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
