ID A0A2K6CP19_MACNE Unreviewed; 372 AA.
AC A0A2K6CP19;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Fatty acid 2-hydroxylase {ECO:0000256|PIRNR:PIRNR005149};
DE EC=1.-.-.- {ECO:0000256|PIRNR:PIRNR005149};
GN Name=FA2H {ECO:0000313|Ensembl:ENSMNEP00000025389.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000025389.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000025389.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes stereospecific hydroxylation of free fatty acids at
CC the C-2 position to produce (R)-2-hydroxy fatty acids, which are
CC building blocks of sphingolipids and glycosphingolipids common in
CC neural tissue and epidermis. Plays an essential role in the synthesis
CC of galactosphingolipids of the myelin sheath. Responsible for the
CC synthesis of sphingolipids and glycosphingolipids involved in the
CC formation of epidermal lamellar bodies critical for skin permeability
CC barrier. Participates in the synthesis of glycosphingolipids and a
CC fraction of type II wax diesters in sebaceous gland, specifically
CC regulating hair follicle homeostasis. Involved in the synthesis of
CC sphingolipids of plasma membrane rafts, controlling lipid raft mobility
CC and trafficking of raft-associated proteins.
CC {ECO:0000256|PIRNR:PIRNR005149}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|PIRSR:PIRSR005149-50};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRNR:PIRNR005149};
CC Note=Binds 2 Zn(2+) ions per subunit that likely form a catalytic
CC dimetal center. {ECO:0000256|PIRNR:PIRNR005149};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. SCS7 subfamily.
CC {ECO:0000256|ARBA:ARBA00005747, ECO:0000256|PIRNR:PIRNR005149}.
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DR RefSeq; XP_011755817.1; XM_011757515.1.
DR AlphaFoldDB; A0A2K6CP19; -.
DR SMR; A0A2K6CP19; -.
DR STRING; 9545.ENSMNEP00000025389; -.
DR Ensembl; ENSMNET00000049664.1; ENSMNEP00000025389.1; ENSMNEG00000036186.1.
DR GeneID; 105491281; -.
DR KEGG; mni:105491281; -.
DR CTD; 79152; -.
DR GeneTree; ENSGT00390000002142; -.
DR OMA; WTIIEYV; -.
DR OrthoDB; 208810at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000036186; Expressed in colon and 1 other cell type or tissue.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0080132; F:fatty acid alpha-hydroxylase activity; IEA:Ensembl.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032286; P:central nervous system myelin maintenance; IEA:Ensembl.
DR GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006682; P:galactosylceramide biosynthetic process; IEA:Ensembl.
DR GO; GO:0006679; P:glucosylceramide biosynthetic process; IEA:Ensembl.
DR GO; GO:0030258; P:lipid modification; IEA:Ensembl.
DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; IEA:Ensembl.
DR GO; GO:0044857; P:plasma membrane raft organization; IEA:Ensembl.
DR GO; GO:1904697; P:regulation of acinar cell proliferation; IEA:Ensembl.
DR GO; GO:0042634; P:regulation of hair cycle; IEA:Ensembl.
DR GO; GO:1904002; P:regulation of sebum secreting cell proliferation; IEA:Ensembl.
DR GO; GO:0001949; P:sebaceous gland cell differentiation; IEA:Ensembl.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR InterPro; IPR014430; Scs7.
DR PANTHER; PTHR12863:SF1; FATTY ACID 2-HYDROXYLASE; 1.
DR PANTHER; PTHR12863; FATTY ACID HYDROXYLASE; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF04116; FA_hydroxylase; 1.
DR PIRSF; PIRSF005149; IPC-B_HD; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR005149};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|PIRNR:PIRNR005149};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832,
KW ECO:0000256|PIRNR:PIRNR005149};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR005149-50};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR005149};
KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR005149};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR005149};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR005149};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR005149};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR005149};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..86
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT BINDING 43
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR005149-50"
FT BINDING 69
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR005149-50"
SQ SEQUENCE 372 AA; 42812 MW; F64EA229AA819559 CRC64;
MAPAPPPAAS FSPSEVQRRL AAGACWVRRG ARLYDLSSFV RHHPGGEQLL RARAGQDISA
DLDGPPHRHS ANARRWLEQY YVGELRGEQQ GSMENEAVAL EETQKTDPAM EPWFKVVDWD
KDLVDWQKPL LWQVGHLGEK YDEWVHQPVT RPIRLFHSDL IEGLSKTVWY SVPIIWVPLV
LYLSWSYYRT FAQGNVRLFT SFTTEYALAV PKSMFPGLFM LGIFLWSLIE YLIHRFLFHM
KPPSDSYYLI MLHFVMHGQH HKAPFDGSRL VFPPVPASLV IGVFYLCLQL ILPEAVGGTV
FAGGLLGYVL YDMTHYYLHF GSPHRGSYLY NLKAHHVKHH FAHQKSGFGI STKLWDYCFH
TLIPEKPHLK TQ
//