LAG1_SCHPO
ID LAG1_SCHPO Reviewed; 390 AA.
AC P78970; O13860;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Sphingosine N-acyltransferase lag1;
DE EC=2.3.1.24;
DE AltName: Full=Longevity assurance factor 1;
DE AltName: Full=Longevity assurance protein 1;
GN Name=lag1; ORFNames=SPAC1A6.09c;
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 [GENOMIC DNA].
RA Chanda E.R., Lingner C., Ko Z., Young P.G.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372 AND SER-374, 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). Involved in the aging process
CC (By similarity). {ECO:0000250}.
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; U76608; AAB19113.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB16359.1; -; Genomic_DNA.
DR PIR; T38012; T38012.
DR RefSeq; NP_593201.1; NM_001018597.2.
DR AlphaFoldDB; P78970; -.
DR SMR; P78970; -.
DR BioGRID; 278925; 37.
DR STRING; 4896.SPAC1A6.09c.1; -.
DR iPTMnet; P78970; -.
DR MaxQB; P78970; -.
DR PaxDb; P78970; -.
DR PRIDE; P78970; -.
DR EnsemblFungi; SPAC1A6.09c.1; SPAC1A6.09c.1:pep; SPAC1A6.09c.
DR PomBase; SPAC1A6.09c; lag1.
DR VEuPathDB; FungiDB:SPAC1A6.09c; -.
DR eggNOG; KOG1607; Eukaryota.
DR HOGENOM; CLU_028277_2_0_1; -.
DR InParanoid; P78970; -.
DR OMA; IAIEWIF; -.
DR PhylomeDB; P78970; -.
DR Reactome; R-SPO-1660661; Sphingolipid de novo biosynthesis.
DR PRO; PR:P78970; -.
DR Proteomes; UP000002485; Chromosome I.
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 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 Membrane; Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..390
FT /note="Sphingosine N-acyltransferase lag1"
FT /id="PRO_0000185526"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 153..365
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT REGION 367..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..390
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 379..390
FT /note="EDEEASSTNEDK -> GRRGGEFNE (in Ref. 1; AAB19113)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 45668 MW; DC00FB5C2D2F22CC CRC64;
MSNRKADEKH HMSSSSLTND RSYIRNLSNR KTSISRKVPI TRTLEDPSNF VAKDGTKLVQ
APLFLLVWQK EICLSIIAIC FACLLSPSLR PYAEPFIFLS YKQPDGSYGK GPKDACFPIF
WVIVFTAFRV IVMDYVFRPF VLNWGVRNRK VIIRFCEQGY SFFYYLCFWF LGLYIYRSSN
YWSNEEKLFE DYPQYYMSPL FKAYYLIQLG FWLQQILVLH LEQRRADHWQ MFAHHIVTCA
LIILSYGFNF LRVGNAILYI FDLSDYILSG GKMLKYLGFG KICDYLFGIF VASWVYSRHY
LFSKILRVVV TNAPEIIGGF HLDVPNGYIF NKPIYIAFII LLFTLQLLIY IWFGMIVKVA
YRVFSGEEAT DSRSDDEGED EEASSTNEDK
