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Protein

Alkylglycerol monooxygenase

Gene

AGMO

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Glyceryl-ether monooxygenase that cleaves the O-alkyl bond of ether lipids. Ether lipids are essential components of brain membranes.1 Publication

Catalytic activityi

1-alkyl-sn-glycerol + tetrahydrobiopterin + O2 = 1-O-alkyl-sn-glycerol + dihydrobiopterin + H2O.1 Publication

Cofactori

Fe cation1 Publication

Kineticsi

  1. KM=11 µM for 1-O pyrenedecyl glycerol (in presence of ALDH3A2)1 Publication
  2. KM=2.58 µM for tetrahydrobiopterin (in presence of ALDH3A2)1 Publication

    GO - Molecular functioni

    • glyceryl-ether monooxygenase activity Source: UniProtKB
    • iron ion binding Source: UniProtKB

    GO - Biological processi

    • ether lipid metabolic process Source: UniProtKB
    • fatty acid biosynthetic process Source: InterPro
    • membrane lipid metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Iron

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alkylglycerol monooxygenase (EC:1.14.16.5)
    Alternative name(s):
    Transmembrane protein 195
    Gene namesi
    Name:AGMO
    Synonyms:TMEM195
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:33784. AGMO.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei43 – 6321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei111 – 13121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei334 – 35421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei363 – 38321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei413 – 43321HelicalSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    • endoplasmic reticulum Source: UniProtKB
    • endoplasmic reticulum membrane Source: UniProtKB-SubCell
    • integral component of membrane Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi132 – 1321H → A: Loss of function; when associated with A-136; A-145; A-148; A-149; A-221; A-224 and A-225. 1 Publication
    Mutagenesisi136 – 1361H → A: Loss of function; when associated with A-132; A-145; A-148; A-149; A-221; A-224 and A-225. 1 Publication
    Mutagenesisi145 – 1451H → A: Loss of function; when associated with A-132; A-136; A-148; A-149; A-221; A-224 and A-225. 1 Publication
    Mutagenesisi148 – 1481H → A: Loss of function; when associated with A-132; A-136; A-145; A-149; A-221; A-224 and A-225. 1 Publication
    Mutagenesisi149 – 1491H → A: Loss of function; when associated with A-132; A-136; A-145; A-148; A-221; A-224 and A-225. 1 Publication
    Mutagenesisi221 – 2211H → A: Loss of function; when associated with A-132; A-136; A-145; A-148; A-149; A-224 and A-225. 1 Publication
    Mutagenesisi224 – 2241H → A: Loss of function; when associated with A-132; A-136; A-145; A-148; A-149; A-221 and A-225. 1 Publication
    Mutagenesisi225 – 2251H → A: Loss of function; when associated with A-132; A-136; A-145; A-148; A-149; A-221 and A-224. 1 Publication

    Organism-specific databases

    PharmGKBiPA162406334.

    Polymorphism and mutation databases

    BioMutaiAGMO.
    DMDMi74710656.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 445445Alkylglycerol monooxygenasePRO_0000299300Add
    BLAST

    Proteomic databases

    PaxDbiQ6ZNB7.
    PRIDEiQ6ZNB7.

    PTM databases

    PhosphoSiteiQ6ZNB7.

    Expressioni

    Gene expression databases

    BgeeiQ6ZNB7.
    CleanExiHS_TMEM195.
    ExpressionAtlasiQ6ZNB7. baseline and differential.
    GenevestigatoriQ6ZNB7.

    Organism-specific databases

    HPAiHPA040332.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000341662.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6ZNB7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi132 – 1365Histidine box-1
    Motifi145 – 1495Histidine box-2
    Motifi221 – 2255Histidine box-3

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3000.
    HOVERGENiHBG097659.
    InParanoidiQ6ZNB7.
    KOiK15537.
    OMAiFAFEIFF.
    OrthoDBiEOG7HQN81.
    PhylomeDBiQ6ZNB7.
    TreeFamiTF314881.

