ID ALKMO_HUMAN Reviewed; 445 AA. AC Q6ZNB7; A4D114; A6NCH5; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 24-JAN-2024, entry version 132. DE RecName: Full=Alkylglycerol monooxygenase; DE EC=1.14.16.5 {ECO:0000269|PubMed:20643956}; DE AltName: Full=Transmembrane protein 195; GN Name=AGMO; Synonyms=TMEM195; 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; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; 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). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-132; HIS-136; HIS-145; RP HIS-148; HIS-149; HIS-221; HIS-224 AND HIS-225. 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). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Glyceryl-ether monooxygenase that cleaves the O-alkyl bond of CC ether lipids. Ether lipids are essential components of brain membranes. CC {ECO:0000269|PubMed:20643956}. 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 Evidence={ECO:0000269|PubMed:20643956}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000305|PubMed:20643956}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=11 uM for 1-O pyrenedecyl glycerol (in presence of ALDH3A2) CC {ECO:0000269|PubMed:20643956}; CC KM=2.58 uM for tetrahydrobiopterin (in presence of ALDH3A2) CC {ECO:0000269|PubMed:20643956}; CC -!- INTERACTION: CC Q6ZNB7; Q13520: AQP6; NbExp=3; IntAct=EBI-18509181, EBI-13059134; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:20643956}; Multi-pass membrane protein CC {ECO:0000269|PubMed:20643956}. CC -!- SIMILARITY: Belongs to the sterol desaturase family. TMEM195 subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=EAL24290.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK131284; BAD18458.1; -; mRNA. DR EMBL; CH236948; EAL24290.1; ALT_SEQ; Genomic_DNA. DR EMBL; BC108676; AAI08677.1; -; mRNA. DR CCDS; CCDS34604.1; -. DR RefSeq; NP_001004320.1; NM_001004320.1. DR AlphaFoldDB; Q6ZNB7; -. DR BioGRID; 134295; 1. DR IntAct; Q6ZNB7; 2. DR STRING; 9606.ENSP00000341662; -. DR SwissLipids; SLP:000000633; -. DR iPTMnet; Q6ZNB7; -. DR PhosphoSitePlus; Q6ZNB7; -. DR BioMuta; AGMO; -. DR DMDM; 74710656; -. DR MassIVE; Q6ZNB7; -. DR PaxDb; 9606-ENSP00000341662; -. DR PeptideAtlas; Q6ZNB7; -. DR ProteomicsDB; 68010; -. DR TopDownProteomics; Q6ZNB7; -. DR Antibodypedia; 25207; 62 antibodies from 13 providers. DR DNASU; 392636; -. DR Ensembl; ENST00000342526.8; ENSP00000341662.3; ENSG00000187546.14. DR GeneID; 392636; -. DR KEGG; hsa:392636; -. DR MANE-Select; ENST00000342526.8; ENSP00000341662.3; NM_001004320.2; NP_001004320.1. DR AGR; HGNC:33784; -. DR CTD; 392636; -. DR DisGeNET; 392636; -. DR GeneCards; AGMO; -. DR HGNC; HGNC:33784; AGMO. DR HPA; ENSG00000187546; Tissue enriched (liver). DR MIM; 613738; gene. DR neXtProt; NX_Q6ZNB7; -. DR OpenTargets; ENSG00000187546; -. DR PharmGKB; PA162406334; -. DR VEuPathDB; HostDB:ENSG00000187546; -. DR eggNOG; KOG0872; Eukaryota. DR GeneTree; ENSGT00440000033807; -. DR HOGENOM; CLU_033631_2_1_1; -. DR InParanoid; Q6ZNB7; -. DR OMA; FMPTGWR; -. DR OrthoDB; 2486271at2759; -. DR PhylomeDB; Q6ZNB7; -. DR TreeFam; TF314881; -. DR BRENDA; 1.14.16.5; 2681. DR PathwayCommons; Q6ZNB7; -. DR Reactome; R-HSA-75109; Triglyceride biosynthesis. DR SignaLink; Q6ZNB7; -. DR BioGRID-ORCS; 392636; 10 hits in 1155 CRISPR screens. DR