ELOH2_SCHPO
ID ELOH2_SCHPO Reviewed; 365 AA.
AC Q7LKX0;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 3.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Putative elongation of fatty acids protein 2 {ECO:0000250|UniProtKB:P25358};
DE EC=2.3.1.199 {ECO:0000250|UniProtKB:P25358};
DE AltName: Full=3-keto acyl-CoA synthase SPAC1639.01c {ECO:0000250|UniProtKB:P25358};
DE AltName: Full=Very-long-chain 3-oxoacyl-CoA synthase 2 {ECO:0000250|UniProtKB:P25358};
GN ORFNames=SPAC1639.01c {ECO:0000312|PomBase:SPAC1639.01c}, SPAC806.09c;
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 [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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
CC -!- FUNCTION: May be involved in the synthesis of very long chain fatty
CC acids. {ECO:0000250|UniProtKB:P25358}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-
CC chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736;
CC EC=2.3.1.199; Evidence={ECO:0000250|UniProtKB:P25358};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P25358}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ELO family. {ECO:0000305}.
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DR EMBL; CU329670; CAB55288.3; -; Genomic_DNA.
DR PIR; T37734; T37734.
DR RefSeq; NP_592859.3; NM_001018260.3.
DR AlphaFoldDB; Q7LKX0; -.
DR SMR; Q7LKX0; -.
DR BioGRID; 279607; 1.
DR STRING; 4896.SPAC1639.01c.1; -.
DR iPTMnet; Q7LKX0; -.
DR MaxQB; Q7LKX0; -.
DR PaxDb; Q7LKX0; -.
DR EnsemblFungi; SPAC1639.01c.1; SPAC1639.01c.1:pep; SPAC1639.01c.
DR GeneID; 2543177; -.
DR KEGG; spo:SPAC1639.01c; -.
DR PomBase; SPAC1639.01c; -.
DR VEuPathDB; FungiDB:SPAC1639.01c; -.
DR eggNOG; KOG3071; Eukaryota.
DR HOGENOM; CLU_048483_6_1_1; -.
DR InParanoid; Q7LKX0; -.
DR OMA; MQANWSK; -.
DR PRO; PR:Q7LKX0; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; EXP:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; EXP:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0009922; F:fatty acid elongase activity; ISO:PomBase.
DR GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IBA:GO_Central.
DR GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IBA:GO_Central.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IBA:GO_Central.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; ISO:PomBase.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR InterPro; IPR002076; ELO_fam.
DR PANTHER; PTHR11157; PTHR11157; 1.
DR Pfam; PF01151; ELO; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Glycoprotein; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..365
FT /note="Putative elongation of fatty acids protein 2"
FT /id="PRO_0000350770"
FT TOPO_DOM 1..68
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P25358"
FT TRANSMEM 69..89
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P25358"
FT TRANSMEM 112..132
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..149
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P25358"
FT TRANSMEM 150..170
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P25358"
FT TRANSMEM 180..198
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..204
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P25358"
FT TRANSMEM 205..225
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P25358"
FT TRANSMEM 242..262
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..278
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P25358"
FT TRANSMEM 279..299
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P25358"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 365 AA; 41541 MW; 14AF319BB74F9415 CRC64;
MPDSPTLHHN HIIGLENGSL TSNNNHQGMA SVSVGQFQYP IWSWLNSLAD ATFGKRPSSF
EFIVNKTRFS SAPVVATIII SYYLLILVGG RIMRNRQPIR LQKIFQYYNL TFSIASAILA
LLIFEQVAPA IYKHGFFFSI CNEKAWTQPL VFLYYCAYIS KFLELTDTFF LVLRKKPLQF
LHCYHHGATA VLVYTQIVGR TSISWLIIEI NLLVHVTMYY YYYLVAKGIR VPWKKWVTRF
QIVQFFADLG FIYFAVYTEV AYRLKFYKAC MGHCSGHPLA AFCGLATISS YLVLFIVFYH
NTYKKNAALK MKAKAAAATK GNSSESSKNA DLKRLSKSNA SIAEVKCNNI VTNLYPISSG
LNNEK
