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Alkaline ceramidase 2 (AlkCDase 2) (Alkaline CDase 2) (haCER2) (EC 3.5.1.23) (Acylsphingosine deacylase 3-like) (N-acylsphingosine amidohydrolase 3-like)

 ACER2_HUMAN             Reviewed;         275 AA.
Q5QJU3; A2A3R8; Q569G5; Q5VZR7; Q71RD2;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
25-JUL-2006, sequence version 2.
27-SEP-2017, entry version 97.
RecName: Full=Alkaline ceramidase 2;
Short=AlkCDase 2;
Short=Alkaline CDase 2;
Short=haCER2;
EC=3.5.1.23;
AltName: Full=Acylsphingosine deacylase 3-like;
AltName: Full=N-acylsphingosine amidohydrolase 3-like;
Name=ACER2; Synonyms=ASAH3L; ORFNames=PP11646;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=16940153; DOI=10.1096/fj.05-5689com;
Xu R., Jin J., Hu W., Sun W., Bielawski J., Szulc Z., Taha T.,
Obeid L.M., Mao C.;
"Golgi alkaline ceramidase regulates cell proliferation and survival
by controlling levels of sphingosine and S1P.";
FASEB J. 20:1813-1825(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION.
PubMed=18945876; DOI=10.1096/fj.08-115634;
Sun W., Hu W., Xu R., Jin J., Szulc Z.M., Zhang G., Galadari S.H.,
Obeid L.M., Mao C.;
"Alkaline ceramidase 2 regulates beta1 integrin maturation and cell
adhesion.";
FASEB J. 23:656-666(2009).
[6]
FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=20089856; DOI=10.1074/jbc.M109.069203;
Sun W., Jin J., Xu R., Hu W., Szulc Z.M., Bielawski J., Obeid L.M.,
Mao C.;
"Substrate specificity, membrane topology, and activity regulation of
human alkaline ceramidase 2 (ACER2).";
J. Biol. Chem. 285:8995-9007(2010).
-!- FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine
and free fatty acid. Unsaturated long-chain ceramides are the best
substrates, saturated long-chain ceramides and unsaturated very
long-chain ceramides are good substrates, whereas saturated very
long-chain ceramides and short-chain ceramides were poor
substrates. The substrate preference is D-erythro-C(18:1)-,
C(20:1)-, C(20:4)-ceramide > D-erythro-C(16:0)-, C(18:0), C(20:0)-
ceramide > D-erythro-C(24:1)-ceramide > D-erythro-C(12:0)-
ceramide, D-erythro-C(14:0)-ceramides > D-erythro-C(24:0)-ceramide
> D-erythro-C(6:0)-ceramide. Inhibits the maturation of protein
glycosylation in the Golgi complex, including that of integrin
beta-1 (ITGB1) and of LAMP1, by increasing the levels of
sphingosine. Inhibits cell adhesion by reducing the level of ITGB1
in the cell surface. May have a role in cell proliferation and
apoptosis that seems to depend on the balance between sphingosine
and sphingosine-1-phosphate. {ECO:0000269|PubMed:16940153,
ECO:0000269|PubMed:18945876, ECO:0000269|PubMed:20089856}.
-!- CATALYTIC ACTIVITY: N-acylsphingosine + H(2)O = a carboxylate +
sphingosine.
-!- ENZYME REGULATION: Specifically activated by lumenal, but not
cytosolic Ca(2+). Inhibited by Zn(2+) or Cu(2+). Mg(2+) or Mn(2+)
have no effect on ceramidase activity.
{ECO:0000269|PubMed:20089856}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=81 uM for D-erythro-C(24:1)-ceramide (at 37 degrees Celsius
and pH 9.0) {ECO:0000269|PubMed:20089856};
Vmax=27 pmol/min/mg enzyme with D-erythro-C(24:1)-ceramide as
substrate {ECO:0000269|PubMed:20089856};
pH dependence:
Optimum pH is 7.5-9.0. {ECO:0000269|PubMed:20089856};
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000269|PubMed:16940153, ECO:0000269|PubMed:20089856}; Multi-
pass membrane protein {ECO:0000269|PubMed:16940153,
ECO:0000269|PubMed:20089856}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q5QJU3-1; Sequence=Displayed;
Name=2;
IsoId=Q5QJU3-2; Sequence=VSP_020033;
Name=3;
IsoId=Q5QJU3-3; Sequence=VSP_020033, VSP_020034, VSP_020035;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in placenta.
{ECO:0000269|PubMed:16940153}.
-!- SIMILARITY: Belongs to the alkaline ceramidase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY312516; AAQ85132.1; -; mRNA.
EMBL; AF370405; AAQ15241.1; -; mRNA.
EMBL; AL158206; CAH73022.1; -; Genomic_DNA.
EMBL; AL391834; CAH73022.1; JOINED; Genomic_DNA.
EMBL; AL391834; CAM21146.1; -; Genomic_DNA.
EMBL; AL158206; CAM21146.1; JOINED; Genomic_DNA.
EMBL; BC092487; AAH92487.1; -; mRNA.
CCDS; CCDS34992.1; -. [Q5QJU3-1]
RefSeq; NP_001010887.2; NM_001010887.2. [Q5QJU3-1]
RefSeq; XP_005251505.1; XM_005251448.3. [Q5QJU3-2]
RefSeq; XP_016870183.1; XM_017014694.1. [Q5QJU3-2]
UniGene; Hs.41379; -.
UniGene; Hs.99785; -.
ProteinModelPortal; Q5QJU3; -.
