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PHO88_SCHPO
ID   PHO88_SCHPO             Reviewed;         194 AA.
AC   O42940;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=SRP-independent targeting protein 3 homolog {ECO:0000250|UniProtKB:P38264};
DE   AltName: Full=Inorganic phosphate transport protein pho88;
DE   AltName: Full=Phosphate metabolism protein pho88;
GN   Name=pho88 {ECO:0000250|UniProtKB:P38264};
GN   ORFNames=SPBC16H5.04 {ECO:0000312|PomBase:SPBC16H5.04};
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).
RN   [2]
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).
CC   -!- FUNCTION: May function in a SRP (signal recognition particle) and GET
CC       (guided entry of tail-anchored proteins) independent pathway for
CC       targeting a broad range of substrate proteins to the endoplasmic
CC       reticulum. Involved in inorganic phosphate uptake. Also involved in
CC       telomere length regulation and maintenance (By similarity).
CC       {ECO:0000250|UniProtKB:P38264}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the PHO88 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA17902.2; -; Genomic_DNA.
DR   PIR; T39622; T39622.
DR   RefSeq; NP_595944.2; NM_001021852.3.
DR   AlphaFoldDB; O42940; -.
DR   BioGRID; 276618; 4.
DR   STRING; 4896.SPBC16H5.04.1; -.
DR   MaxQB; O42940; -.
DR   PaxDb; O42940; -.
DR   EnsemblFungi; SPBC16H5.04.1; SPBC16H5.04.1:pep; SPBC16H5.04.
DR   GeneID; 2540080; -.
DR   KEGG; spo:SPBC16H5.04; -.
DR   PomBase; SPBC16H5.04; -.
DR   VEuPathDB; FungiDB:SPBC16H5.04; -.
DR   eggNOG; KOG4554; Eukaryota.
DR   HOGENOM; CLU_099163_0_0_1; -.
DR   InParanoid; O42940; -.
DR   OMA; TTMFMHL; -.
DR   PhylomeDB; O42940; -.
DR   PRO; PR:O42940; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:PomBase.
DR   GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0045048; P:protein insertion into ER membrane; ISO:PomBase.
DR   GO; GO:0045047; P:protein targeting to ER; ISO:PomBase.
DR   InterPro; IPR012098; SND3_fun.
DR   PANTHER; PTHR28112; PTHR28112; 1.
DR   Pfam; PF10032; Pho88; 1.
DR   PIRSF; PIRSF008756; P_tr_PHO88; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; Phosphate transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..194
FT                   /note="SRP-independent targeting protein 3 homolog"
FT                   /id="PRO_0000372626"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   194 AA;  21964 MW;  D13D2BEF686149DB CRC64;
     MVSRWEKLKN NPQTKSIGIS IFLMMITRVI DFSRPSLLWP LRILYATVNI VQIGIFLYTK
     IIIEKKNDLT VLKYVEPATP MSGREHSKFV ATTVRDYDLS KLLTSFKQML VTIATTLFMH
     LYMGYAPPLL LQSVSAARGL FDNSEVQIHV QNKPAIDELR RPFKSSGGLL GSFGQVLTDK
     KSVDEAELTK LKPT
 
 
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