Q9H6B9 (EPHX3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Epoxide hydrolase 3
EC=3.3.-.-

Alternative name(s):
Abhydrolase domain-containing protein 9

Gene names

Name:	EPHX3
Synonyms:	ABHD9

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	360 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Subcellular location	Secreted Potential.
Sequence similarities	Belongs to the AB hydrolase superfamily. Epoxide hydrolase family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 35	35	Potential
	Chain	36 – 360	325	Epoxide hydrolase 3		PRO_0000264232
Sites
	Active site	173	1	Nucleophile By similarity
	Active site	281	1	Proton donor By similarity
	Active site	337	1	Proton acceptor By similarity
Amino acid modifications
	Glycosylation	267	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9H6B9 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: C465A4B0E2D56BA0	FASTA	360	40,909
	10 20 30 40 50 60 MPELVVTALL APSRLSLKLL RAFMWSLVFS VALVAAAVYG CIALTHVLCR PRRGCCGRRR 70 80 90 100 110 120 SASPACLSDP SLGEHGFLNL KSSGLRLHYV SAGRGNGPLM LFLHGFPENW FSWRYQLREF 130 140 150 160 170 180 QSRFHVVAVD LRGYGPSDAP RDVDCYTIDL LLVDIKDVIL GLGYSKCILV AHDWGALLAW 190 200 210 220 230 240 HFSIYYPSLV ERMVVVSGAP MSVYQDYSLH HISQFFRSHY MFLFQLPWLP EKLLSMSDFQ 250 260 270 280 290 300 ILKTTLTHRK TGIPCLTPSE LEAFLYNFSQ PGGLTGPLNY YRNLFRNFPL EPQELTTPTL 310 320 330 340 350 360 LLWGEKDTYL ELGLVEAIGS RFVPGRLEAH ILPGIGHWIP QSNPQEMHQY MWAFLQDLLD

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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Embryonic stem cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK026061 mRNA. Translation: BAB15342.1. CH471106 Genomic DNA. Translation: EAW84467.1. BC115002 mRNA. Translation: AAI15003.1. BC132958 mRNA. Translation: AAI32959.1. BC132960 mRNA. Translation: AAI32961.1.
IPI	IPI00015658.
RefSeq	NP_001136358.1. NM_001142886.1. NP_079070.1. NM_024794.2.
UniGene	Hs.156457.
3D structure databases
HSSP	HSSP built from PDB template 2CJP based on UniProtKB Q41415.
ProteinModelPortal	Q9H6B9.
SMR	Q9H6B9. Positions 73-357.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9H6B9.
Protein family/group databases
MEROPS	S33.978.
Polymorphism databases
DMDM	74718486.
Proteomic databases
PRIDE	Q9H6B9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000221730; ENSP00000221730; ENSG00000105131. ENST00000435261; ENSP00000410323; ENSG00000105131.
GeneID	79852.
KEGG	hsa:79852.
UCSC	uc002nap.1. human.
Organism-specific databases
CTD	79852.
GeneCards	GC19M015337.
HGNC	HGNC:23760. EPHX3.
HPA	HPA012842.
neXtProt	NX_Q9H6B9.
PharmGKB	PA164719188.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00530000063213.
InParanoid	Q9H6B9.
OMA	PMSVYQD.
OrthoDB	EOG4JM7Q4.
PhylomeDB	Q9H6B9.
Gene expression databases
ArrayExpress	Q9H6B9.
Bgee	Q9H6B9.
CleanEx	HS_ABHD9.
Genevestigator	Q9H6B9.
GermOnline	ENSG00000105131. Homo sapiens.
Family and domain databases
InterPro	IPR000073. AB_hydrolase_1. IPR000639. Epox_hydrolase-like. [Graphical view]
PRINTS	PR00111. ABHYDROLASE. PR00412. EPOXHYDRLASE.
ProtoNet	Search...
Other
NextBio	69563.

Entry information

Entry name

EPHX3_HUMAN

Accession

Primary (citable) accession number: Q9H6B9
Secondary accession number(s): A3KMR3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 73 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.