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[1]
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NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1074/jbc.M303875200; PubMed=12783875 [NCBI, ExPASy, EBI, Israel, Japan]
Mao C.,
Xu R.,
Szulc Z.M.,
Bielawski J.,
Becker K.P.,
Bielawska A.,
Galadari S.H.,
Hu W.,
Obeid L.M.;
"Cloning and characterization of a mouse endoplasmic reticulum alkaline ceramidase: an enzyme that preferentially regulates metabolism of very long chain ceramides.";
J. Biol. Chem. 278:31184-31191(2003).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Skin, and Tongue;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
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- FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid at an optimal pH of 8.0. Has a highly restricted substrate specificity for the natural stereoisomer of ceramide with D-erythro-sphingosine but not D-ribo-phytosphingosine or D-erythro-dihydrosphingosine as a backbone. May have a role in regulating the levels of bioactive lipids ceramide and sphingosine 1-phosphate, as well as complex sphingolipids.
- CATALYTIC ACTIVITY: N-acylsphingosine + H2O = a carboxylate + sphingosine.
- ENZYME REGULATION: Inhibited by sphingosine. Inhibited by Mn(2+), Zn(2+), and Cu(2+) in a dose-dependent manner. Slightly activated by Ca(2+) in a dose-dependent manner.
- BIOPHYSICOCHEMICAL PROPERTIES:
- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein.
- TISSUE SPECIFICITY: Highly expressed in skin. Weakly or not expressed in other tissues.
- SIMILARITY: Belongs to the alkaline ceramidase family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 273 AA [This is the length of the unprocessed precursor] |
Molecular weight: 32082 Da [This is the MW of the unprocessed precursor] |
CRC64: 0B84D015D7870219 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MHVPGTRAKM SSIFAYQSSE VDWCESNFQH SELVAEFYNT FSNVFFLIFG PLMMFLMHPY
70 80 90 100 110 120
AQKRTRCFYG VSVLFMLIGL FSMYFHMTLS FLGQLLDEIS ILWLLASGYS VWLPRCYFPK
130 140 150 160 170 180
FVKGNRFYFS CLVTITTIIS TFLTFVKPTV NAYALNSIAI HILYIVRTEY KKIRDDDLRH
190 200 210 220 230 240
LIAVSVVLWA AALTSWISDR VLCSFWQRIH FYYLHSIWHV LISITFPYGI VTMALVDAKY
250 260 270
EMPDKTLKVH YWPRDSWVIG LPYVEIQEND KNC
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Q8R4X1 in FASTA format |
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