ID H0ZNR6_TAEGU Unreviewed; 527 AA.
AC H0ZNR6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN Name=FAR2 {ECO:0000313|Ensembl:ENSTGUP00000012243.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000012243.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000012243.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000012243.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
CC {ECO:0000256|RuleBase:RU363097}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 NADPH + octadecanoyl-CoA = CoA + 2 NADP(+) +
CC octadecan-1-ol; Xref=Rhea:RHEA:36319, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32154, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.84;
CC Evidence={ECO:0000256|ARBA:ARBA00000278};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36320;
CC Evidence={ECO:0000256|ARBA:ARBA00000278};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hexadecanoyl-CoA + 2 NADPH = CoA + hexadecan-1-ol + 2
CC NADP(+); Xref=Rhea:RHEA:36315, ChEBI:CHEBI:15378, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.84;
CC Evidence={ECO:0000256|ARBA:ARBA00000203};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36316;
CC Evidence={ECO:0000256|ARBA:ARBA00000203};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain
CC primary fatty alcohol + CoA + 2 NADP(+); Xref=Rhea:RHEA:52716,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:77396, ChEBI:CHEBI:83139; EC=1.2.1.84;
CC Evidence={ECO:0000256|ARBA:ARBA00000233};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52717;
CC Evidence={ECO:0000256|ARBA:ARBA00000233};
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000256|ARBA:ARBA00004549}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004549}.
CC -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC {ECO:0000256|ARBA:ARBA00005928, ECO:0000256|RuleBase:RU363097}.
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DR AlphaFoldDB; H0ZNR6; -.
DR Ensembl; ENSTGUT00000012377.2; ENSTGUP00000012243.2; ENSTGUG00000011875.2.
DR GeneTree; ENSGT00390000006367; -.
DR HOGENOM; CLU_024661_0_2_1; -.
DR Proteomes; UP000007754; Chromosome 1A.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0102965; F:alcohol-forming long-chain fatty acyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0080019; F:alcohol-forming very long-chain fatty acyl-CoA reductase activity; IEA:InterPro.
DR GO; GO:1901568; P:fatty acid derivative metabolic process; IEA:UniProt.
DR CDD; cd05236; FAR-N_SDR_e; 1.
DR CDD; cd09071; FAR_C; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR026055; FAR.
DR InterPro; IPR033640; FAR_C.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR11011:SF117; FATTY ACYL-COA REDUCTASE 2; 1.
DR PANTHER; PTHR11011; MALE STERILITY PROTEIN 2-RELATED; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF03015; Sterile; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU363097};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU363097}; Membrane {ECO:0000256|RuleBase:RU363097};
KW NADP {ECO:0000256|RuleBase:RU363097};
KW Oxidoreductase {ECO:0000256|RuleBase:RU363097};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW Transmembrane {ECO:0000256|RuleBase:RU363097};
KW Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT TRANSMEM 466..483
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 15..284
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 357..448
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 527 AA; 60539 MW; 79C6F69F83AAEBDF CRC64;
MSSVSAYYNG KTVLITGATG FMGKVLVEKL LRSSPEVKAV YILVRPKAGQ SMQERVANML
KCKVFDRVRE DCPNFHEKIK PINAELTQPK LAISAEDEEE LLTRVNVVFH CAATVRFDEP
LKHALQLNVM GTQRLLELAR QMRNLEAFIH ISTAYANCIR KCIEEIIYPP PAEPQKLFDL
VEWLDESIIQ DITPKLLGEW PNTYTYTKAL SEYLIQQEKG NLNIAIIRPS IVGASWHEPF
PGWIDNFNGT SGIFIAAGKG ILRTVIANNE AVADMIPVDV AINLTLAAGW YTAVHRPKNL
LVYNCTTGGI NPFFWGEMGQ YVMSTFKRNP LEQAFRTPNA HMTSSYLINQ YWITVSHKAP
AILYDLYMRL TGRKPRMMKI INRLHKSMTL LQYFSTQSWS WSSDNMNMLM THLNTEDKKL
YNFDVRQLHW SEYIESYCIG AKKYLLNEDM AGIPAAKQHL RKLRNIRYAF NTTLLVIIWR
IFIARSQMAR NIWYFVVSLC YKQKNPLPPT AAGTYCTRLH AHLFNFN
//
