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Entry version 113 (02 Dec 2020)
Sequence version 1 (01 Dec 2001)
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Protein

Neutral ceramidase

Gene

Asah2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Plasma membrane ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at neutral pH (PubMed:11328816, PubMed:10488143, PubMed:15217782). Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation (PubMed:11328816). Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine (PubMed:15123644, PubMed:11278489). Together with sphingomyelinase, participates in the production of sphingosine and sphingosine-1-phosphate from the degradation of sphingomyelin, a sphingolipid enriched in the plasma membrane of cells (PubMed:15217782). Also participates in the hydrolysis of ceramides from the extracellular milieu allowing the production of sphingosine-1-phosphate inside and outside cells. This is the case for instance with the digestion of dietary sphingolipids in the intestinal tract (By similarity).1 PublicationBy similarity5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The reverse reaction is inhibited by Zn2+ and Cu2+ (PubMed:11278489). Inhibited by cardiolipin and phosphatidic acid (PubMed:11278489).1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

More efficiently hydrolyzes N-lauroylsphingosine/C12:0-ceramides compared to N-palmitoylsphingosine/C16:0-ceramides and N-stearoylsphingosine/C18:0-ceramides (PubMed:11328816). The catalytic efficiency towards dihydroceramides and phytoceramides is very low (PubMed:11328816, PubMed:10488143). For the reverse synthetic reaction exhibits a higher activity with D-erythro-sphing-4-enine and the fatty acid tetradecanoate as substrates (PubMed:11278489).3 Publications
  1. KM=71.4 µM for N-(octanoyl)-sphing-4-enine1 Publication
  2. KM=66 µM for N-hexadecanoylsphing-4-enine1 Publication
  1. Vmax=160 µmol/min/mg enzyme with N-(octanoyl)-sphing-4-enine as substrate1 Publication
  2. Vmax=16 µmol/min/mg enzyme with N-hexadecanoylsphing-4-enine as substrate1 Publication
  3. Vmax=4.4 µmol/min/mg enzyme with N-hexadecanoylsphing-4-enine as substrate1 Publication
  4. Vmax=1.2 µmol/min/mg enzyme with dihydroceramide as substrate1 Publication
  5. Vmax=0.63 µmol/min/mg enzyme toward tetradecanoate for the synthesis of N-tetradecanoylsphing-4-enine (at pH 7.0)1 Publication
  6. Vmax=0.47 µmol/min/mg enzyme toward hexadecanoate for the synthesis of N-hexadecanoylsphing-4-enine (at pH 7.0)1 Publication
  7. Vmax=0.28 µmol/min/mg enzyme toward (9Z)-octadecenoate for the synthesis of N-(9Z-octadecenoyl)-sphing-4-enine (at pH 7.0)1 Publication
  8. Vmax=0.25 µmol/min/mg enzyme toward (15Z)-tetracosenoate for the synthesis of N-(15Z-tetracosenoyl)sphing-4-enine (at pH 7.0)1 Publication
  9. Vmax=0.3 µmol/min/mg enzyme toward D-erythro-sphing-4-enine for the synthesis of N-hexadecanoylsphing-4-enine (at pH 7.0)1 Publication

pH dependencei

Optimum pH is 6-7 for N-hexadecanoylsphing-4-enine hydrolysis (PubMed:11328816). Optimum pH is 7-10 for N-hexadecanoylsphing-4-enine hydrolysis (PubMed:10488143). Optimum pH is 6-8 for N-(octanoyl)-sphing-4-enine hydrolysis (PubMed:15217782). Optimum pH is 6.5-7 for hexadecanoate in the reverse reaction (PubMed:11278489).4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: sphingolipid metabolism

This protein is involved in the pathway sphingolipid metabolism, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway sphingolipid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi115Calcium; via carbonyl oxygenBy similarity1
Metal bindingi175Zinc; via tele nitrogenBy similarity1
Metal bindingi284Zinc; via tele nitrogenBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei335NucleophileBy similarity1
Metal bindingi521ZincBy similarity1
Metal bindingi560ZincBy similarity1
Metal bindingi693Calcium; via carbonyl oxygenBy similarity1
Metal bindingi695Calcium; via carbonyl oxygenBy similarity1
Metal bindingi698CalciumBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processApoptosis, Lipid metabolism, Sphingolipid metabolism
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.5.1.23, 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1660662, Glycosphingolipid metabolism

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q91XT9

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00222

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000682

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Neutral ceramidaseCurated (EC:3.5.1.-2 Publications, EC:3.5.1.235 Publications)
Short name:
N-CDase
Short name:
NCDase
Alternative name(s):
Acylsphingosine deacylase 2
N-acylsphingosine amidohydrolase 2
Cleaved into the following chain:
Neutral ceramidase soluble form1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Asah2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Rat genome database

