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Protein

N-acylethanolamine-hydrolyzing acid amidase

Gene

Naaa

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Degrades bioactive fatty acid amides to their corresponding acids, with a preference for N-palmitoylethanolamine.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei131 – 1311NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.5.1.4. 3474.

Protein family/group databases

MEROPSiC89.002.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acylethanolamine-hydrolyzing acid amidase (EC:3.5.1.-)
Alternative name(s):
N-acylsphingosine amidohydrolase-like
Short name:
ASAH-like protein
Cleaved into the following 2 chains:
Gene namesi
Name:Naaa
Synonyms:Asahl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1914361. Naaa.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333By similarityAdd
BLAST
Chaini34 – 362329N-acylethanolamine-hydrolyzing acid amidasePRO_0000002319Add
BLAST
Chaini34 – 13097N-acylethanolamine-hydrolyzing acid amidase subunit alphaPRO_0000419652Add
BLAST
Chaini131 – 349219N-acylethanolamine-hydrolyzing acid amidase subunit betaPRO_0000419653Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence analysis
Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence analysis
Glycosylationi314 – 3141N-linked (GlcNAc...)Sequence analysis
Glycosylationi338 – 3381N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Autoproteolytic cleavage in the acidic lumen of the lysosome activates the enzyme.By similarity

Keywords - PTMi

Autocatalytic cleavage, Glycoprotein, Zymogen

Proteomic databases

EPDiQ9D7V9.
MaxQBiQ9D7V9.
PaxDbiQ9D7V9.
PRIDEiQ9D7V9.

Expressioni

Gene expression databases

BgeeiQ9D7V9.
ExpressionAtlasiQ9D7V9. baseline and differential.
GenevisibleiQ9D7V9. MM.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit, non-covalently linked.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9D7V9. 2 interactions.
MINTiMINT-4123901.
STRINGi10090.ENSMUSP00000108726.

Structurei

3D structure databases

ProteinModelPortaliQ9D7V9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acid ceramidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IJHJ. Eukaryota.
ENOG4111HJY. LUCA.
GeneTreeiENSGT00530000063548.
HOGENOMiHOG000007253.
HOVERGENiHBG050586.
InParanoidiQ9D7V9.
KOiK13720.
OMAiHWKPVPK.
OrthoDBiEOG7JMGDW.
PhylomeDBiQ9D7V9.
TreeFamiTF313219.

Family and domain databases

InterProiIPR016699. Acid_ceramidase-like.
IPR029130. Acid_ceramidase_N.
IPR029132. CBAH/NAAA_C.
[Graphical view]
PfamiPF02275. CBAH. 1 hit.
PF15508. NAAA-beta. 1 hit.
[Graphical view]
PIRSFiPIRSF017632. Acid_ceramidase-like. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D7V9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTLATRAAC HGAHLALALL LLLSLSGPWL SAVVPGTPPL FNVSLDAAPE
60 70 80 90 100
QRWLPMLRHY DPDFLRTAVA QVIGDRVPQW VLGMVGEIVS KVESFLPQPF
110 120 130 140 150
TDEIRSICDS LNLSLADGIL VNLAYEASAF CTSIVAQDSQ GHIYHGRNLD
160 170 180 190 200
YPFGKILRKL TANVQFIKNG QIAFTGTTFV GYVGLWTGQS PHKFTISGDE
210 220 230 240 250
RDKGWWWENM IAALSLGHSP ISWLIRKTLS ESESFEAAVY TLAKTPLIAD
260 270 280 290 300
VYYIVGGTSP KEGVVITRDR GGPADIWPLD PLNGEWFRVE TNYDHWKPAP
310 320 330 340 350
KVDDRRTPAI KALNATGQAH LNLETLFQVL SLFPVYNNYT IYTTVMSAAE
360
PDKYLTMIRN PS
Length:362
Mass (Da):40,075
Last modified:June 21, 2005 - v2
Checksum:i49480CCA1630699F
GO