IntAct; Q5QJU3; 1.
STRING; 9606.ENSP00000342609; -.
BindingDB; Q5QJU3; -.
ChEMBL; CHEMBL2331067; -.
SwissLipids; SLP:000000164; -.
BioMuta; ACER2; -.
DMDM; 110832756; -.
PaxDb; Q5QJU3; -.
PRIDE; Q5QJU3; -.
Ensembl; ENST00000340967; ENSP00000342609; ENSG00000177076. [Q5QJU3-1]
GeneID; 340485; -.
KEGG; hsa:340485; -.
UCSC; uc003zny.2; human. [Q5QJU3-1]
CTD; 340485; -.
DisGeNET; 340485; -.
EuPathDB; HostDB:ENSG00000177076.5; -.
GeneCards; ACER2; -.
H-InvDB; HIX0025758; -.
HGNC; HGNC:23675; ACER2.
MIM; 613492; gene.
neXtProt; NX_Q5QJU3; -.
OpenTargets; ENSG00000177076; -.
PharmGKB; PA164714853; -.
eggNOG; KOG2329; Eukaryota.
eggNOG; ENOG4111RPN; LUCA.
GeneTree; ENSGT00730000110920; -.
HOGENOM; HOG000220878; -.
InParanoid; Q5QJU3; -.
KO; K01441; -.
OMA; KFWPSER; -.
OrthoDB; EOG091G0HT1; -.
PhylomeDB; Q5QJU3; -.
TreeFam; TF313019; -.
BRENDA; 3.5.1.23; 2681.
Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
SABIO-RK; Q5QJU3; -.
ChiTaRS; ACER2; human.
GeneWiki; ACER2; -.
GenomeRNAi; 340485; -.
PRO; PR:Q5QJU3; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000177076; -.
CleanEx; HS_ACER2; -.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0030173; C:integral component of Golgi membrane; IDA:UniProtKB.
GO; GO:0017040; F:ceramidase activity; IDA:UniProtKB.
GO; GO:0071633; F:dihydroceramidase activity; IDA:BHF-UCL.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:BHF-UCL.
GO; GO:0035690; P:cellular response to drug; IEP:BHF-UCL.
GO; GO:0006672; P:ceramide metabolic process; IEA:InterPro.
GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IDA:UniProtKB.
GO; GO:0090285; P:negative regulation of protein glycosylation in Golgi; IMP:UniProtKB.
GO; GO:0010942; P:positive regulation of cell death; IMP:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0032526; P:response to retinoic acid; IDA:UniProtKB.
GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
GO; GO:0046512; P:sphingosine biosynthetic process; IDA:UniProtKB.
InterPro; IPR008901; Ceramidase.
Pfam; PF05875; Ceramidase; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Glycoprotein;
Golgi apparatus; Hydrolase; Lipid metabolism; Membrane; Polymorphism;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 275 Alkaline ceramidase 2.
/FTId=PRO_0000247748.
TOPO_DOM 1 32 Lumenal. {ECO:0000255}.
TRANSMEM 33 53 Helical. {ECO:0000255}.
TOPO_DOM 54 62 Cytoplasmic. {ECO:0000255}.
TRANSMEM 63 83 Helical. {ECO:0000255}.
TOPO_DOM 84 86 Lumenal. {ECO:0000255}.
TRANSMEM 87 107 Helical. {ECO:0000255}.
TOPO_DOM 108 124 Cytoplasmic. {ECO:0000255}.
TRANSMEM 125 142 Helical. {ECO:0000255}.
TOPO_DOM 143 143 Lumenal. {ECO:0000255}.
TRANSMEM 144 164 Helical. {ECO:0000255}.
TOPO_DOM 165 173 Cytoplasmic. {ECO:0000255}.
TRANSMEM 174 194 Helical. {ECO:0000255}.
TOPO_DOM 195 211 Lumenal. {ECO:0000255}.
TRANSMEM 212 232 Helical. {ECO:0000255}.
TOPO_DOM 233 275 Cytoplasmic. {ECO:0000255}.
REGION 1 13 Essential for localization in the Golgi
apparatus and for activity.
CARBOHYD 23 23 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 49 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15498874}.
/FTId=VSP_020033.
VAR_SEQ 169 189 CDNMRVFKLGLFSGLWWTLAL -> HERNQRRRHRKGGQQG
GGDKV (in isoform 3).
{ECO:0000303|PubMed:15498874}.
/FTId=VSP_020034.
VAR_SEQ 190 275 Missing (in isoform 3).
{ECO:0000303|PubMed:15498874}.
/FTId=VSP_020035.
VARIANT 134 134 A -> V (in dbSNP:rs10964136).
/FTId=VAR_027150.
CONFLICT 274 274 I -> T (in Ref. 1; AAQ85132).
{ECO:0000305}.
SEQUENCE 275 AA; 31309 MW; 56FD619B53C296B1 CRC64;
MGAPHWWDQL QAGSSEVDWC EDNYTIVPAI AEFYNTISNV LFFILPPICM CLFRQYATCF
NSGIYLIWTL LVVVGIGSVY FHATLSFLGQ MLDELAVLWV LMCALAMWFP RRYLPKIFRN
DRGRFKVVVS VLSAVTTCLA FVKPAINNIS LMTLGVPCTA LLIAELKRCD NMRVFKLGLF
SGLWWTLALF CWISDRAFCE LLSSFNFPYL HCMWHILICL AAYLGCVCFA YFDAASEIPE
QGPVIKFWPN EKWAFIGVPY VSLLCANKKS SVKIT


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