Reviewed, UniProtKB/Swiss-Prot P78970 (LAG1_SCHPO)

Names and origin

Protein names

Recommended name:
    Sphingosine N-acyltransferase lag1
    EC=2.3.1.24
Alternative name(s):
    Longevity assurance factor 1
    Longevity assurance protein 1

Gene names

Name:	lag1
ORF Names:	SPAC1A6.09c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the ceramide synthase complex required for C26-CoA-dependent ceramide synthesis. Facilitates ER-to-Golgi transport of GPI-anchored proteins By similarity. Involved in the aging process By similarity.
Catalytic activity	Acyl-CoA + sphingosine = CoA + N-acylsphingosine.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the sphingosine N-acyltransferase family. Contains 1 TLC (TRAM/LAG1/CLN8) domain.

Ontologies

Keywords
Biological process	Lipid metabolism Lipid synthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Molecular function	Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW response to drug Inferred from genetic interaction. Source: GeneDB_SPombe response to toxin Inferred from mutant phenotype. Source: GeneDB_SPombe vacuolar acidification Inferred from genetic interaction. Source: GeneDB_SPombe
Cellular component	integral to endoplasmic reticulum membrane Non-traceable author statement. Source: GeneDB_SPombe
Molecular function	sphingosine N-acyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 390	390	Sphingosine N-acyltransferase lag1		PRO_0000185526
Regions
	Transmembrane	63 – 83	21	Potential
	Transmembrane	117 – 137	21	Potential
	Transmembrane	155 – 175	21	Potential
	Transmembrane	199 – 219	21	Potential
	Transmembrane	231 – 251	21	Potential
	Transmembrane	276 – 296	21	Potential
	Transmembrane	336 – 356	21	Potential
	Domain	153 – 365	213	TLC
	Compositional bias	13 – 16	4	Poly-Ser
Amino acid modifications
	Modified residue	372	1	Phosphoserine Ref.3
	Modified residue	374	1	Phosphoserine Ref.3
	Glycosylation	26	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	379 – 390	12	EDEEA…TNEDK → GRRGGEFNE in AAB19113. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P78970-1 [UniParc]. Last modified December 15, 1998. Version 2. Checksum: DC00FB5C2D2F22CC	FASTA	390	45,668
	10 20 30 40 50 60 MSNRKADEKH HMSSSSLTND RSYIRNLSNR KTSISRKVPI TRTLEDPSNF VAKDGTKLVQ 70 80 90 100 110 120 APLFLLVWQK EICLSIIAIC FACLLSPSLR PYAEPFIFLS YKQPDGSYGK GPKDACFPIF 130 140 150 160 170 180 WVIVFTAFRV IVMDYVFRPF VLNWGVRNRK VIIRFCEQGY SFFYYLCFWF LGLYIYRSSN 190 200 210 220 230 240 YWSNEEKLFE DYPQYYMSPL FKAYYLIQLG FWLQQILVLH LEQRRADHWQ MFAHHIVTCA 250 260 270 280 290 300 LIILSYGFNF LRVGNAILYI FDLSDYILSG GKMLKYLGFG KICDYLFGIF VASWVYSRHY 310 320 330 340 350 360 LFSKILRVVV TNAPEIIGGF HLDVPNGYIF NKPIYIAFII LLFTLQLLIY IWFGMIVKVA 370 380 390 YRVFSGEEAT DSRSDDEGED EEASSTNEDK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Chanda E.R., Lingner C., Ko Z., Young P.G. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372 AND SER-374, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U76608 Genomic DNA. Translation: AAB19113.1. CU329670 Genomic DNA. Translation: CAB16359.1.
PIR	T38012.
RefSeq	NP_593201.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2542464.
GenomeReviews	Gene locus lag1 in contig CU329670_GR.
KEGG	spo:SPAC1A6.09c.
NMPDR	fig|4896.1.peg.3171.
Organism-specific databases
GeneDB_Spombe	SPAC1A6.09c.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000896-MON.
BRENDA	2.3.1.24. 653.
Gene expression databases
ArrayExpress	P78970.
Family and domain databases
InterPro	IPR016439. Longevity_assurance_LAG1_LAC1. IPR006634. TLC-dom. IPR013599. TRAM1. [Graphical view]
Pfam	PF08390. TRAM1. 1 hit. PF03798. TRAM_LAG1_CLN8. 1 hit. [Graphical view]
PIRSF	PIRSF005225. LAG1_LAC1. 1 hit.
SMART	SM00724. TLC. 1 hit. [Graphical view]
PROSITE	PS50922. TLC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LAG1_SCHPO

Accession

Primary (citable) accession number: P78970
Secondary accession number(s): O13860

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	December 15, 1998
Last modified:	September 22, 2009
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)