Sequence cautioni

The sequence BAB29350.2 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51A → D in BAB25888 (PubMed:16141072).Curated
Sequence conflicti47 – 471A → V in AAH04572 (PubMed:15489334).Curated
Sequence conflicti142 – 1421H → R in AAH04572 (PubMed:15489334).Curated
Sequence conflicti163 – 1631N → D in AAH04572 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB162194 mRNA. Translation: BAD88530.1.
AK008776 mRNA. Translation: BAB25888.1.
AK014438 mRNA. Translation: BAB29350.2. Sequence problems.
BC004572 mRNA. Translation: AAH04572.1.
CCDSiCCDS19428.1.
RefSeqiNP_001157159.1. NM_001163687.1.
NP_080248.2. NM_025972.4.
UniGeneiMm.28890.

Genome annotation databases

EnsembliENSMUST00000113102; ENSMUSP00000108726; ENSMUSG00000029413.
GeneIDi67111.
KEGGimmu:67111.
UCSCiuc008ycq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB162194 mRNA. Translation: BAD88530.1.
AK008776 mRNA. Translation: BAB25888.1.
AK014438 mRNA. Translation: BAB29350.2. Sequence problems.
BC004572 mRNA. Translation: AAH04572.1.
CCDSiCCDS19428.1.
RefSeqiNP_001157159.1. NM_001163687.1.
NP_080248.2. NM_025972.4.
UniGeneiMm.28890.

3D structure databases

ProteinModelPortaliQ9D7V9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D7V9. 2 interactions.
MINTiMINT-4123901.
STRINGi10090.ENSMUSP00000108726.

Protein family/group databases

MEROPSiC89.002.

Proteomic databases

EPDiQ9D7V9.
MaxQBiQ9D7V9.
PaxDbiQ9D7V9.
PRIDEiQ9D7V9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000113102; ENSMUSP00000108726; ENSMUSG00000029413.
GeneIDi67111.
KEGGimmu:67111.
UCSCiuc008ycq.2. mouse.

Organism-specific databases

CTDi27163.
MGIiMGI:1914361. Naaa.

Phylogenomic databases

eggNOGiENOG410IJHJ. Eukaryota.
ENOG4111HJY. LUCA.
GeneTreeiENSGT00530000063548.
HOGENOMiHOG000007253.
HOVERGENiHBG050586.
InParanoidiQ9D7V9.
KOiK13720.
OMAiHWKPVPK.
OrthoDBiEOG7JMGDW.
PhylomeDBiQ9D7V9.
TreeFamiTF313219.

Enzyme and pathway databases

BRENDAi3.5.1.4. 3474.

Miscellaneous databases

NextBioi323601.
PROiQ9D7V9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D7V9.
ExpressionAtlasiQ9D7V9. baseline and differential.
GenevisibleiQ9D7V9. MM.

Family and domain databases

InterProiIPR016699. Acid_ceramidase-like.
IPR029130. Acid_ceramidase_N.
IPR029132. CBAH/NAAA_C.
[Graphical view]
PfamiPF02275. CBAH. 1 hit.
PF15508. NAAA-beta. 1 hit.
[Graphical view]
PIRSFiPIRSF017632. Acid_ceramidase-like. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of N-acylethanolamine-hydrolyzing acid amidase, a novel member of the choloylglycine hydrolase family with structural and functional similarity to acid ceramidase."
    Tsuboi K., Sun Y.-X., Okamoto Y., Araki N., Tonai T., Ueda N.
    J. Biol. Chem. 280:11082-11092(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Lung.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Extraembryonic tissue, Placenta and Stomach.
  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].
    Strain: FVB/N.
    Tissue: Mammary gland.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiNAAA_MOUSE
AccessioniPrimary (citable) accession number: Q9D7V9
Secondary accession number(s): Q5KTC6, Q99KM3, Q9D6B4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 21, 2005
Last modified: April 13, 2016
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.