Q6ZNB7 (ALKMO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alkylglycerol monooxygenase
EC=1.14.16.5

Alternative name(s):
Transmembrane protein 195

Gene names

Name:	AGMO
Synonyms:	TMEM195

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	445 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	Iron
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ether lipid metabolic process Inferred from direct assay Ref.4. Source: UniProtKB fatty acid biosynthetic process Inferred from electronic annotation. Source: InterPro membrane lipid metabolic process Inferred from direct assay Ref.4. Source: UniProtKB
Cellular_component	endoplasmic reticulum Inferred from direct assay Ref.4. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	glyceryl-ether monooxygenase activity Inferred from direct assay Ref.4. Source: UniProtKB iron ion binding Inferred from mutant phenotype Ref.4. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 445	445	Alkylglycerol monooxygenase		PRO_0000299300
Regions
	Transmembrane	43 – 63	21	Helical; Potential
	Transmembrane	111 – 131	21	Helical; Potential
	Transmembrane	334 – 354	21	Helical; Potential
	Transmembrane	363 – 383	21	Helical; Potential
	Transmembrane	413 – 433	21	Helical; Potential
	Motif	132 – 136	5	Histidine box-1
	Motif	145 – 149	5	Histidine box-2
	Motif	221 – 225	5	Histidine box-3
Natural variations
	Natural variant	279	1	F → L. Corresponds to variant rs58564185 [ dbSNP | Ensembl ].		VAR_062201
	Natural variant	280	1	S → Y. Corresponds to variant rs59160822 [ dbSNP | Ensembl ].		VAR_062202
Experimental info
	Mutagenesis	132	1	H → A: Loss of function; when associated with A-136; A-145; A-148; A-149; A-221; A-224 and A-225. Ref.4
	Mutagenesis	136	1	H → A: Loss of function; when associated with A-132; A-145; A-148; A-149; A-221; A-224 and A-225. Ref.4
	Mutagenesis	145	1	H → A: Loss of function; when associated with A-132; A-136; A-148; A-149; A-221; A-224 and A-225. Ref.4
	Mutagenesis	148	1	H → A: Loss of function; when associated with A-132; A-136; A-145; A-149; A-221; A-224 and A-225. Ref.4
	Mutagenesis	149	1	H → A: Loss of function; when associated with A-132; A-136; A-145; A-148; A-221; A-224 and A-225. Ref.4
	Mutagenesis	221	1	H → A: Loss of function; when associated with A-132; A-136; A-145; A-148; A-149; A-224 and A-225. Ref.4
	Mutagenesis	224	1	H → A: Loss of function; when associated with A-132; A-136; A-145; A-148; A-149; A-221 and A-225. Ref.4
	Mutagenesis	225	1	H → 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		Length	Mass (Da)
	Q6ZNB7 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: D6C8705DF1A8E043	FASTA	445	51,500
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
+	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.
IPI	IPI00418595.
RefSeq	NP_001004320.1. NM_001004320.1.
UniGene	Hs.670634.
3D structure databases
ProteinModelPortal	Q6ZNB7.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000341662.
PTM databases
PhosphoSite	Q6ZNB7.
Polymorphism databases
DMDM	74710656.
Proteomic databases
PaxDb	Q6ZNB7.
PRIDE	Q6ZNB7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000342526; ENSP00000341662; ENSG00000187546.
GeneID	392636.
KEGG	hsa:392636.
UCSC	uc003stb.1. human.
Organism-specific databases
CTD	392636.
GeneCards	GC07M015239.
HGNC	HGNC:33784. AGMO.
HPA	HPA040332.
MIM	613738. gene.
neXtProt	NX_Q6ZNB7.
PharmGKB	PA162406334.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG3000.
HOVERGEN	HBG097659.
InParanoid	Q6ZNB7.
KO	K15537.
OMA	QGFRMLF.
OrthoDB	EOG4X3H1M.
Gene expression databases
ArrayExpress	Q6ZNB7.
Bgee	Q6ZNB7.
CleanEx	HS_TMEM195.
Genevestigator	Q6ZNB7.
Family and domain databases
InterPro	IPR006694. Fatty_acid_hydroxylase. [Graphical view]
Pfam	PF04116. FA_hydroxylase. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	392636.
NextBio	105330.
SOURCE	Search...

Entry information

Entry name

ALKMO_HUMAN

Accession

Primary (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 3, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.