TECR_DICDI
ID TECR_DICDI Reviewed; 300 AA.
AC Q55C17;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Very-long-chain enoyl-CoA reductase {ECO:0000305};
DE EC=1.3.1.93 {ECO:0000250|UniProtKB:Q9NZ01};
DE AltName: Full=Synaptic glycoprotein SC2-like protein;
DE AltName: Full=Trans-2,3-enoyl-CoA reductase;
DE Short=TER;
GN Name=gpsn2; ORFNames=DDB_G0270270;
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).
CC -!- FUNCTION: Catalyzes the last of the four reactions of the long-chain
CC fatty acids elongation cycle. This endoplasmic reticulum-bound
CC enzymatic process, allows the addition of 2 carbons to the chain of
CC long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme
CC reduces the trans-2,3-enoyl-CoA fatty acid intermediate to an acyl-CoA
CC that can be further elongated by entering a new cycle of elongation.
CC Thereby, it participates in the production of VLCFAs of different chain
CC lengths that are involved in multiple biological processes as
CC precursors of membrane lipids and lipid mediators.
CC {ECO:0000250|UniProtKB:Q9NZ01}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain 2,3-saturated fatty acyl-CoA + NADP(+) = a
CC very-long-chain (2E)-enoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:14473,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:83724, ChEBI:CHEBI:83728; EC=1.3.1.93;
CC Evidence={ECO:0000250|UniProtKB:Q9NZ01};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q9NZ01}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NZ01}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9NZ01}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72485.1; -; Genomic_DNA.
DR RefSeq; XP_646664.1; XM_641572.1.
DR AlphaFoldDB; Q55C17; -.
DR SMR; Q55C17; -.
DR STRING; 44689.DDB0237530; -.
DR PaxDb; Q55C17; -.
DR EnsemblProtists; EAL72485; EAL72485; DDB_G0270270.
DR GeneID; 8617636; -.
DR KEGG; ddi:DDB_G0270270; -.
DR dictyBase; DDB_G0270270; gpsn2.
DR eggNOG; KOG1639; Eukaryota.
DR HOGENOM; CLU_059260_0_0_1; -.
DR InParanoid; Q55C17; -.
DR OMA; TVFVIEY; -.
DR PhylomeDB; Q55C17; -.
DR Reactome; R-DDI-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q55C17; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0102758; F:very-long-chain enoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR InterPro; IPR039357; SRD5A/TECR.
DR PANTHER; PTHR10556; PTHR10556; 1.
DR Pfam; PF02544; Steroid_dh; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Glycoprotein; Lipid biosynthesis; Lipid metabolism; Membrane; NADP;
KW Oxidoreductase; Reference proteome; Steroid biosynthesis; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..300
FT /note="Very-long-chain enoyl-CoA reductase"
FT /id="PRO_0000328151"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 300 AA; 34378 MW; B9C17B6D31C118C9 CRC64;
MVDIKVVSQR SKKEVGSFST SSSTTVGELK KQISSKTRLG TERIRLAVPS KTSKLPNAFE
ALGKDSDLVS KHVGADSTLY FKDLGPQISW SLVFICEYAG PLFVYPIFYF LSNLIYGTDS
PKSFAQKVAL VCYSLHYIKR IYETIFVHRF SHGTMPIFNL FKNCSYYWGC TAMVSYFVNH
PLYTEAPIER VYLGLGLWII GEVFNYICHI QLRNLRPAGS TERKIPRGLL FEFVSCPNYT
VEILSWIGFS ILTQTLTSWI FALMGAAQMW IWAVGKHRRY RKEFGDKYPK SRKILIPFLL
