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TLG2_SCHPO
ID   TLG2_SCHPO              Reviewed;         301 AA.
AC   Q9P6P1;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=t-SNARE affecting a late Golgi compartment protein 2;
DE   AltName: Full=Syntaxin tlg2;
GN   Name=tlg2; ORFNames=SPAC823.05c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: t-SNARE that functions in transport from the endosome to the
CC       late Golgi and on the endocytic pathway. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
CC       Endosome membrane {ECO:0000250}; Single-pass type IV membrane protein
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB90150.1; -; Genomic_DNA.
DR   RefSeq; NP_593832.1; NM_001019261.2.
DR   AlphaFoldDB; Q9P6P1; -.
DR   SMR; Q9P6P1; -.
DR   BioGRID; 279856; 20.
DR   STRING; 4896.SPAC823.05c.1; -.
DR   iPTMnet; Q9P6P1; -.
DR   MaxQB; Q9P6P1; -.
DR   PaxDb; Q9P6P1; -.
DR   PRIDE; Q9P6P1; -.
DR   EnsemblFungi; SPAC823.05c.1; SPAC823.05c.1:pep; SPAC823.05c.
DR   GeneID; 2543436; -.
DR   KEGG; spo:SPAC823.05c; -.
DR   PomBase; SPAC823.05c; tlg2.
DR   VEuPathDB; FungiDB:SPAC823.05c; -.
DR   eggNOG; KOG0809; Eukaryota.
DR   HOGENOM; CLU_038177_0_0_1; -.
DR   InParanoid; Q9P6P1; -.
DR   OMA; QTMIIDQ; -.
DR   PhylomeDB; Q9P6P1; -.
DR   Reactome; R-SPO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   PRO; PR:Q9P6P1; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0005484; F:SNAP receptor activity; ISS:PomBase.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR   GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR   InterPro; IPR010989; SNARE.
DR   InterPro; IPR028673; STX16.
DR   InterPro; IPR045242; Syntaxin.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR19957; PTHR19957; 1.
DR   PANTHER; PTHR19957:SF83; PTHR19957:SF83; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; SSF47661; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Endosome; Golgi apparatus; Membrane; Protein transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..301
FT                   /note="t-SNARE affecting a late Golgi compartment protein
FT                   2"
FT                   /id="PRO_0000210278"
FT   TOPO_DOM        1..279
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        301
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          206..268
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   COILED          92..120
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   301 AA;  34441 MW;  80DD1F68E5B664C5 CRC64;
     MAYRDRTGLY ITFRQSYSHH GQRLELSGWD PKEERQSLVH KDNKDNTVIE MDMLAPRWVT
     VEGEIDSLLL NTRRNINLLD KQYAKHVLPS FSDKTEQENE IQRLTIQITQ DFQRCQKLLQ
     VTKAQTNSAT GSEALMAKNF LSNLASRIQT ESAQFRKKQS TYLKKLRGLN ANISPVESKL
     DETVSDVAIS QSTIQQVALM EEQGEDEQAI RHERAVAKIA EGIIELAQMF QDLQVLVIEQ
     GALVDRIDFN IEQTQVHAKS AEKELIKAES HQKNTGRLRF ICFLILLIVA LIVILAIKLL
     R
 
 
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