More...
RGDi
69410, Asah2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 11CytoplasmicSequence analysisAdd BLAST11
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei12 – 32Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini33 – 761LumenalSequence analysisAdd BLAST729

Keywords - Cellular componenti

Cell membrane, Golgi apparatus, Membrane, Mitochondrion, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi44S → A: Abolishes O-glycosylation and localization at the cell surface; when associated with A-50; A-51; A-52; A-56; A-57; A-58; A-60; A-61; A-62; A-63; A-65; A-76; A-68; A-69; A-71 and A-77. 1 Publication1
Mutagenesisi50 – 71STTQG…PTTQT → AAAQGPAAAQAAPAAQAPAA QA: Abolishes O-glycosylation and localization at the cell surface; when associated with A-44 and A-77. 1 PublicationAdd BLAST22
Mutagenesisi77S → A: Abolishes O-glycosylation and localization at the cell surface; when associated with A-44; A-50; A-51; A-52; A-56; A-57; A-58; A-60; A-61; A-62; A-63; A-65; A-76; A-68; A-69 and A-71. 1 Publication1
Mutagenesisi756F → I: No effect. 1 Publication1
Mutagenesisi756F → R or D: Loss of function. 1 Publication1
Mutagenesisi757E → R: No effect. 1 Publication1
Mutagenesisi758I → F: Impairs enzyme activity. 1 Publication1
Mutagenesisi758I → R or D: Loss of function. 1 Publication1
Mutagenesisi758I → V: No effect. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002471031 – 761Neutral ceramidaseAdd BLAST761
ChainiPRO_000024710480 – 761Neutral ceramidase soluble form1 PublicationAdd BLAST682

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi51O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi52O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi56O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi57O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi58O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi60O-linked (GalNAc...) serineSequence analysis1
Glycosylationi61O-linked (GalNAc...) serineSequence analysis1
Glycosylationi63O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi64O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi66O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi68O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi69O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi71O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi198N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi343 ↔ 357By similarity
Disulfide bondi350 ↔ 365By similarity
Glycosylationi412N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi429 ↔ 479By similarity
Glycosylationi449N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Proteolytic cleavage of the N-terminus removes the signal-anchor and produces a soluble form of the protein.1 Publication
N-glycosylated (PubMed:11328816, PubMed:15123644). Required for enzyme activity (PubMed:11328816).2 Publications
O-glycosylated (PubMed:12499379). Required to retain it as a type II membrane protein at the cell surface (PubMed:12499379).1 Publication
Phosphorylated. May prevent ubiquitination and subsequent degradation.2 Publications
Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is triggered by nitric oxide.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei79 – 80Cleavage1 Publication2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q91XT9

PRoteomics IDEntifications database

More...
PRIDEi
Q91XT9

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
Q91XT9, 16 sites

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highly expressed in brain, kidney and heart (PubMed:11328816). Expressed at lower level in other tissues such as liver (PubMed:11328816). Expressed in intestine, kidney and liver (at protein level) (PubMed:11328816, PubMed:11330410). Localizes in the epithelia of the jejunum and ileum (PubMed:11330410).2 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By interleukin-1-beta in renal mesangial cells.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000012196, Expressed in duodenum and 21 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q91XT9, RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000016688

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q91XT9

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni751 – 761Required for correct folding and localization1 PublicationAdd BLAST11

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the neutral ceramidase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2232, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000015792

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q91XT9

Identification of Orthologs from Complete Genome Data

More...
OMAi
NADIAMG

Database of Orthologous Groups

More...
OrthoDBi
967085at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q91XT9

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.2300, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006823, Ceramidase_alk
IPR038445, NCDase_C_sf
IPR031331, NEUT/ALK_ceramidase_C
IPR031329, NEUT/ALK_ceramidase_N

