ID Q9NUX8_HUMAN Unreviewed; 515 AA.
AC Q9NUX8;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAA91983.1};
RN [1] {ECO:0000313|EMBL:BAA91983.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Placenta {ECO:0000313|EMBL:BAA91983.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M.,
RA Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S.,
RA Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S.,
RA Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H.,
RA Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M.,
RA Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M.,
RA Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y.,
RA Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N.,
RA Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S.,
RA Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T.,
RA Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M.,
RA Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y.,
RA Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y.,
RA Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T.,
RA Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
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 EMBL; AK001927; BAA91983.1; -; mRNA.
DR RefSeq; NP_001258712.1; NM_001271783.1.
DR RefSeq; NP_001258713.1; NM_001271784.1.
DR RefSeq; NP_060569.3; NM_018099.4.
DR AlphaFoldDB; Q9NUX8; -.
DR PeptideAtlas; Q9NUX8; -.
DR DNASU; 55711; -.
DR GeneID; 55711; -.
DR KEGG; hsa:55711; -.
DR CTD; 55711; -.
DR OrthoDB; 1434498at2759; -.
DR BioGRID-ORCS; 55711; 164 hits in 1163 CRISPR screens.
DR GenomeRNAi; 55711; -.
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 2: Evidence at transcript level;
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 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 TRANSMEM 492..509
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 15..285
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 515 AA; 59339 MW; D31EA2DA66A727CA CRC64;
MSTIAAFYGG KSILITGATG FLGKVLMEKL FRTSPDLKVI YILVRPKAGQ TLQQGVFQIL
DSKLFEKVKE VCPNVHEKIR AIYADLNQND FAISKEDMQE LLSCTNIIFH CAATVRFDDT
LRHAVQLNVT ATRQLLLMAS QMPKLEAFIH ISTAYSNCNL KHIDEVIYPC PVEPKKIIDS
LEWLDDAIID EITPKLIRDW PNIYTYTKAL GEMVVQQESR NLNIAIIRPS IVGATWQEPF
PGWVDNINGP NGIIIATGKG FLRAIKATPM AVADVIPVDT VVNLMLAVGW YTAVHRPKST
LVYHITSGNM NPCNWHKMGV QVLATFEKIP FERPFRRPNA NFTSNSFTSQ YWNAVSHRAP
AIIYDCYLRL TGRKPRMTKL MNRLLRTVSM LEYFINRSWE WSTYNTEMLM SELSPEDQRV
FNFDVRQLNW LEYIENYVLG VKKYLLKEDM AGIPKAKQRL KRLRNIHYLF NTALFLIAWR
LLIARSQMAR NVWFFIVSFC YKFLSYFRAS STLKV
//
