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Q8TB40 (ABHD4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Abhydrolase domain-containing protein 4

EC=3.1.1.-
Alternative name(s):
Alpha/beta-hydrolase 4
Lyso-N-acylphosphatidylethanolamine lipase
Gene names
Name:ABHD4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Lysophospholipase selective for N-acyl phosphatidylethanolamine (NAPE). Contributes to the biosynthesis of N-acyl ethanolamines, including the endocannabinoid anandamide by hydrolyzing the sn-1 and sn-2 acyl chains from N-acyl phosphatidylethanolamine (NAPE) generating glycerophospho-N-acyl ethanolamine (GP-NAE), an intermediate for N-acyl ethanolamine biosynthesis. Hydrolyzes substrates bearing saturated, monounsaturated, polyunsaturated N-acyl chains. Shows no significant activity towards other lysophospholipids, including lysophosphatidylcholine, lysophosphatidylethanolamine and lysophosphatidylserine By similarity.

Sequence similarities

Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.

Caution

Thr-291 is present instead of the conserved His which is expected to be an active site residue.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionhydrolase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 342342Abhydrolase domain-containing protein 4
PRO_0000080864

Experimental info

Sequence conflict183 – 1853EIR → GIC in BAB14289. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8TB40 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 867EA9E0092559CB

FASTA34238,794
        10         20         30         40         50         60 
MADDLEQQSQ GWLSSWLPTW RPTSMSQLKN VEARILQCLQ NKFLARYVSL PNQNKIWTVT 

        70         80         90        100        110        120 
VSPEQNDRTP LVMVHGFGGG VGLWILNMDS LSARRTLHTF DLLGFGRSSR PAFPRDPEGA 

       130        140        150        160        170        180 
EDEFVTSIET WRETMGIPSM ILLGHSLGGF LATSYSIKYP DRVKHLILVD PWGFPLRPTN 

       190        200        210        220        230        240 
PSEIRAPPAW VKAVASVLGR SNPLAVLRVA GPWGPGLVQR FRPDFKRKFA DFFEDDTISE 

       250        260        270        280        290        300 
YIYHCNAQNP SGETAFKAMM ESFGWARRPM LERIHLIRKD VPITMIYGSD TWIDTSTGKK 

       310        320        330        340 
VKMQRPDSYV RDMEIKGASH HVYADQPHIF NAVVEEICDS VD 

« Hide

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]"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: Cervix.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK022878 mRNA. Translation: BAB14289.1.
BC024779 mRNA. Translation: AAH24779.1.
RefSeqNP_071343.2. NM_022060.2.
UniGeneHs.445665.

3D structure databases

ProteinModelPortalQ8TB40.
SMRQ8TB40. Positions 61-268.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121967. 3 interactions.
IntActQ8TB40. 2 interactions.
MINTMINT-3044114.
STRING9606.ENSP00000216327.

Protein family/group databases

MEROPSS33.013.

PTM databases

PhosphoSiteQ8TB40.

Polymorphism databases

DMDM74762601.

Proteomic databases

PaxDbQ8TB40.
PRIDEQ8TB40.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000428304; ENSP00000414558; ENSG00000100439.
GeneID63874.
KEGGhsa:63874.
UCSCuc001wgm.3. human.

Organism-specific databases

CTD63874.
GeneCardsGC14P023067.
HGNCHGNC:20154. ABHD4.
HPAHPA000600.
neXtProtNX_Q8TB40.
PharmGKBPA128394705.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0596.
HOGENOMHOG000007445.
HOVERGENHBG054445.
InParanoidQ8TB40.
KOK13698.
OMAGLFTMAD.
OrthoDBEOG751NG1.
PhylomeDBQ8TB40.
TreeFamTF314196.

Gene expression databases

ArrayExpressQ8TB40.
BgeeQ8TB40.
CleanExHS_ABHD4.
GenevestigatorQ8TB40.

Family and domain databases

InterProIPR000073. AB_hydrolase_1.
[Graphical view]
PRINTSPR00111. ABHYDROLASE.
ProtoNetSearch...

Other

ChiTaRSABHD4. human.
GenomeRNAi63874.
NextBio65552.
PROQ8TB40.

Entry information

Entry nameABHD4_HUMAN
AccessionPrimary (citable) accession number: Q8TB40
Secondary accession number(s): Q9H9E0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: June 1, 2002
Last modified: March 19, 2014
This is version 92 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

Peptidase families

Classification of peptidase families and list of entries

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM