CSS1_SCHPO
ID CSS1_SCHPO Reviewed; 424 AA.
AC O74369; Q9Y7M0;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2000, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Inositol phosphosphingolipids phospholipase C;
DE Short=IPS phospholipase C;
DE Short=IPS-PLC;
DE EC=3.1.4.-;
GN Name=css1; ORFNames=SPBC32F12.01c, SPBC685.10c;
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, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11514435; DOI=10.1093/genetics/158.4.1397;
RA Feoktistova A., Magnelli P., Abeijon C., Perez P., Lester R.L.,
RA Dickson R.C., Gould K.L.;
RT "Coordination between fission yeast glucan formation and growth requires a
RT sphingolipase activity.";
RL Genetics 158:1397-1411(2001).
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).
CC -!- FUNCTION: Inositol phosphosphingolipids phospholipase essential for the
CC coordination of cell wall formation. Responsible for the hydrolysis of
CC the phosphosphingolipids (IPS), inositol phosphorylceramide (IPC),
CC mannosylinositol phosphorylceramide (MIPC), and mannosyldiinositol
CC phosphorylceramide (M(IP)2C). {ECO:0000269|PubMed:11514435}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11514435};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11514435}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:11514435}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:11514435}.
CC -!- SIMILARITY: Belongs to the neutral sphingomyelinase family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAB39367.1; -; Genomic_DNA.
DR PIR; T40641; T40641.
DR RefSeq; NP_596144.2; NM_001022062.3.
DR AlphaFoldDB; O74369; -.
DR SMR; O74369; -.
DR BioGRID; 277628; 3.
DR STRING; 4896.SPBC32F12.01c.1; -.
DR iPTMnet; O74369; -.
DR MaxQB; O74369; -.
DR PaxDb; O74369; -.
DR EnsemblFungi; SPBC32F12.01c.1; SPBC32F12.01c.1:pep; SPBC32F12.01c.
DR PomBase; SPBC32F12.01c; css1.
DR VEuPathDB; FungiDB:SPBC32F12.01c; -.
DR eggNOG; KOG3873; Eukaryota.
DR HOGENOM; CLU_034001_0_0_1; -.
DR InParanoid; O74369; -.
DR OMA; LCHRTAQ; -.
DR PhylomeDB; O74369; -.
DR Reactome; R-SPO-1660662; Glycosphingolipid metabolism.
DR UniPathway; UPA00222; -.
DR PRO; PR:O74369; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0071944; C:cell periphery; IDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISO:PomBase.
DR GO; GO:0016020; C:membrane; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; EXP:PomBase.
DR GO; GO:0052712; F:inositol phosphosphingolipid phospholipase activity; IMP:PomBase.
DR GO; GO:0052714; F:mannosyl-inositol phosphorylceramide phospholipase activity; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0046513; P:ceramide biosynthetic process; EXP:PomBase.
DR GO; GO:0046521; P:sphingoid catabolic process; EXP:PomBase.
DR GO; GO:0030149; P:sphingolipid catabolic process; IBA:GO_Central.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR038772; SMPD2-like.
DR PANTHER; PTHR12393; PTHR12393; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Endoplasmic reticulum;
KW Hydrolase; Lipid metabolism; Magnesium; Membrane; Metal-binding;
KW Reference proteome; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..424
FT /note="Inositol phosphosphingolipids phospholipase C"
FT /id="PRO_0000075691"
FT TRANSMEM 335..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 181
FT /note="Important for substrate recognition"
FT /evidence="ECO:0000250"
SQ SEQUENCE 424 AA; 48345 MW; 8C5DC4C3FEA4550F CRC64;
MSVEKAPELR VLSFNCWGLR FVSKYRTERL KAVGEKLAKC DYDIVLLQEV WSIYDFQEIR
NLVSCNLVYS RFFHSAAMGA GLAMFSKFPI IESSMNKYPL NGRPQAFWRG DWYVGKGVAT
ASLQHPSGRI ISLFNTHLHA PYGKGADTYL CHRLSQAWYI SKLLRAAVQR GHIVIAAGDF
NIQPLSVPHE IITSYGLVND AWLSVYPDQV EHPPNRFSMN DKELVEIAGT TCDSRLNTWR
ENISSKDMDD FVAKRLDYVF HSPSTCEAKN AKVVFLERVP KLDCSYSDHF AIETVLSIKL
QPIPVQETRV SYSIIDDTLG ITYQYMARER LHMRLRIAHL LISIPLIIGV HVAIAWCDPA
WLKVIILFFT VMLTIAAVVN GFCIGLLFGR WEFNGLLEFV AELKEQKLLC KQYLVDHPLP
FAKS
