FACR2_BOVIN
ID FACR2_BOVIN Reviewed; 515 AA.
AC Q0P5J1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Fatty acyl-CoA reductase 2 {ECO:0000250|UniProtKB:Q96K12};
DE EC=1.2.1.84 {ECO:0000250|UniProtKB:Q96K12};
GN Name=FAR2 {ECO:0000250|UniProtKB:Q96K12};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reduction of saturated but not unsaturated C16
CC or C18 fatty acyl-CoA to fatty alcohols. A lower activity can be
CC observed with shorter fatty acyl-CoA substrates. It may play a role in
CC the production of ether lipids/plasmalogens and wax monoesters which
CC synthesis requires fatty alcohols as substrates.
CC {ECO:0000250|UniProtKB:Q96K12}.
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:0000250|UniProtKB:Q96K12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52717;
CC Evidence={ECO:0000250|UniProtKB:Q96K12};
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:0000250|UniProtKB:Q96K12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36316;
CC Evidence={ECO:0000250|UniProtKB:Q96K12};
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:0000250|UniProtKB:Q7TNT2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36320;
CC Evidence={ECO:0000250|UniProtKB:Q7TNT2};
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:Q96K12}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96K12}.
CC -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC119968; AAI19969.1; -; mRNA.
DR RefSeq; NP_001069490.1; NM_001076022.1.
DR RefSeq; XP_005206959.1; XM_005206902.3.
DR RefSeq; XP_010803676.1; XM_010805374.2.
DR RefSeq; XP_010803677.1; XM_010805375.2.
DR AlphaFoldDB; Q0P5J1; -.
DR STRING; 9913.ENSBTAP00000014725; -.
DR PaxDb; Q0P5J1; -.
DR PRIDE; Q0P5J1; -.
DR Ensembl; ENSBTAT00000014725; ENSBTAP00000014725; ENSBTAG00000011095.
DR GeneID; 534380; -.
DR KEGG; bta:534380; -.
DR CTD; 55711; -.
DR VEuPathDB; HostDB:ENSBTAG00000011095; -.
DR VGNC; VGNC:28864; FAR2.
DR eggNOG; KOG1221; Eukaryota.
DR GeneTree; ENSGT00390000006367; -.
DR HOGENOM; CLU_024661_0_0_1; -.
DR InParanoid; Q0P5J1; -.
DR OMA; WLEYTEN; -.
DR OrthoDB; 815047at2759; -.
DR TreeFam; TF313011; -.
DR Reactome; R-BTA-9640463; Wax biosynthesis.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000011095; Expressed in zone of skin and 97 other tissues.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0102965; F:alcohol-forming fatty acyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0080019; F:fatty-acyl-CoA reductase (alcohol-forming) activity; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IBA:GO_Central.
DR CDD; cd09071; FAR_C; 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; PTHR11011; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF03015; Sterile; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW Peroxisome; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..515
FT /note="Fatty acyl-CoA reductase 2"
FT /id="PRO_0000261400"
FT TOPO_DOM 1..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96K12"
FT TRANSMEM 466..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..515
FT /note="Peroxisomal"
FT /evidence="ECO:0000250|UniProtKB:Q96K12"
SQ SEQUENCE 515 AA; 59077 MW; F27A2F66AD1F4C64 CRC64;
MSMIAAFYGG KSILITGATG FMGKVLMEKL FRTSPDLKVV YILVRPKQGQ TLQQRVFQIL
DSKLFEKVKE VCPNVHEKIR AISADLNQND FAISKEDMKE LLSHTNIIFH CAATVRFDDH
LRHAVQLNVT ATQQLLLMAS QMPKLEAFIH ISTAFSNCNL KHIDEVVYPC PVEPKKIIDS
MEWLDDAIID EITPKLIGDW PNTYTYTKAL GEVVVQQEGG NLNIAIIRPS IMGATWQEPF
PGWVDNLNGP SGLIIAAGKG FLRSIRATPM AVADLIPADT VVNLTLAVGW YTAVHRPKST
LVYHCTSGNL NPCNWGKMGL QVLATFEKIP FERAFRRPNA DFTTNNITTH YWNAVSHRAP
AIIYDFYLRL TGRKPRMTKL MNRLLRTLSM LEYFVNRSWE WSTYNTEMLM SELSPEDQRV
FNFDVRQLNW LEYIENYVLG VKKYLLKEDM AGIPEAKQHL KRLRNIHYLF NTALFLIAWR
LLIARSQVAR NVWFFIVSFC YKFLSYFRAS STLNV
