ALKMO_MOUSE
ID ALKMO_MOUSE Reviewed; 447 AA.
AC Q8BS35; Q3TR15; Q8C7H5; Q8CAA6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Alkylglycerol monooxygenase;
DE EC=1.14.16.5;
DE AltName: Full=Transmembrane protein 195;
GN Name=Agmo; Synonyms=Tmem195;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 10-447 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Aorta, Cerebellum, Hypothalamus, Liver, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=20643956; DOI=10.1073/pnas.1002404107;
RA Watschinger K., Keller M.A., Golderer G., Hermann M., Maglione M., Sarg B.,
RA Lindner H.H., Hermetter A., Werner-Felmayer G., Konrat R., Hulo N.,
RA Werner E.R.;
RT "Identification of the gene encoding alkylglycerol monooxygenase defines a
RT third class of tetrahydrobiopterin-dependent enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13672-13677(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BS35-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BS35-2; Sequence=VSP_027599;
CC Name=3;
CC IsoId=Q8BS35-3; Sequence=VSP_027600;
CC -!- TISSUE SPECIFICITY: Highly expressed in lever and small intestine.
CC {ECO:0000269|PubMed:20643956}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. TMEM195 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC30271.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC34143.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AK039191; BAC30271.1; ALT_INIT; mRNA.
DR EMBL; AK040702; BAC30675.1; -; mRNA.
DR EMBL; AK050246; BAC34143.1; ALT_SEQ; mRNA.
DR EMBL; AK163155; BAE37216.1; -; mRNA.
DR CCDS; CCDS49052.1; -. [Q8BS35-1]
DR RefSeq; NP_848882.2; NM_178767.5. [Q8BS35-1]
DR AlphaFoldDB; Q8BS35; -.
DR STRING; 10090.ENSMUSP00000051441; -.
DR GlyConnect; 2117; 2 N-Linked glycans (1 site).
DR GlyGen; Q8BS35; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q8BS35; -.
DR PhosphoSitePlus; Q8BS35; -.
DR CPTAC; non-CPTAC-3447; -.
DR jPOST; Q8BS35; -.
DR MaxQB; Q8BS35; -.
DR PaxDb; Q8BS35; -.
DR PRIDE; Q8BS35; -.
DR ProteomicsDB; 296196; -. [Q8BS35-1]
DR ProteomicsDB; 296197; -. [Q8BS35-2]
DR ProteomicsDB; 296198; -. [Q8BS35-3]
DR Antibodypedia; 25207; 58 antibodies from 13 providers.
DR DNASU; 319660; -.
DR Ensembl; ENSMUST00000049874; ENSMUSP00000051441; ENSMUSG00000050103. [Q8BS35-1]
DR Ensembl; ENSMUST00000159998; ENSMUSP00000123801; ENSMUSG00000050103. [Q8BS35-2]
DR Ensembl; ENSMUST00000160390; ENSMUSP00000125639; ENSMUSG00000050103. [Q8BS35-3]
DR GeneID; 319660; -.
DR KEGG; mmu:319660; -.
DR UCSC; uc007nkg.1; mouse. [Q8BS35-1]
DR CTD; 392636; -.
DR MGI; MGI:2442495; Agmo.
DR VEuPathDB; HostDB:ENSMUSG00000050103; -.
DR eggNOG; KOG0872; Eukaryota.
DR GeneTree; ENSGT00440000033807; -.
DR HOGENOM; CLU_033631_2_1_1; -.
DR InParanoid; Q8BS35; -.
DR OMA; FMPTGWR; -.
DR OrthoDB; 1446475at2759; -.
DR PhylomeDB; Q8BS35; -.
DR TreeFam; TF314881; -.
DR Reactome; R-MMU-75109; Triglyceride biosynthesis.
DR BioGRID-ORCS; 319660; 3 hits in 75 CRISPR screens.
DR PRO; PR:Q8BS35; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BS35; protein.
DR Bgee; ENSMUSG00000050103; Expressed in urinary bladder urothelium and 145 other tissues.
DR ExpressionAtlas; Q8BS35; baseline and differential.
DR Genevisible; Q8BS35; MM.
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 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Iron; Lipid metabolism;
KW Membrane; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..447
FT /note="Alkylglycerol monooxygenase"
FT /id="PRO_0000299301"
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 340..360
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 119..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"
FT VAR_SEQ 422..447
FT /note="IFFSVCIAFWGVRSITQLTSGSWKKP -> IPQLSVLTFVVT (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027599"
FT VAR_SEQ 422..447
FT /note="IFFSVCIAFWGVRSITQLTSGSWKKP -> GWCTEVWSSALPPS (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027600"
SQ SEQUENCE 447 AA; 51778 MW; 6712E58FC3FD18FD CRC64;
MRSPGAQDNV SVSQGMRAMF YMMEPSETAF QTVEEVPDYV KKATPFFIFL ILLELVISWI
LKGKPSGRLD DALTSISAGV VSRLPSLFFR SLEVTSYIYI WENYRLLELP WDSTWTWYFT
FLGVDFGYYW FHRMAHEINI FWAAHQAHHS SEDYNLSTAL RQSVLQQYSS WVFYCPLALF
IPPSVFAVHI QFNLLYQFWI HTEIIRTLGP LEVILNTPSH HRVHHGRNRY CIDKNYAGTL
IIWDRIFGTF EAENEQVIYG LTHPIGTFEP FNVQFHHLLY IWTTFWTTPG FCHKFSVLFK
GPGWGPGKPR LGLSEEIPEV TGQEVPFSSS ASQLLKIYTV LQFAVMLAFY EETFANTAVL
SQVTLLLRIF FFILTLTSIG FLLDQRSKAA TMETFRCLLF LTLHRFGHLK PLIPSLSFAF
EIFFSVCIAF WGVRSITQLT SGSWKKP