The PANTHER Classification System

More...
PANTHERi
PTHR12670, PTHR12670, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04734, Ceramidase_alk, 1 hit
PF17048, Ceramidse_alk_C, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q91XT9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKRTFSSLE AFLIFLLVMM TAITVALLTL LFVTSGTIEN HKDSGNHWVS
60 70 80 90 100
TTQGPTTTQS SPTTQTPTTQ TPDLPPSQNF SGYYIGVGRA DCTGQVSDIN
110 120 130 140 150
LMGYGKNGQN AQGLLTRLFS RAFILADPDG SNRMAFVSVE LCMISQRLRL
160 170 180 190 200
EVLKRLQSKY GSLYRRDNVI LSATHTHSGP AGFFQYTLYI LASEGFSNRT
210 220 230 240 250
FQYIVSGIVK SIDIAHTNLK PGKVLINKGN VANVQINRSP SSYLQNPPSE
260 270 280 290 300
RARYSSDTDK EMVVLKLVDL NGEDLGLISW FAVHPVSMNN SNHLVNSDNM
310 320 330 340 350
GYAAYLFEQE KNRGYLPGQG PFVAGFASSN LGDVSPNILG PHCVNTGESC
360 370 380 390 400
DNDKSTCPSG GPSMCMASGP GQDMFESTHI IGRVIYQKAK ELHASASQEV
410 420 430 440 450
TGPVLTAHQW VNMTDVSVQL NATHTVKTCK AALGYSFAAG TIDGVSGLNI
460 470 480 490 500
TQGTTEGNLF WDTLRDQLLG KPSEEIIECQ KPKPILIHTG ELTKPHPWQP
510 520 530 540 550
DIVDIQIVTL GSLAIAAIPG EFTTMSGRRL REAVKKEFAL YGMKDMTVVI
560 570 580 590 600
AGLSNVYTHY ITTYEEYQAQ RYEAASTIYG PHTLSAYIQL FRALAKAIAT
610 620 630 640 650
DTVANMSSGP EPPFFKNLIG SLIPNIADRA PIGKQFGDVL QPAKPEYRVG
660 670 680 690 700
EVVEVVFVGA NPKNSAENQT HQTFLTVEKY EDSVANWQIM HNDASWETRF
710 720 730 740 750
YWHKGVLGLS NATIHWHIPD TALPGVYRIR YFGHNRKQEL LKPAVILAFE
760
GISSPFEIVT T
Length:761
Mass (Da):83,488
Last modified:December 1, 2001 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i68B91BC78AEB6324
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti325G → N AA sequence (PubMed:10781606).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AB057433 mRNA Translation: BAB62033.1

NCBI Reference Sequences

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RefSeqi
NP_446098.1, NM_053646.2
XP_006231325.1, XM_006231263.1
XP_006231330.1, XM_006231268.3
XP_006231332.1, XM_006231270.1
XP_008758542.1, XM_008760320.2
XP_017444135.1, XM_017588646.1
XP_017444136.1, XM_017588647.1
XP_017444137.1, XM_017588648.1
XP_017444138.1, XM_017588649.1
XP_017444139.1, XM_017588650.1
XP_017444140.1, XM_017588651.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSRNOT00000016688; ENSRNOP00000016688; ENSRNOG00000012196
ENSRNOT00000077135; ENSRNOP00000073116; ENSRNOG00000012196

Database of genes from NCBI RefSeq genomes

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GeneIDi
114104

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:114104

UCSC genome browser

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UCSCi
RGD:69410, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB057433 mRNA Translation: BAB62033.1
RefSeqiNP_446098.1, NM_053646.2
XP_006231325.1, XM_006231263.1
XP_006231330.1, XM_006231268.3
XP_006231332.1, XM_006231270.1
XP_008758542.1, XM_008760320.2
XP_017444135.1, XM_017588646.1
XP_017444136.1, XM_017588647.1
XP_017444137.1, XM_017588648.1
XP_017444138.1, XM_017588649.1
XP_017444139.1, XM_017588650.1
XP_017444140.1, XM_017588651.1

3D structure databases

SMRiQ91XT9
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016688

Chemistry databases

SwissLipidsiSLP:000000682

PTM databases

GlyGeniQ91XT9, 16 sites

Proteomic databases

PaxDbiQ91XT9
PRIDEiQ91XT9

Genome annotation databases

EnsembliENSRNOT00000016688; ENSRNOP00000016688; ENSRNOG00000012196
ENSRNOT00000077135; ENSRNOP00000073116; ENSRNOG00000012196
GeneIDi114104
KEGGirno:114104
UCSCiRGD:69410, rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
56624
RGDi69410, Asah2

Phylogenomic databases

eggNOGiKOG2232, Eukaryota
GeneTreeiENSGT00390000015792
InParanoidiQ91XT9
OMAiNADIAMG
OrthoDBi967085at2759
PhylomeDBiQ91XT9

Enzyme and pathway databases

UniPathwayiUPA00222
BRENDAi3.5.1.23, 5301
ReactomeiR-RNO-1660662, Glycosphingolipid metabolism
SABIO-RKiQ91XT9

Miscellaneous databases

Protein Ontology

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PROi
PR:Q91XT9

Gene expression databases

BgeeiENSRNOG00000012196, Expressed in duodenum and 21 other tissues
GenevisibleiQ91XT9, RN

Family and domain databases

Gene3Di2.60.40.2300, 1 hit
InterProiView protein in InterPro
IPR006823, Ceramidase_alk
IPR038445, NCDase_C_sf
IPR031331, NEUT/ALK_ceramidase_C
IPR031329, NEUT/ALK_ceramidase_N
PANTHERiPTHR12670, PTHR12670, 1 hit
PfamiView protein in Pfam
PF04734, Ceramidase_alk, 1 hit
PF17048, Ceramidse_alk_C, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiASAH2_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q91XT9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: December 1, 2001
Last modified: December 2, 2020
This is version 113 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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