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LSD90_SCHPO
ID   LSD90_SCHPO             Reviewed;         756 AA.
AC   A9ZLL8;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Protein lsd90;
DE   AltName: Full=90kDa large and small daughter protein;
GN   Name=lsd90; ORFNames=SPBC16E9.16c;
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 [MRNA], PROTEIN SEQUENCE OF 2-21; 68-106; 112-123;
RP   215-234; 284-289; 404-411; 418-442 AND 607-629, FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=18079165; DOI=10.1093/jb/mvm232;
RA   Yokoyama K., Nakagawa M., Satoh M., Saitoh S., Dohmae N., Harada A.,
RA   Satoh N., Karasawa K., Takio K., Yanagida M., Inoue K.;
RT   "Expression of a novel 90-kDa protein, Lsd90, involved in the metabolism of
RT   very long-chain fatty acid-containing phospholipids in a mitosis-defective
RT   fission yeast mutant.";
RL   J. Biochem. 143:369-375(2008).
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).
CC   -!- FUNCTION: May be involved in the metabolism of very long-chain fatty
CC       acid-containing phospholipids (VLCFA-PL).
CC       {ECO:0000269|PubMed:18079165}.
CC   -!- SUBCELLULAR LOCATION: Note=Localizes to small particle-like structures,
CC       that differ from either the mitochondria, the endoplasmic reticulum
CC       near the nucleus, or the peroxisomes. {ECO:0000269|PubMed:18079165}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB16908.4; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB012755; BAF98920.1; -; mRNA.
DR   EMBL; CU329671; CAB16908.4; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; A9ZLL8; -.
DR   SMR; A9ZLL8; -.
DR   STRING; 4896.SPBC16E9.16c.1; -.
DR   iPTMnet; A9ZLL8; -.
DR   SwissPalm; A9ZLL8; -.
DR   MaxQB; A9ZLL8; -.
DR   PaxDb; A9ZLL8; -.
DR   PomBase; SPBC16E9.16c; lsd90.
DR   HOGENOM; CLU_351304_0_0_1; -.
DR   PRO; PR:A9ZLL8; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IMP:PomBase.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Direct protein sequencing; Nucleotide-binding;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:18079165"
FT   CHAIN           2..756
FT                   /note="Protein lsd90"
FT                   /id="PRO_0000415924"
FT   REGION          1..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          656..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          166..603
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..632
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..697
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        704..724
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..756
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         717..724
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   756 AA;  82324 MW;  DCC5A9EE7182036D CRC64;
     MVGTINESMQ NMKIGAKETA QSAKQGIKNA GQSSSKTARD VMGNPVPGSY TAGNTANDGD
     SSYASSKNPS GNADIGATSS ERTAYAAPQR AAVDTSNVSP PSTQTGGYAS KDTTSTYEGA
     QPLSSQSSRS SNYTNVKITA TQNNVDALTG APIRIVTTTN ARIQPDEKTL QDLLEQRQVA
     LREAREAEEE LQRARQYNDR STSEALELEA RAKKAAQDAE LASERAREAQ SSIERSASLR
     EKQAREEAER AATALREAEL KHRLAQANAD VDVANSKLDI ALKNEAAWKA ERESSLAHQK
     AVIDSARAEL ERARHEAAVA DATYKKEHYE YNALVAELEE RNDNTLRTAS IREAEARNLE
     VHMEDTLKDA RMRSRNATEQ VEVVKREINS EIDVYRSSVE KTKAELASYQ KGLPSQKEAC
     DRELDDATRA LQAAQDRFNA AKLRVNQFDV DSRQQLAMLT KKVRDAEDAE EKYRISCHQR
     EEEITRCATQ AYDAVKAAEK RNETIAEAAR AKENEAKDLY SKAESITQDL NAKRSHPPQP
     ANLDYSSAIQ RAQERLTLEE SKLTDLRTAE PSQYVNDVEV ARRALRDAQA EQSKVESEYN
     SVKGSKLYTT EPVHPHAVTT NEPTDVSTKS KSAAYHYPAT TETVSSKAAR SATTPAYVGG
     ATKTPSTTKA VESTPSTLPT SASTNAAATT TTKKPKAAKS TAVRDDVSSA SSDSDKGTTG
     LGKSESKSSR KERRSSTSSG HGLMNNVRHA LGMSNK
 
 
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