Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q6ZUV0 (BACHL_HUMAN)

Last modified November 3, 2009. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cytosolic acyl coenzyme A thioester hydrolase-like
    EC=3.1.2.2
Alternative name(s):
    Acyl-CoA thioesterase 7-like
Gene names
Name: ACOT7L
Synonyms: BACHL
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH By similarity.

Catalytic activity

Palmitoyl-CoA + H2O = CoA + palmitate.

Subunit structure

Homodimer Probable.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Expressed in all tissues examined. Up-regulated in nasopharyngeal carcinoma (at protein level). Ref.2

Involvement in disease

Genetic variations in ACOT7L may be a cause of susceptibility to nasopharyngeal carcinoma type 1 (NPCA1) [MIM:607107]. A variant located in the regulatory region of the gene creates an AP1-binding site that significantly enhances binding of AP1 to the promoter, resulting in up-regulation in nasopharyngeal carcinoma. Ref.2

Sequence similarities

Contains 2 acyl coenzyme A hydrolase domains.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRepeat
   Molecular functionHydrolase
Serine esterase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncarboxylesterase activity

Inferred from electronic annotation. Source: UniProtKB-KW

palmitoyl-CoA hydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 252252Cytosolic acyl coenzyme A thioester hydrolase-like
PRO_0000347058

Regions

Domain4 – 7370Acyl coenzyme A hydrolase 1
Domain164 – 24178Acyl coenzyme A hydrolase 2

Sequences

Sequence LengthMass (Da)Tools
Q6ZUV0-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: E9C4DF4A82B87717

FASTA25228,164
        10         20         30         40         50         60 
MIKEAGAIIS TRHCNPQNGD RCVAALARVE CTHFLWPMCI GEVAHVSAEI TYTSKHSVEV 

        70         80         90        100        110        120 
QVNMMSENIL TGAKKLTNKA TLWYAPLSLT NVDKVLEEPP VVYFRQEQEE EGQKRYKTQK 

       130        140        150        160        170        180 
LERMETNWRN GDIVQPVLNP EPNTVSYSQS SLIHLVGPSD CTLHSFVHEG VTMKVMDEVA 

       190        200        210        220        230        240 
GILAARHCKT NLVTASMEAI NFDNKIRKGC IKTISGRMTF TSNKSVEIEV LVDADCVVDS 

       250 
SQKRYRAASV FT 

« 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]"A functional variant in the transcriptional regulatory region of gene LOC344967 cosegregates with disease phenotype in familial nasopharyngeal carcinoma."
Jiang R.-C., Qin H.-D., Zeng M.-S., Huang W., Feng B.-J., Zhang F., Chen H.-K., Jia W.-H., Chen L.-Z., Feng Q.-S., Zhang R.-H., Yu X.-J., Zheng M.-Z., Zeng Y.-X.
Cancer Res. 66:693-700(2006) [PubMed: 16423998] [Abstract]
Cited for: TISSUE SPECIFICITY, INVOLVEMENT IN NPCA1.

Cross-references

Sequence databases

AK125299 mRNA. Translation: BAC86118.1.
IPIIPI00445888.
UniGeneHs.534633

3D structure databases

ModBaseSearch...

Proteomic databases

PRIDEQ6ZUV0.

Genome annotation databases

EnsemblENST00000381811; ENSP00000371232; ENSG00000205794; Homo sapiens. [Genome view]

Organism-specific databases

GeneCardsGC04M039720.
MIM607107. phenotype.
611963. gene.

Phylogenomic databases

HOGENOMQ6ZUV0.
HOVERGENQ6ZUV0.
OMALERMETN.

Gene expression databases

BgeeQ6ZUV0.
GenevestigatorQ6ZUV0.

Family and domain databases

InterProIPR006683. Thioestr_supf.
[Graphical view]
PfamPF03061. 4HBT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameBACHL_HUMAN
AccessionPrimary (citable) accession number: Q6ZUV0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: July 5, 2004
Last modified: November 3, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents