SRE1_DICDI
ID SRE1_DICDI Reviewed; 268 AA.
AC Q54TC9;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Elongation of fatty acids protein sre1;
DE EC=2.3.1.199;
DE AltName: Full=3-keto acyl-CoA synthase sre1;
DE AltName: Full=Protein SRE1 homolog;
DE AltName: Full=Very-long-chain 3-oxoacyl-CoA synthase sre1;
GN Name=sre1; ORFNames=DDB_G0281821;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP DEVELOPMENTAL STAGE [LARGE SCALE ANALYSIS].
RX PubMed=12796308; DOI=10.1128/ec.2.3.627-637.2003;
RA Maeda M., Sakamoto H., Iranfar N., Fuller D., Maruo T., Ogihara S.,
RA Morio T., Urushihara H., Tanaka Y., Loomis W.F.;
RT "Changing patterns of gene expression in Dictyostelium prestalk cell
RT subtypes recognized by in situ hybridization with genes from microarray
RT analyses.";
RL Eukaryot. Cell 2:627-637(2003).
RN [3]
RP INDUCTION BY STATA.
RX PubMed=15470642; DOI=10.1387/ijdb.041862ns;
RA Shimada N., Maeda M., Urushihara H., Kawata T.;
RT "Identification of new modes of Dd-STATa regulation of gene expression in
RT Dictyostelium by in situ hybridisation.";
RL Int. J. Dev. Biol. 48:679-682(2004).
CC -!- FUNCTION: Could be implicated in synthesis of very long chain fatty
CC acids. {ECO:0000250}.
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;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels in prespore cells at the
CC tipped aggregate stage, expressed in the anterior funnel cells in
CC slugs, and then become enriched in upper cup cells during culmination.
CC {ECO:0000269|PubMed:12796308}.
CC -!- INDUCTION: By STATa. {ECO:0000269|PubMed:15470642}.
CC -!- SIMILARITY: Belongs to the ELO family. {ECO:0000305}.
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DR EMBL; AAFI02000043; EAL66470.1; -; Genomic_DNA.
DR RefSeq; XP_640460.1; XM_635368.1.
DR AlphaFoldDB; Q54TC9; -.
DR SMR; Q54TC9; -.
DR STRING; 44689.DDB0214890; -.
DR PaxDb; Q54TC9; -.
DR EnsemblProtists; EAL66470; EAL66470; DDB_G0281821.
DR GeneID; 8623273; -.
DR KEGG; ddi:DDB_G0281821; -.
DR dictyBase; DDB_G0281821; eloB.
DR eggNOG; KOG3071; Eukaryota.
DR HOGENOM; CLU_048483_6_0_1; -.
DR InParanoid; Q54TC9; -.
DR OMA; TITHFQW; -.
DR PhylomeDB; Q54TC9; -.
DR PRO; PR:Q54TC9; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0009922; F:fatty acid elongase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..268
FT /note="Elongation of fatty acids protein sre1"
FT /id="PRO_0000393465"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 268 AA; 31440 MW; 06D3BFBBBAAB5A07 CRC64;
MDIVKNYLIA FDQYTANFRW ESGVTPLSSY VFPFSTSVIY VLVIFALQAI MKNKKGMVLK
GFSIIHNINL IILSFSMMSG VMYAAYQQYL EQGAFSLVCE QSSQSVQGRI GFWIYIFYLS
KYYELVDTVI LALKKKPIIF LHIFHHMAMV PVTWQWLHDQ WLVGSWWCTL VNSFIHVLMY
YYYLQTTLGN PCWFKKYITK AQIVQFLTGT AMVSYWFVIR DSEKCQAPLS PAIVSNTINS
FFIILFGKFY YDSYKSNSRR QEKLNKVE
