ID   ALKMO_RAT               Reviewed;         447 AA.
AC   A0JPQ8;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Alkylglycerol monooxygenase;
DE            EC=1.14.16.5;
DE   AltName: Full=Transmembrane protein 195;
GN   Name=Agmo; Synonyms=Tmem195;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Glyceryl-ether monooxygenase that cleaves the O-alkyl bond of
CC       ether lipids. Ether lipids are essential components of brain membranes
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + 1-O-(1,2-
CC         saturated-alkyl)-sn-glycerol + O2 = (6R)-L-erythro-6,7-
CC         dihydrobiopterin + a 1-(1-hydroxyalkyl)-sn-glycerol + H2O;
CC         Xref=Rhea:RHEA:36255, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:43120, ChEBI:CHEBI:59560, ChEBI:CHEBI:73418,
CC         ChEBI:CHEBI:83957; EC=1.14.16.5;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sterol desaturase family. TMEM195 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC127545; AAI27546.1; -; mRNA.
DR   RefSeq; NP_001129371.1; NM_001135899.1.
DR   AlphaFoldDB; A0JPQ8; -.
DR   SMR; A0JPQ8; -.
DR   STRING; 10116.ENSRNOP00000029816; -.
DR   PhosphoSitePlus; A0JPQ8; -.
DR   PaxDb; A0JPQ8; -.
DR   PeptideAtlas; A0JPQ8; -.
DR   PRIDE; A0JPQ8; -.
DR   Ensembl; ENSRNOT00000032108; ENSRNOP00000029816; ENSRNOG00000023116.
DR   GeneID; 362732; -.
DR   KEGG; rno:362732; -.
DR   UCSC; RGD:1312038; rat.
DR   CTD; 392636; -.
DR   RGD; 1312038; Agmo.
DR   eggNOG; KOG0872; Eukaryota.
DR   GeneTree; ENSGT00440000033807; -.
DR   HOGENOM; CLU_033631_2_1_1; -.
DR   InParanoid; A0JPQ8; -.
DR   OMA; FMPTGWR; -.
DR   OrthoDB; 1446475at2759; -.
DR   PhylomeDB; A0JPQ8; -.
DR   TreeFam; TF314881; -.
DR   BioCyc; MetaCyc:MON-13403; -.
DR   Reactome; R-RNO-75109; Triglyceride biosynthesis.
DR   PRO; PR:A0JPQ8; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000023116; Expressed in liver and 16 other tissues.
DR   Genevisible; A0JPQ8; RN.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050479; F:glyceryl-ether monooxygenase activity; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR   GO; GO:0046485; P:ether lipid metabolic process; ISS:UniProtKB.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   GO; GO:0006643; P:membrane lipid metabolic process; ISS:UniProtKB.
DR   InterPro; IPR006694; Fatty_acid_hydroxylase.
DR   Pfam; PF04116; FA_hydroxylase; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Iron; Lipid metabolism; Membrane; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..447
FT                   /note="Alkylglycerol monooxygenase"
FT                   /id="PRO_0000299302"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          118..249
FT                   /note="Fatty acid hydroxylase"
FT                   /evidence="ECO:0000255"
FT   MOTIF           132..136
FT                   /note="Histidine box-1"
FT   MOTIF           145..149
FT                   /note="Histidine box-2"
FT   MOTIF           221..225
FT                   /note="Histidine box-3"
SQ   SEQUENCE   447 AA;  51698 MW;  5920D097F0D99EB0 CRC64;
     MRNPGAQDNV SVSQGMRAMF YMMKPSETAF QTVEEVPDYV KKATPFFIFL ILLELVVSWI
     LKGKPSGRLD DILTSMSAGV VSRLPNLFFR SLEVTSYIYI WENYRVCELP WDSPWTWYLT
     FLGVDFGYYW FHRMAHEINI IWAAHQAHHS SEDYNLSTAL RQSVLQQYSS WVFYCPLALF
     VPPSVFAVHI QFNLLYQFWI HTEVIRTLGP LELVLNTPSH HRVHHGRNRY CIDKNYAGTL
     IIWDRIFGTF EAENEQVIYG LTHPIGTFEP FKVQFHHLLY IWTTFWATPG FCHKFSVLFK
     GPGWGPGKPR LGLSEEIPEV TGQEVPFTSS ASQFLKIYAV LQFAVMLVFY EETFANTAVL
     SQVTILLRIC FIILTLTSIG FLLDQRPKAA IVETLRCLLF LTLYRFGHLK PLIESLSFAF
     EIFFSVCIAF WGVRSITHLA SGSWKKP