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Protein

Arylacetamide deacetylase-like 4

Gene

AADACL4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei119 – 1191Sequence Analysis
Active sitei193 – 1931Sequence Analysis

GO - Molecular functioni

  1. carboxylic ester hydrolase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Arylacetamide deacetylase-like 4 (EC:3.1.1.-)
Gene namesi
Name:AADACL4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:32038. AADACL4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicSequence Analysis
Transmembranei5 – 2521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini26 – 407382LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA145147537.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 407407Arylacetamide deacetylase-like 4PRO_0000265937Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi168 – 1681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ5VUY2.
PRIDEiQ5VUY2.

PTM databases

PhosphoSiteiQ5VUY2.

Expressioni

Gene expression databases

BgeeiQ5VUY2.
CleanExiHS_AADACL4.
GenevestigatoriQ5VUY2.

Organism-specific databases

HPAiHPA043588.

Structurei

3D structure databases

ProteinModelPortaliQ5VUY2.
SMRiQ5VUY2. Positions 79-383.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi119 – 1213Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity

Sequence similaritiesi

Belongs to the 'GDXG' lipolytic enzyme family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0657.
GeneTreeiENSGT00550000074556.
HOGENOMiHOG000231073.
HOVERGENiHBG058974.
InParanoidiQ5VUY2.
KOiK14351.
OMAiDNIPKKF.
OrthoDBiEOG7P8P80.
PhylomeDBiQ5VUY2.
TreeFamiTF314978.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR017157. Arylacetamide_deacetylase.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 2 hits.
[Graphical view]
PIRSFiPIRSF037251. Arylacetamide_deacetylase. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5VUY2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVPWLVLLL ALPIFFLGVF VWAVFEHFLT TDIPATLQHP AKLRFLHCIF
60 70 80 90 100
LYLVTLGNIF EKLGICSMPK FIRFLHDSVR IKKDPELVVT DLRFGTIPVR
110 120 130 140 150
LFQPKAASSR PRRGIIFYHG GATVFGSLDC YHGLCNYLAR ETESVLLMIG
160 170 180 190 200
YRKLPDHHSP ALFQDCMNAS IHFLKALETY GVDPSRVVVC GESVGGAAVA
210 220 230 240 250
AITQALVGRS DLPRIRAQVL IYPVVQAFCL QLPSFQQNQN VPLLSRKFMV
260 270 280 290 300
TSLCNYLAID LSWRDAILNG TCVPPDVWRK YEKWLSPDNI PKKFKNRGYQ
310 320 330 340 350
PWSPGPFNEA AYLEAKHMLD VENSPLIADD EVIAQLPEAF LVSCENDILR
360 370 380 390 400
DDSLLYKKRL EDQGVRVTWY HLYDGFHGSI IFFDKKALSF PCSLKIVNAV

VSYIKGI
Length:407
Mass (Da):46,082
Last modified:December 6, 2004 - v1
Checksum:iCE95EEE9A2C49970
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL513016 Genomic DNA. Translation: CAH74173.1.
CCDSiCCDS30590.1.
RefSeqiNP_001013652.1. NM_001013630.1.
UniGeneiHs.209954.

Genome annotation databases

EnsembliENST00000376221; ENSP00000365395; ENSG00000204518.
GeneIDi343066.
KEGGihsa:343066.
UCSCiuc001auf.3. human.

Polymorphism databases

DMDMi74747169.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL513016 Genomic DNA. Translation: CAH74173.1.
CCDSiCCDS30590.1.
RefSeqiNP_001013652.1. NM_001013630.1.
UniGeneiHs.209954.

3D structure databases

ProteinModelPortaliQ5VUY2.
SMRiQ5VUY2. Positions 79-383.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ5VUY2.

Polymorphism databases

DMDMi74747169.

Proteomic databases

PaxDbiQ5VUY2.
PRIDEiQ5VUY2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376221; ENSP00000365395; ENSG00000204518.
GeneIDi343066.
KEGGihsa:343066.
UCSCiuc001auf.3. human.

Organism-specific databases

CTDi343066.
GeneCardsiGC01P012627.
HGNCiHGNC:32038. AADACL4.
HPAiHPA043588.
neXtProtiNX_Q5VUY2.
PharmGKBiPA145147537.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0657.
GeneTreeiENSGT00550000074556.
HOGENOMiHOG000231073.
HOVERGENiHBG058974.
InParanoidiQ5VUY2.
KOiK14351.
OMAiDNIPKKF.
OrthoDBiEOG7P8P80.
PhylomeDBiQ5VUY2.
TreeFamiTF314978.

Miscellaneous databases

GeneWikiiAADACL4_(gene).
GenomeRNAii343066.
NextBioi98444.
PROiQ5VUY2.

Gene expression databases

BgeeiQ5VUY2.
CleanExiHS_AADACL4.
GenevestigatoriQ5VUY2.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR017157. Arylacetamide_deacetylase.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 2 hits.
[Graphical view]
PIRSFiPIRSF037251. Arylacetamide_deacetylase. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiADCL4_HUMAN
AccessioniPrimary (citable) accession number: Q5VUY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 11, 2006
Last sequence update: December 6, 2004
Last modified: January 6, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.