAI16817.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48029.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48030.1; -; Genomic_DNA.
DR EMBL; BC011975; AAH11975.1; -; mRNA.
DR RefSeq; NP_003560.2; NM_003569.2.
DR UniGene; Hs.593148; -.
DR UniGene; Hs.605992; -.
DR ProteinModelPortal; O15400; -.
DR SMR; O15400; 10-227.
DR DIP; DIP-57384N; -.
DR IntAct; O15400; 8.
DR MINT; MINT-5002218; -.
DR STRING; 9606.ENSP00000356918; -.
DR PhosphoSite; O15400; -.
DR OGP; O15400; -.
DR PaxDb; O15400; -.
DR PRIDE; O15400; -.
DR DNASU; 8417; -.
DR Ensembl; ENST00000367937; ENSP00000356914; ENSG00000079950.
DR Ensembl; ENST00000367941; ENSP00000356918; ENSG00000079950.
DR GeneID; 8417; -.
DR KEGG; hsa:8417; -.
DR UCSC; uc003qdg.2; human.
DR CTD; 8417; -.
DR GeneCards; GC06M132822; -.
DR HGNC; HGNC:11442; STX7.
DR HPA; HPA001467; -.
DR MIM; 603217; gene.
DR neXtProt; NX_O15400; -.
DR PharmGKB; PA36239; -.
DR eggNOG; COG5325; -.
DR HOGENOM; HOG000188453; -.
DR HOVERGEN; HBG053083; -.
DR InParanoid; O15400; -.
DR KO; K08488; -.
DR OMA; ADVHVQQ; -.
DR OrthoDB; EOG7B31PS; -.
DR PhylomeDB; O15400; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13685; Neuronal System.
DR ChiTaRS; STX7; human.
DR GeneWiki; STX7; -.
DR GenomeRNAi; 8417; -.
DR NextBio; 31504; -.
DR PMAP-CutDB; O15400; -.
DR PRO; PR:O15400; -.
DR Bgee; O15400; -.
DR CleanEx; HS_STX7; -.
DR Genevestigator; O15400; -.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0031201; C:SNARE complex; IBA:RefGenome.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:RefGenome.
DR GO; GO:0000149; F:SNARE binding; IBA:RefGenome.
DR GO; GO:0006886; P:intracellular protein transport; IBA:RefGenome.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:ProtInc.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IBA:RefGenome.
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 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 Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Direct protein sequencing; Endosome; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 261 Syntaxin-7.
FT /FTId=PRO_0000210213.
FT TOPO_DOM 2 238 Cytoplasmic (Potential).
FT TRANSMEM 239 259 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT TOPO_DOM 260 261 Vesicular (Potential).
FT DOMAIN 165 227 t-SNARE coiled-coil homology.
FT COILED 47 69 Potential.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 45 45 Phosphoserine (By similarity).
FT MOD_RES 79 79 Phosphothreonine (By similarity).
FT MOD_RES 125 125 Phosphoserine (By similarity).
FT MOD_RES 126 126 Phosphoserine (By similarity).
FT MOD_RES 129 129 Phosphoserine.
FT MOD_RES 205 205 Phosphoserine (By similarity).
FT VAR_SEQ 232 261 RKSRKTLCIIILILVIGVAIISLIIWGLNH -> KKDSCML
FT M (in isoform 2).
FT /FTId=VSP_012938.
FT CONFLICT 12 12 A -> T (in Ref. 1; AAC51851).
SQ SEQUENCE 261 AA; 29816 MW; 42AC173F0233ACDA CRC64;
MSYTPGVGGD PAQLAQRISS NIQKITQCSV EIQRTLNQLG TPQDSPELRQ QLQQKQQYTN
QLAKETDKYI KEFGSLPTTP SEQRQRKIQK DRLVAEFTTS LTNFQKVQRQ AAEREKEFVA
RVRASSRVSG SFPEDSSKER NLVSWESQTQ PQVQVQDEEI TEDDLRLIHE RESSIRQLEA
DIMDINEIFK DLGMMIHEQG DVIDSIEANV ENAEVHVQQA NQQLSRAADY QRKSRKTLCI
IILILVIGVA IISLIIWGLN H
//
MIM
603217
*RECORD*
*FIELD* NO
603217
*FIELD* TI
*603217 SYNTAXIN 7; STX7
*FIELD* TX
CLONING
In the cell, the specificity of vesicle transport is thought to occur
read morethrough the interaction of vesicle proteins with receptors such as
syntaxins on a particular target membrane. See alpha-SNAP (603215).
