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Database: UniProt
Entry: A0A154PQC5_DUFNO
LinkDB: A0A154PQC5_DUFNO
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ID   A0A154PQC5_DUFNO        Unreviewed;       338 AA.
AC   A0A154PQC5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Fatty acid 2-hydroxylase {ECO:0000256|PIRNR:PIRNR005149};
DE            EC=1.-.-.- {ECO:0000256|PIRNR:PIRNR005149};
GN   ORFNames=WN55_06335 {ECO:0000313|EMBL:KZC14103.1};
OS   Dufourea novaeangliae (Sweat bee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Halictidae; Rophitinae; Dufourea.
OX   NCBI_TaxID=178035 {ECO:0000313|EMBL:KZC14103.1, ECO:0000313|Proteomes:UP000076502};
RN   [1] {ECO:0000313|EMBL:KZC14103.1, ECO:0000313|Proteomes:UP000076502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0120121106 {ECO:0000313|EMBL:KZC14103.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KZC14103.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Dufourea novaeangliae.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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=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   EMBL; KQ435037; KZC14103.1; -; Genomic_DNA.
DR   RefSeq; XP_015436875.1; XM_015581389.1.
DR   AlphaFoldDB; A0A154PQC5; -.
DR   STRING; 178035.A0A154PQC5; -.
DR   EnsemblMetazoa; XM_015581389.1; XP_015436875.1; LOC107192184.
DR   GeneID; 107192184; -.
DR   OrthoDB; 208810at2759; -.
DR   Proteomes; UP000076502; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0080132; F:fatty acid alpha-hydroxylase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
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; 2.
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|ARBA:ARBA00022824,
KW   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}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR005149};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|PIRNR:PIRNR005149};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   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:UP000076502};
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        145..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        234..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..91
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
SQ   SEQUENCE   338 AA;  39582 MW;  49483175D5DD895E CRC64;
     MKRHVKNGGD RKPIETRVVD RQPAVETTEN TFLISYRDRS YDLRKFLRYH PGGKKVLGYF
     ENRSLDKALD ENPHSRSAFH LLEDFTVNEQ EKYQEYEDLI DWNAPILGQV GKLGDQYWEW
     MNLPVNREIR LFQSNLLETI SITPWYLVPI VWIPVCIYFL YSGFNSIADD PSGNTLFQAL
     SSYILGILLW SILEYVLHRK LFHFKPPATS KLLISLHFIL HGVHHKAPFD NRRLVFPPVA
     GLSIAKLLWY LYEALFSRTM IYFIAAGTTT GYVCYDLIHY YLHHGAPRAG SYLYTMKRNH
     NYHHFSHHEL GFGISSKLWD HAFGTNICLP QLTKPIEW
//
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