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Q6ZNB7 (ALKMO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alkylglycerol monooxygenase

EC=1.14.16.5
Alternative name(s):
Transmembrane protein 195
Gene names
Name:AGMO
Synonyms:TMEM195
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Glyceryl-ether monooxygenase that cleaves the O-alkyl bond of ether lipids. Ether lipids are essential components of brain membranes. Ref.4

Catalytic activity

1-alkyl-sn-glycerol + tetrahydrobiopterin + O2 = 1-O-alkyl-sn-glycerol + dihydrobiopterin + H2O. Ref.4

Cofactor

Iron Probable. Ref.4

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.4.

Sequence similarities

Belongs to the sterol desaturase family. TMEM195 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=11 µM for 1-O pyrenedecyl glycerol (in presence of ALDH3A2) Ref.4

KM=2.58 µM for tetrahydrobiopterin (in presence of ALDH3A2)

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Alkylglycerol monooxygenase
PRO_0000299300

Regions

Transmembrane43 – 6321Helical; Potential
Transmembrane111 – 13121Helical; Potential
Transmembrane334 – 35421Helical; Potential
Transmembrane363 – 38321Helical; Potential
Transmembrane413 – 43321Helical; Potential
Motif132 – 1365Histidine box-1
Motif145 – 1495Histidine box-2
Motif221 – 2255Histidine box-3

Natural variations

Natural variant2791F → L.
Corresponds to variant rs58564185 [ dbSNP | Ensembl ].
VAR_062201
Natural variant2801S → Y.
Corresponds to variant rs59160822 [ dbSNP | Ensembl ].
VAR_062202

Experimental info

Mutagenesis1321H → A: Loss of function; when associated with A-136; A-145; A-148; A-149; A-221; A-224 and A-225. Ref.4
Mutagenesis1361H → A: Loss of function; when associated with A-132; A-145; A-148; A-149; A-221; A-224 and A-225. Ref.4
Mutagenesis1451H → A: Loss of function; when associated with A-132; A-136; A-148; A-149; A-221; A-224 and A-225. Ref.4
Mutagenesis1481H → A: Loss of function; when associated with A-132; A-136; A-145; A-149; A-221; A-224 and A-225. Ref.4
Mutagenesis1491H → A: Loss of function; when associated with A-132; A-136; A-145; A-148; A-221; A-224 and A-225. Ref.4
Mutagenesis2211H → A: Loss of function; when associated with A-132; A-136; A-145; A-148; A-149; A-224 and A-225. Ref.4
Mutagenesis2241H → A: Loss of function; when associated with A-132; A-136; A-145; A-148; A-149; A-221 and A-225. Ref.4
Mutagenesis2251H → A: Loss of function; when associated with A-132; A-136; A-145; A-148; A-149; A-221 and A-224. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q6ZNB7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: D6C8705DF1A8E043

FASTA44551,500
        10         20         30         40         50         60 
MKNPEAQQDV SVSQGFRMLF YTMKPSETSF QTLEEVPDYV KKATPFFISL MLLELVVSWI 

        70         80         90        100        110        120 
LKGKPPGRLD DALTSISAGV LSRLPSLFFR SIELTSYIYI WENYRLFNLP WDSPWTWYSA 

       130        140        150        160        170        180 
FLGVDFGYYW FHRMAHEVNI MWAGHQTHHS SEDYNLSTAL RQSVLQIYTS WIFYSPLALF 

       190        200        210        220        230        240 
IPPSVYAVHL QFNLLYQFWI HTEVINNLGP LELILNTPSH HRVHHGRNRY CIDKNYAGVL 

       250        260        270        280        290        300 
IIWDKIFGTF EAENEKVVYG LTHPINTFEP IKVQFHHLFS IWTTFWATPG FFNKFSVIFK 

       310        320        330        340        350        360 
GPGWGPGKPR LGLSEEIPEV TGKEVPFSSS SSQLLKIYTV VQFALMLAFY EETFADTAAL 

       370        380        390        400        410        420 
SQVTLLLRVC FIILTLTSIG FLLDQRPKAA IMETLRCLMF LMLYRFGHLK PLVPSLSSAF 

       430        440 
EIVFSICIAF WGVRSMKQLT SHPWK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK131284 mRNA. Translation: BAD18458.1.
CH236948 Genomic DNA. Translation: EAL24290.1. Sequence problems.
BC108676 mRNA. Translation: AAI08677.1.
RefSeqNP_001004320.1. NM_001004320.1.
UniGeneHs.670634.

3D structure databases

ProteinModelPortalQ6ZNB7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000341662.

PTM databases

PhosphoSiteQ6ZNB7.

Polymorphism databases

DMDM74710656.

Proteomic databases

PaxDbQ6ZNB7.
PRIDEQ6ZNB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342526; ENSP00000341662; ENSG00000187546.
GeneID392636.
KEGGhsa:392636.
UCSCuc003stb.1. human.

Organism-specific databases

CTD392636.
GeneCardsGC07M015239.
HGNCHGNC:33784. AGMO.
HPAHPA040332.
MIM613738. gene.
neXtProtNX_Q6ZNB7.
PharmGKBPA162406334.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3000.
HOVERGENHBG097659.
InParanoidQ6ZNB7.
KOK15537.
OMAQGFRMLF.
OrthoDBEOG7HQN81.
PhylomeDBQ6ZNB7.
TreeFamTF314881.

Gene expression databases

BgeeQ6ZNB7.
CleanExHS_TMEM195.
GenevestigatorQ6ZNB7.

Family and domain databases

InterProIPR006694. Fatty_acid_hydroxylase.
[Graphical view]
PfamPF04116. FA_hydroxylase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi392636.
NextBio105330.
PROQ6ZNB7.
SOURCESearch...

Entry information

Entry nameALKMO_HUMAN
AccessionPrimary (citable) accession number: Q6ZNB7
Secondary accession number(s): A4D114, A6NCH5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM