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TXL1_SCHPO
ID   TXL1_SCHPO              Reviewed;         290 AA.
AC   Q9USR1;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 144.
DE   RecName: Full=Thioredoxin-like protein 1;
DE   AltName: Full=Thioredoxin homolog 3;
GN   Name=txl1; Synonyms=trx3; ORFNames=SPBC577.08c;
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 [GENOMIC DNA], AND FUNCTION.
RX   PubMed=17668038; DOI=10.1139/w07-040;
RA   Kim S.-J., Jung E.-M., Jung H.-J., Song Y.S., Park E.-H., Lim C.-J.;
RT   "Cellular functions and transcriptional regulation of a third thioredoxin
RT   from Schizosaccharomyces pombe.";
RL   Can. J. Microbiol. 53:775-783(2007).
RN   [2]
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).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17476701; DOI=10.1002/yea.1483;
RA   Jimenez A., Mateos L., Pedrajas J.R., Miranda-Vizuete A., Revuelta J.L.;
RT   "The txl1+ gene from Schizosaccharomyces pombe encodes a new thioredoxin-
RT   like 1 protein that participates in the antioxidant defence against tert-
RT   butyl hydroperoxide.";
RL   Yeast 24:481-490(2007).
CC   -!- FUNCTION: Has a role in cellular detoxification of alkyl hydroperoxide.
CC       {ECO:0000269|PubMed:17476701, ECO:0000269|PubMed:17668038}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372,
CC       ECO:0000269|PubMed:17476701}. Nucleus {ECO:0000269|PubMed:16823372,
CC       ECO:0000269|PubMed:17476701}.
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DR   EMBL; DQ386686; ABD47124.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAB54816.1; -; Genomic_DNA.
DR   PIR; T40552; T40552.
DR   RefSeq; NP_595306.1; NM_001021213.2.
DR   AlphaFoldDB; Q9USR1; -.
DR   SMR; Q9USR1; -.
DR   BioGRID; 277543; 21.
DR   STRING; 4896.SPBC577.08c.1; -.
DR   iPTMnet; Q9USR1; -.
DR   MaxQB; Q9USR1; -.
DR   PaxDb; Q9USR1; -.
DR   PRIDE; Q9USR1; -.
DR   EnsemblFungi; SPBC577.08c.1; SPBC577.08c.1:pep; SPBC577.08c.
DR   GeneID; 2541028; -.
DR   KEGG; spo:SPBC577.08c; -.
DR   PomBase; SPBC577.08c; txl1.
DR   VEuPathDB; FungiDB:SPBC577.08c; -.
DR   eggNOG; KOG0908; Eukaryota.
DR   HOGENOM; CLU_072377_0_1_1; -.
DR   InParanoid; Q9USR1; -.
DR   OMA; CAPCVRI; -.
DR   PhylomeDB; Q9USR1; -.
DR   Reactome; R-SPO-9013420; RHOU GTPase cycle.
DR   Reactome; R-SPO-9013424; RHOV GTPase cycle.
DR   Reactome; R-SPO-9696273; RND1 GTPase cycle.
DR   PRO; PR:Q9USR1; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IDA:PomBase.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IMP:PomBase.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:PomBase.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:PomBase.
DR   Gene3D; 2.60.120.470; -; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR010400; PITH_dom.
DR   InterPro; IPR037047; PITH_dom_sf.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF06201; PITH; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51532; PITH; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Cytoplasm; Disulfide bond; Electron transport; Nucleus;
KW   Redox-active center; Reference proteome; Transport.
FT   CHAIN           1..290
FT                   /note="Thioredoxin-like protein 1"
FT                   /id="PRO_0000372631"
FT   DOMAIN          24..104
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          118..290
FT                   /note="PITH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00864"
FT   DISULFID        31..34
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   290 AA;  31889 MW;  02C661616AEC2F2F CRC64;
     MSVIEIRSYQ HWISTIPKSG YLAVDCYADW CGPCKAISPL FSQLASKYAS PKFVFAKVNV
     DEQRQIASGL GVKAMPTFVF FENGKQIDML TGANPQALKE KVALISSKAT GTGALASSSS
     APVKGFASLQ GCIENPQLEC LNQQDDHDLK SAFNSNPSSF LESDVDEQLM IYIPFLEVVK
     VHSIAITPVK GETSSAPKTI KLYINQPNNL SFEDAESFTP TQVIEDIVYE QDDQPTIIPL
     RFVKFQRVNS LVIFIYSNVG EEETTKISRL ELFGEPVGDS SKGKLQKVEA
 
 
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