Pep12p, or Vps6p, is a syntaxin identified in S. cerevisiae and in
Arabidopsis that is required for the sorting of soluble hydrolases from
the Golgi complex to the vacuole. By searching an EST database for human
homologs of Pep12p, Wang et al. (1997) identified partial syntaxin-7
(STX7) cDNAs. Using a partial cDNA as a probe, they isolated a fetal
brain cDNA corresponding to the entire coding region of syntaxin-7. The
deduced 261-amino acid STX7 protein contains a putative C-terminal
transmembrane domain and 3 coiled-coil domains. The human protein shares
34% and 25% sequence identity with Arabidopsis and yeast Pep12p,
respectively. In vitro, recombinant protein bound specifically to
alpha-SNAP, a key regulator of transport vesicle fusion at multiple
stages of the secretory pathway. Northern blot analysis revealed that
syntaxin-7 was expressed as 1.8- and 3.6-kb mRNAs in all tissues tested.
GENE FUNCTION
Using immunocytochemistry, fluorescence, and confocal microscopy,
Collins et al. (2002) showed that STX7 and STX13 (STX12; 606892) are
involved in the ordered fusion of endosomes and lysosomes with the
phagosome, where phagocytic cells kill and degrade internalized foreign
particles. STX12 is localized to the recycling endosome compartment,
whereas STX7 is found in late endosomes and lysosomes and both are
recruited to the phagosome. However, STX12 is acquired earlier before
rapidly recycling off the phagosome, whereas STX7 is recruited later and
continues to accumulate throughout the phagosome maturation process.
MAPPING
By analysis of a human monochromosomal panel, Wang et al. (1997) mapped
the STX7 gene to chromosome 6.
*FIELD* RF
1. Collins, R. F.; Schreiber, A. D.; Grinstein, S.; Trimble, W. S.
: Syntaxins 13 and 7 function at distinct steps during phagocytosis. J.
Immun. 169: 3250-3256, 2002.
2. Wang, H.; Frelin, L.; Pevsner, J.: Human syntaxin 7: a Pep12p/Vps6p
homologue implicated in vesicle trafficking to lysosomes. Gene 199:
39-48, 1997.
*FIELD* CN
Paul J. Converse - updated: 8/5/2003
*FIELD* CD
Rebekah S. Rasooly: 10/27/1998
*FIELD* ED
carol: 01/31/2007
cwells: 8/5/2003
alopez: 12/1/1998
alopez: 10/27/1998
*RECORD*
*FIELD* NO
603217
*FIELD* TI
*603217 SYNTAXIN 7; STX7
*FIELD* TX
CLONING
In the cell, the specificity of vesicle transport is thought to occur
read morethrough the interaction of vesicle proteins with receptors such as
syntaxins on a particular target membrane. See alpha-SNAP (603215).
Pep12p, or Vps6p, is a syntaxin identified in S. cerevisiae and in
Arabidopsis that is required for the sorting of soluble hydrolases from
the Golgi complex to the vacuole. By searching an EST database for human
homologs of Pep12p, Wang et al. (1997) identified partial syntaxin-7
(STX7) cDNAs. Using a partial cDNA as a probe, they isolated a fetal
brain cDNA corresponding to the entire coding region of syntaxin-7. The
deduced 261-amino acid STX7 protein contains a putative C-terminal
transmembrane domain and 3 coiled-coil domains. The human protein shares
34% and 25% sequence identity with Arabidopsis and yeast Pep12p,
respectively. In vitro, recombinant protein bound specifically to
alpha-SNAP, a key regulator of transport vesicle fusion at multiple
stages of the secretory pathway. Northern blot analysis revealed that
syntaxin-7 was expressed as 1.8- and 3.6-kb mRNAs in all tissues tested.
GENE FUNCTION
Using immunocytochemistry, fluorescence, and confocal microscopy,
Collins et al. (2002) showed that STX7 and STX13 (STX12; 606892) are
involved in the ordered fusion of endosomes and lysosomes with the
phagosome, where phagocytic cells kill and degrade internalized foreign
particles. STX12 is localized to the recycling endosome compartment,
whereas STX7 is found in late endosomes and lysosomes and both are
recruited to the phagosome. However, STX12 is acquired earlier before
rapidly recycling off the phagosome, whereas STX7 is recruited later and
continues to accumulate throughout the phagosome maturation process.
MAPPING
By analysis of a human monochromosomal panel, Wang et al. (1997) mapped
the STX7 gene to chromosome 6.
*FIELD* RF
1. Collins, R. F.; Schreiber, A. D.; Grinstein, S.; Trimble, W. S.
: Syntaxins 13 and 7 function at distinct steps during phagocytosis. J.
Immun. 169: 3250-3256, 2002.
2. Wang, H.; Frelin, L.; Pevsner, J.: Human syntaxin 7: a Pep12p/Vps6p
homologue implicated in vesicle trafficking to lysosomes. Gene 199:
39-48, 1997.
*FIELD* CN
Paul J. Converse - updated: 8/5/2003
*FIELD* CD
Rebekah S. Rasooly: 10/27/1998
*FIELD* ED
carol: 01/31/2007
cwells: 8/5/2003
alopez: 12/1/1998
alopez: 10/27/1998