ELOH1_SCHPO
ID ELOH1_SCHPO Reviewed; 334 AA.
AC Q9UTF7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Putative elongation of fatty acids protein 1 {ECO:0000250|UniProtKB:P40319};
DE EC=2.3.1.199 {ECO:0000250|UniProtKB:P40319};
DE AltName: Full=3-keto acyl-CoA synthase SPAC1B2.03c {ECO:0000250|UniProtKB:P40319};
DE AltName: Full=Very-long-chain 3-oxoacyl-CoA synthase 1 {ECO:0000250|UniProtKB:P40319};
GN ORFNames=SPAC1B2.03c {ECO:0000312|PomBase:SPAC1B2.03c};
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 [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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION BY
RP 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: May be involved in the synthesis of very long chain fatty
CC acids. {ECO:0000250|UniProtKB:P40319}.
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:P40319};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ELO family. {ECO:0000305}.
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DR EMBL; CU329670; CAB61470.1; -; Genomic_DNA.
DR PIR; T50139; T50139.
DR RefSeq; NP_593930.1; NM_001019359.2.
DR AlphaFoldDB; Q9UTF7; -.
DR SMR; Q9UTF7; -.
DR BioGRID; 278963; 1.
DR STRING; 4896.SPAC1B2.03c.1; -.
DR iPTMnet; Q9UTF7; -.
DR MaxQB; Q9UTF7; -.
DR PaxDb; Q9UTF7; -.
DR PRIDE; Q9UTF7; -.
DR EnsemblFungi; SPAC1B2.03c.1; SPAC1B2.03c.1:pep; SPAC1B2.03c.
DR GeneID; 2542505; -.
DR KEGG; spo:SPAC1B2.03c; -.
DR PomBase; SPAC1B2.03c; -.
DR VEuPathDB; FungiDB:SPAC1B2.03c; -.
DR eggNOG; KOG3071; Eukaryota.
DR HOGENOM; CLU_048483_6_1_1; -.
DR InParanoid; Q9UTF7; -.
DR OMA; WVVIDIN; -.
DR PhylomeDB; Q9UTF7; -.
DR PRO; PR:Q9UTF7; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; 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:0009922; F:fatty acid elongase activity; IMP: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:0071763; P:nuclear membrane organization; IMP:PomBase.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IMP: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 1: Evidence at protein level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..334
FT /note="Putative elongation of fatty acids protein 1"
FT /id="PRO_0000316229"
FT TOPO_DOM 1..51
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P40319"
FT TRANSMEM 52..72
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P40319"
FT TRANSMEM 87..107
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..135
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P40319"
FT TRANSMEM 136..156
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P40319"
FT TRANSMEM 161..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..187
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P40319"
FT TRANSMEM 188..208
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P40319"
FT TRANSMEM 225..245
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..260
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P40319"
FT TRANSMEM 261..281
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P40319"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 334 AA; 38337 MW; D4089923F898612F CRC64;
MDLTGAHMLK IHRPSIDHPF GVDLWHLFEQ LSIKTIGWNP SEFEYIPGKT PMSQWSSVIV
SITAYYVIIL SGRAIMTNRK PLKQRRLFQL HNFILTIISG ALLALLVEEV FRNYMRNGLF
YCVCDSRHFT QRLVTLYYLN YLTKYLELMD TVFLFLKKKP LAFLHCYHHG ITALLCFTQL
LGRTSVQWGV IGLNLYVHVI MYSYYFLAAC GRRVWWKQWV TRVQIIQFVL DLILCYFGTY
SHIAFRYFPW LPHVGDCSGS LFAAFFGCGV LSSYLFLFIG FYINTYIKRG AKKNQRKAAG
KADNTSVAAA AGSEALAATT ATNASPFSAR SRKL