ChiTaRS; AGMO; human. DR GenomeRNAi; 392636; -. DR Pharos; Q6ZNB7; Tbio. DR PRO; PR:Q6ZNB7; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q6ZNB7; Protein. DR Bgee; ENSG00000187546; Expressed in liver and 91 other cell types or tissues. DR ExpressionAtlas; Q6ZNB7; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0050479; F:glyceryl-ether monooxygenase activity; IDA:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IMP:UniProtKB. DR GO; GO:0046485; P:ether lipid metabolic process; IDA:UniProtKB. DR GO; GO:0006643; P:membrane lipid metabolic process; IDA:UniProtKB. DR GO; GO:0019432; P:triglyceride biosynthetic process; TAS:Reactome. DR InterPro; IPR006694; Fatty_acid_hydroxylase. DR PANTHER; PTHR21624:SF1; ALKYLGLYCEROL MONOOXYGENASE; 1. DR PANTHER; PTHR21624; STEROL DESATURASE-RELATED PROTEIN; 1. DR Pfam; PF04116; FA_hydroxylase; 1. PE 1: Evidence at protein level; KW Endoplasmic reticulum; Iron; Lipid metabolism; Membrane; Oxidoreductase; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..445 FT /note="Alkylglycerol monooxygenase" FT /id="PRO_0000299300" FT TRANSMEM 43..63 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 111..131 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 120..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 VARIANT 279 FT /note="F -> L (in dbSNP:rs58564185)" FT /id="VAR_062201" FT VARIANT 280 FT /note="S -> Y (in dbSNP:rs59160822)" FT /id="VAR_062202" FT MUTAGEN 132 FT /note="H->A: Loss of function; when associated with A-136; FT A-145; A-148; A-149; A-221; A-224 and A-225." FT /evidence="ECO:0000269|PubMed:20643956" FT MUTAGEN 136 FT /note="H->A: Loss of function; when associated with A-132; FT A-145; A-148; A-149; A-221; A-224 and A-225." FT /evidence="ECO:0000269|PubMed:20643956" FT MUTAGEN 145 FT /note="H->A: Loss of function; when associated with A-132; FT A-136; A-148; A-149; A-221; A-224 and A-225." FT /evidence="ECO:0000269|PubMed:20643956" FT MUTAGEN 148 FT /note="H->A: Loss of function; when associated with A-132; FT A-136; A-145; A-149; A-221; A-224 and A-225." FT /evidence="ECO:0000269|PubMed:20643956" FT MUTAGEN 149 FT /note="H->A: Loss of function; when associated with A-132; FT A-136; A-145; A-148; A-221; A-224 and A-225." FT /evidence="ECO:0000269|PubMed:20643956" FT MUTAGEN 221 FT /note="H->A: Loss of function; when associated with A-132; FT A-136; A-145; A-148; A-149; A-224 and A-225." FT /evidence="ECO:0000269|PubMed:20643956" FT MUTAGEN 224 FT /note="H->A: Loss of function; when associated with A-132; FT A-136; A-145; A-148; A-149; A-221 and A-225." FT /evidence="ECO:0000269|PubMed:20643956" FT MUTAGEN 225 FT /note="H->A: Loss of function; when associated with A-132; FT A-136; A-145; A-148; A-149; A-221 and A-224." FT /evidence="ECO:0000269|PubMed:20643956" SQ SEQUENCE 445 AA; 51500 MW; D6C8705DF1A8E043 CRC64; MKNPEAQQDV SVSQGFRMLF YTMKPSETSF QTLEEVPDYV KKATPFFISL MLLELVVSWI LKGKPPGRLD DALTSISAGV LSRLPSLFFR SIELTSYIYI WENYRLFNLP WDSPWTWYSA FLGVDFGYYW FHRMAHEVNI MWAGHQTHHS SEDYNLSTAL RQSVLQIYTS WIFYSPLALF IPPSVYAVHL QFNLLYQFWI HTEVINNLGP LELILNTPSH HRVHHGRNRY CIDKNYAGVL IIWDKIFGTF EAENEKVVYG LTHPINTFEP IKVQFHHLFS IWTTFWATPG FFNKFSVIFK GPGWGPGKPR LGLSEEIPEV TGKEVPFSSS SSQLLKIYTV VQFALMLAFY EETFADTAAL SQVTLLLRVC FIILTLTSIG FLLDQRPKAA IMETLRCLMF LMLYRFGHLK PLVPSLSSAF EIVFSICIAF WGVRSMKQLT SHPWK //