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Alkaline ceramidase 3 (AlkCDase 3) (Alkaline CDase 3) (EC 3.5.1.-) (Alkaline dihydroceramidase SB89) (Alkaline phytoceramidase) (aPHC)

 ACER3_HUMAN             Reviewed;         267 AA.
Q9NUN7; B2RC99;
14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
27-SEP-2017, entry version 136.
RecName: Full=Alkaline ceramidase 3;
Short=AlkCDase 3;
Short=Alkaline CDase 3;
EC=3.5.1.-;
AltName: Full=Alkaline dihydroceramidase SB89;
AltName: Full=Alkaline phytoceramidase;
Short=aPHC;
Name=ACER3; Synonyms=APHC, PHCA;
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), AND CHARACTERIZATION.
TISSUE=Kidney;
PubMed=11356846; DOI=10.1074/jbc.M102818200;
Mao C., Xu R., Szulc Z.M., Bielawska A., Galadari S.H., Obeid L.M.;
"Cloning and characterization of a novel human alkaline ceramidase. A
mammalian enzyme that hydrolyzes phytoceramide.";
J. Biol. Chem. 276:26577-26588(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Li N., Zhang W., Wan T., Chen T., Cao X.;
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Placenta, and Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye;
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).
-!- FUNCTION: Hydrolyzes only phytoceramide into phytosphingosine and
free fatty acid. Does not have reverse activity.
-!- ENZYME REGULATION: Activated by Ca(2+) and inhibited by Zn(2+).
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein. Golgi apparatus membrane; Multi-pass membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NUN7-1; Sequence=Displayed;
Name=2;
IsoId=Q9NUN7-2; Sequence=VSP_039162, VSP_039163;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Highest expression in
placenta.
-!- SIMILARITY: Belongs to the alkaline ceramidase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF214454; AAK71923.1; -; mRNA.
EMBL; AF327353; AAL56013.1; -; mRNA.
EMBL; AK002100; BAA92085.1; -; mRNA.
EMBL; AK315000; BAG37496.1; -; mRNA.
EMBL; AP000752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP002498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP003119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471076; EAW75010.1; -; Genomic_DNA.
EMBL; BC073853; AAH73853.1; -; mRNA.
CCDS; CCDS8247.1; -. [Q9NUN7-1]
RefSeq; NP_060837.3; NM_018367.6. [Q9NUN7-1]
UniGene; Hs.23862; -.
UniGene; Hs.720248; -.
ProteinModelPortal; Q9NUN7; -.
BioGrid; 120612; 2.
IntAct; Q9NUN7; 1.
STRING; 9606.ENSP00000434480; -.
SwissLipids; SLP:000000680; -.
iPTMnet; Q9NUN7; -.
PhosphoSitePlus; Q9NUN7; -.
BioMuta; ACER3; -.
DMDM; 296439452; -.
PaxDb; Q9NUN7; -.
PeptideAtlas; Q9NUN7; -.
PRIDE; Q9NUN7; -.
TopDownProteomics; Q9NUN7-1; -. [Q9NUN7-1]
DNASU; 55331; -.
Ensembl; ENST00000532485; ENSP00000434480; ENSG00000078124. [Q9NUN7-1]
GeneID; 55331; -.
KEGG; hsa:55331; -.
UCSC; uc009yum.2; human. [Q9NUN7-1]
CTD; 55331; -.
DisGeNET; 55331; -.
EuPathDB; HostDB:ENSG00000078124.11; -.
GeneCards; ACER3; -.
H-InvDB; HIX0021493; -.
HGNC; HGNC:16066; ACER3.
neXtProt; NX_Q9NUN7; -.
OpenTargets; ENSG00000078124; -.
PharmGKB; PA33256; -.
eggNOG; KOG2329; Eukaryota.
eggNOG; ENOG4111RPN; LUCA.
GeneTree; ENSGT00730000111189; -.
HOGENOM; HOG000192011; -.
InParanoid; Q9NUN7; -.
KO; K04711; -.
OMA; VFHQVMY; -.
OrthoDB; EOG091G0DCZ; -.
PhylomeDB; Q9NUN7; -.
TreeFam; TF313019; -.
BRENDA; 3.5.1.23; 2681.
Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
ChiTaRS; ACER3; human.
GeneWiki; ACER3; -.
GenomeRNAi; 55331; -.
PRO; PR:Q9NUN7; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000078124; -.
CleanEx; HS_ACER3; -.
ExpressionAtlas; Q9NUN7; baseline and differential.
Genevisible; Q9NUN7; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0030173; C:integral component of Golgi membrane; IDA:UniProtKB.
GO; GO:0070774; F:phytoceramidase activity; IDA:UniProtKB.
GO; GO:0006672; P:ceramide metabolic process; IEA:InterPro.
GO; GO:0071602; P:phytosphingosine biosynthetic process; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP: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; Endoplasmic reticulum;
Glycoprotein; Golgi apparatus; Hydrolase; Membrane;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 267 Alkaline ceramidase 3.
/FTId=PRO_0000212463.
TRANSMEM 29 51 Helical. {ECO:0000255}.
TRANSMEM 63 84 Helical. {ECO:0000255}.
TRANSMEM 94 111 Helical. {ECO:0000255}.
TRANSMEM 118 137 Helical. {ECO:0000255}.
TRANSMEM 147 169 Helical. {ECO:0000255}.
TRANSMEM 174 196 Helical. {ECO:0000255}.
TRANSMEM 216 238 Helical. {ECO:0000255}.
CARBOHYD 24 24 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 133 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_039162.
VAR_SEQ 134 145 TVYLKVKEPIFH -> MAQSRLIGTSTS (in isoform
2). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_039163.
CONFLICT 52 52 V -> I (in Ref. 1; AAK71923, 2; AAL56013,
3; BAG37496, 5; EAW75010 and 6;
AAH73853). {ECO:0000305}.
SEQUENCE 267 AA; 31552 MW; CFD2A901F12A5918 CRC64;
MAPAADREGY WGPTTSTLDW CEENYSVTWY IAEFWNTVSN LIMIIPPMFG AVQSVRDGLE
KRYIASYLAL TVVGMGSWCF HMTLKYEMQL LDELPMIYSC CIFVYCMFEC FKIKNSVNYH
LLFTLVLFSL IVTTVYLKVK EPIFHQVMYG MLVFTLVLRS IYIVTWVYPW LRGLGYTSLG
IFLLGFLFWN IDNIFCESLR NFRKKVPPII GITTQFHAWW HILTGLGSYL HILFSLYTRT
LYLRYRPKVK FLFGIWPVIL FEPLRKH


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