LAC1_SCHPO
ID LAC1_SCHPO Reviewed; 384 AA.
AC O59735;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Sphingosine N-acyltransferase lac1;
DE EC=2.3.1.24;
DE AltName: Full=Meiotically up-regulated gene 83 protein;
GN Name=lac1; Synonyms=mug83; ORFNames=SPBC3E7.15c, SPBC4F6.02c;
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 FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; THR-361 AND SER-366, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Component of the ceramide synthase complex required for C26-
CC CoA-dependent ceramide synthesis. Facilitates ER-to-Golgi transport of
CC GPI-anchored proteins (By similarity). Has a role in meiosis.
CC {ECO:0000250, ECO:0000269|PubMed:16303567}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-CoA + sphing-4-enine = an N-acylsphing-4-enine +
CC CoA + H(+); Xref=Rhea:RHEA:23768, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:57287, ChEBI:CHEBI:57756,
CC ChEBI:CHEBI:77636; EC=2.3.1.24;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sphingosine N-acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA19018.2; -; Genomic_DNA.
DR PIR; T40389; T40389.
DR RefSeq; NP_596102.1; NM_001022018.2.
DR AlphaFoldDB; O59735; -.
DR BioGRID; 276994; 7.
DR STRING; 4896.SPBC3E7.15c.1; -.
DR iPTMnet; O59735; -.
DR PaxDb; O59735; -.
DR PRIDE; O59735; -.
DR EnsemblFungi; SPBC3E7.15c.1; SPBC3E7.15c.1:pep; SPBC3E7.15c.
DR GeneID; 2540466; -.
DR KEGG; spo:SPBC3E7.15c; -.
DR PomBase; SPBC3E7.15c; lac1.
DR VEuPathDB; FungiDB:SPBC3E7.15c; -.
DR eggNOG; KOG1607; Eukaryota.
DR HOGENOM; CLU_028277_4_0_1; -.
DR InParanoid; O59735; -.
DR OMA; FRIAYRF; -.
DR PhylomeDB; O59735; -.
DR Reactome; R-SPO-1660661; Sphingolipid de novo biosynthesis.
DR PRO; PR:O59735; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; EXP:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; NAS:PomBase.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0050291; F:sphingosine N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0046513; P:ceramide biosynthetic process; EXP:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007009; P:plasma membrane organization; IMP:PomBase.
DR InterPro; IPR016439; Lag1/Lac1-like.
DR InterPro; IPR006634; TLC-dom.
DR InterPro; IPR013599; TRAM1.
DR PANTHER; PTHR12560; PTHR12560; 1.
DR Pfam; PF08390; TRAM1; 1.
DR Pfam; PF03798; TRAM_LAG1_CLN8; 1.
DR PIRSF; PIRSF005225; LAG1_LAC1; 1.
DR SMART; SM00724; TLC; 1.
DR PROSITE; PS50922; TLC; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW Meiosis; Membrane; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..384
FT /note="Sphingosine N-acyltransferase lac1"
FT /id="PRO_0000185534"
FT TOPO_DOM 1..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..103
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..194
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..269
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..384
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT DOMAIN 141..357
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT REGION 19..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 361
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 384 AA; 45336 MW; 82FCF8EA6638849A CRC64;
MGNNTSRRSQ SQKFKNIPSI SAGSFSTMPV QHRGRRRRSK SIVGRAAQNA VLRSKEKTWI
VPLILLTLLV GWYFVNPNGY IKYGIFLSYP IPGTNPAQYG KGRLDIAFCL FYALFFTFCR
EFIMQEIIAR IGRHFNIRAP AKLRRFEEQA YTCLYFTVMG SWGLYVMKQT PMWFFNTDAF
WEEYPHFYHV GSFKAFYLIE AAYWIQQALV LILQLEKPRK DFKELVVHHI ITLLLIGLSY
YFHFTWIGLA VFITMDTSDI WLALSKCLNY VNTVIVYPIF VIFVFVWIYM RHYLNFKIMW
AVWGTMRTIN SFDLDWAAEQ YKCWISRDVT LILLTALQLV NIYWLILILR IGYRAFTTND
THDERSEDED EEVSDEKSSA KKND
