ID A0A096N5U6_PAPAN Unreviewed; 516 AA.
AC A0A096N5U6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 49.
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:ENSPANP00000007819.2};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000007819.2, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000007819.2, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000007819.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A096N5U6; -.
DR STRING; 9555.ENSPANP00000007819; -.
DR Ensembl; ENSPANT00000009295.4; ENSPANP00000007819.2; ENSPANG00000018372.4.
DR GeneTree; ENSGT00390000006367; -.
DR HOGENOM; CLU_024661_0_0_1; -.
DR OMA; NCILKHF; -.
DR OrthoDB; 1434498at2759; -.
DR Proteomes; UP000028761; Chromosome 9.
DR Bgee; ENSPANG00000018372; Expressed in putamen and 67 other cell types or tissues.
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:Ensembl.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IEA:Ensembl.
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:UP000028761};
KW Transmembrane {ECO:0000256|RuleBase:RU363097};
KW Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT TRANSMEM 467..484
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT TRANSMEM 493..510
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 15..283
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 358..449
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 516 AA; 59439 MW; AF873E44DBFBD8BB CRC64;
MSVIAAFYGG KSILITGATG FLGKVLMEKL FRTSPDLKVI YILVRPKAGQ TLQQRVFQIL
NSKLFEKVKE VCPNVHEKIR AIYADLNQND FAISKEDMQE LLSCTNIIFH CAATVRFDDT
LRHAVQLNVT ATRQLLLMAS QMPKLEAFIH ISTAYSNCNL KHIDEVIYPC PVEPKKIIDS
LEWLDDAIIE EIAPKLIRDW PNIYTYTKAL GEMVVQQESR NLNIAIIRPS IVGATWQEPF
PGWVDNINGP NGLIIAAGKG FLLAIKTTPM AVADLIPVDT AINLPLAVGW YAAVHRPKSM
LVYHCTSGNL NPCNWDKMGV QVLATFEIQI PLERAFRRPY ADFTTSNFTT QYWNAISHQA
PAIIYDFYLW LTGRKLRMTK VMNQILRTAS MLEYFLNRSW EWSTYNTEML MSELSPEDQR
VFNFDVRQLN WLEYIENYVL GVKKYLLKED MAGIPEAKQH LKRLRNIHYL FNTALFLIVW
RLLIARSQMA RNVWFFIVSF CYKFLSYFRA SSTLKV
//