    Family and domain databases

    InterProiIPR006694. Fatty_acid_hydroxylase.
    [Graphical view]
    PfamiPF04116. FA_hydroxylase. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6ZNB7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKNPEAQQDV SVSQGFRMLF YTMKPSETSF QTLEEVPDYV KKATPFFISL
    60 70 80 90 100
    MLLELVVSWI LKGKPPGRLD DALTSISAGV LSRLPSLFFR SIELTSYIYI
    110 120 130 140 150
    WENYRLFNLP WDSPWTWYSA FLGVDFGYYW FHRMAHEVNI MWAGHQTHHS
    160 170 180 190 200
    SEDYNLSTAL RQSVLQIYTS WIFYSPLALF IPPSVYAVHL QFNLLYQFWI
    210 220 230 240 250
    HTEVINNLGP LELILNTPSH HRVHHGRNRY CIDKNYAGVL IIWDKIFGTF
    260 270 280 290 300
    EAENEKVVYG LTHPINTFEP IKVQFHHLFS IWTTFWATPG FFNKFSVIFK
    310 320 330 340 350
    GPGWGPGKPR LGLSEEIPEV TGKEVPFSSS SSQLLKIYTV VQFALMLAFY
    360 370 380 390 400
    EETFADTAAL SQVTLLLRVC FIILTLTSIG FLLDQRPKAA IMETLRCLMF
    410 420 430 440
    LMLYRFGHLK PLVPSLSSAF EIVFSICIAF WGVRSMKQLT SHPWK
    Length:445
    Mass (Da):51,500
    Last modified:July 5, 2004 - v1
    Checksum:iD6C8705DF1A8E043
    GO

    Sequence cautioni

    The sequence EAL24290.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti279 – 2791F → L.
    Corresponds to variant rs58564185 [ dbSNP | Ensembl ].
    VAR_062201
    Natural varianti280 – 2801S → Y.
    Corresponds to variant rs59160822 [ dbSNP | Ensembl ].
    VAR_062202

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK131284 mRNA. Translation: BAD18458.1.
    CH236948 Genomic DNA. Translation: EAL24290.1. Sequence problems.
    BC108676 mRNA. Translation: AAI08677.1.
    CCDSiCCDS34604.1.
    RefSeqiNP_001004320.1. NM_001004320.1.
    UniGeneiHs.670634.

    Genome annotation databases

    EnsembliENST00000342526; ENSP00000341662; ENSG00000187546.
    GeneIDi392636.
    KEGGihsa:392636.
    UCSCiuc003stb.1. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK131284 mRNA. Translation: BAD18458.1.
    CH236948 Genomic DNA. Translation: EAL24290.1. Sequence problems.
    BC108676 mRNA. Translation: AAI08677.1.
    CCDSiCCDS34604.1.
    RefSeqiNP_001004320.1. NM_001004320.1.
    UniGeneiHs.670634.

    3D structure databases

    ProteinModelPortaliQ6ZNB7.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9606.ENSP00000341662.

    PTM databases

    PhosphoSiteiQ6ZNB7.

    Polymorphism and mutation databases

    BioMutaiAGMO.
    DMDMi74710656.

    Proteomic databases

    PaxDbiQ6ZNB7.
    PRIDEiQ6ZNB7.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000342526; ENSP00000341662; ENSG00000187546.
    GeneIDi392636.
    KEGGihsa:392636.
    UCSCiuc003stb.1. human.

    Organism-specific databases

    CTDi392636.
    GeneCardsiGC07M015239.
    HGNCiHGNC:33784. AGMO.
    HPAiHPA040332.
    MIMi613738. gene.
    neXtProtiNX_Q6ZNB7.
    PharmGKBiPA162406334.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG3000.
    HOVERGENiHBG097659.
    InParanoidiQ6ZNB7.
    KOiK15537.
    OMAiFAFEIFF.
    OrthoDBiEOG7HQN81.
    PhylomeDBiQ6ZNB7.
    TreeFamiTF314881.

    Miscellaneous databases

    GenomeRNAii392636.
    NextBioi105330.
    PROiQ6ZNB7.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ6ZNB7.
    CleanExiHS_TMEM195.
    ExpressionAtlasiQ6ZNB7. baseline and differential.
    GenevestigatoriQ6ZNB7.

    Family and domain databases

    InterProiIPR006694. Fatty_acid_hydroxylase.
    [Graphical view]
    PfamiPF04116. FA_hydroxylase. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    2. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Eye.
    4. "Identification of the gene encoding alkylglycerol monooxygenase defines a third class of tetrahydrobiopterin-dependent enzymes."
      Watschinger K., Keller M.A., Golderer G., Hermann M., Maglione M., Sarg B., Lindner H.H., Hermetter A., Werner-Felmayer G., Konrat R., Hulo N., Werner E.R.
      Proc. Natl. Acad. Sci. U.S.A. 107:13672-13677(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-132; HIS-136; HIS-145; HIS-148; HIS-149; HIS-221; HIS-224 AND HIS-225.
    5. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiALKMO_HUMAN
    AccessioniPrimary (citable) accession number: Q6ZNB7
    Secondary accession number(s): A4D114, A6NCH5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: July 5, 2004
    Last modified: May 27, 2015
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.