ALKMO_HUMAN
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 03-AUG-2022, entry version 126.
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};
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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; Q6ZNB7; -.
DR PeptideAtlas; Q6ZNB7; -.
DR PRIDE; Q6ZNB7; -.
DR ProteomicsDB; 68010; -.
DR TopDownProteomics; Q6ZNB7; -.
DR Antibodypedia; 25207; 58 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 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; 1446475at2759; -.
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 1077 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 90 other 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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
