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Protein

Alkaline ceramidase 3

Gene

Acer3

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

Functioni

Hydrolyzes only phytoceramide into phytosphingosine and free fatty acid. Does not have reverse activity (By similarity).By similarity

Enzyme regulationi

Activated by Ca2+ and inhibited by Zn2+.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.5.1.23. 3474.
ReactomeiR-MMU-1660661. Sphingolipid de novo biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkaline ceramidase 3 (EC:3.5.1.-)
Short name:
AlkCDase 3
Short name:
Alkaline CDase 3
Alternative name(s):
Alkaline phytoceramidase
Short name:
aPHC
Gene namesi
Name:Acer3
Synonyms:Aphc, Phca
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1913440. Acer3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei30 – 5223HelicalSequence analysisAdd
BLAST
Transmembranei65 – 8420HelicalSequence analysisAdd
BLAST
Transmembranei94 – 11118HelicalSequence analysisAdd
BLAST
Transmembranei118 – 13720HelicalSequence analysisAdd
BLAST
Transmembranei147 – 16923HelicalSequence analysisAdd
BLAST
Transmembranei174 – 19623HelicalSequence analysisAdd
BLAST
Transmembranei216 – 23823HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 267267Alkaline ceramidase 3PRO_0000212464Add
BLAST

Proteomic databases

MaxQBiQ9D099.
PaxDbiQ9D099.
PRIDEiQ9D099.

PTM databases

PhosphoSiteiQ9D099.

Expressioni

Gene expression databases

BgeeiQ9D099.
CleanExiMM_PHCA.
ExpressionAtlasiQ9D099. baseline and differential.
GenevisibleiQ9D099. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033020.

Structurei

3D structure databases

ProteinModelPortaliQ9D099.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alkaline ceramidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2329. Eukaryota.
ENOG4111RPN. LUCA.
GeneTreeiENSGT00730000111189.
HOGENOMiHOG000192011.
InParanoidiQ9D099.
KOiK04711.
OMAiVYIVLWV.
OrthoDBiEOG7K9K3J.
PhylomeDBiQ9D099.
TreeFamiTF313019.

Family and domain databases

InterProiIPR008901. Ceramidase.
[Graphical view]
PfamiPF05875. Ceramidase. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D099-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPAVDRKGY WGPTTSTLDW CEENYVVTLF VAEFWNTVSN LIMIIPPIFG
60 70 80 90 100
AIQGIRDRLE KRYIAAYLAL TVVGMGSWCF HMTLKYEMQL LDELPMIYSC
110 120 130 140 150
CIFVYCMFEC FKTKSSINYH LLFTLFLYSL TVTTIYLKVK EPIFHQVMYG
160 170 180 190 200
MLVFTLVLRS IYIVTWVYPW LRGLGYTSLT VFLLGFLLWN IDNIFCDSLR
210 220 230 240 250
NFRKRVPPVL GVTTQFHAWW HILTGLGSYL HILFSLYTRT LYLRYRPKVK
260
FLFGIWPAVM FEPQRKH
Length:267
Mass (Da):31,565
Last modified:June 1, 2001 - v1
Checksum:i4EF7E912CBB4E9BB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101C → F in BAB23250 (PubMed:16141072).Curated
Sequence conflicti262 – 2621E → D in BAB30708 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004287 mRNA. Translation: BAB23250.1.
AK011668 mRNA. Translation: BAB27768.1.
AK017361 mRNA. Translation: BAB30708.1.
AK080977 mRNA. Translation: BAC38101.1.
AK150629 mRNA. Translation: BAE29719.1.
AK162403 mRNA. Translation: BAE36897.1.
CCDSiCCDS21468.1.
RefSeqiNP_079684.2. NM_025408.2.
UniGeneiMm.334041.

Genome annotation databases

EnsembliENSMUST00000033020; ENSMUSP00000033020; ENSMUSG00000030760.
GeneIDi66190.
KEGGimmu:66190.
UCSCiuc009ikg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004287 mRNA. Translation: BAB23250.1.
AK011668 mRNA. Translation: BAB27768.1.
AK017361 mRNA. Translation: BAB30708.1.
AK080977 mRNA. Translation: BAC38101.1.
AK150629 mRNA. Translation: BAE29719.1.
AK162403 mRNA. Translation: BAE36897.1.
CCDSiCCDS21468.1.
RefSeqiNP_079684.2. NM_025408.2.
UniGeneiMm.334041.

3D structure databases

ProteinModelPortaliQ9D099.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033020.

PTM databases

PhosphoSiteiQ9D099.

Proteomic databases

MaxQBiQ9D099.
PaxDbiQ9D099.
PRIDEiQ9D099.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033020; ENSMUSP00000033020; ENSMUSG00000030760.
GeneIDi66190.
KEGGimmu:66190.
UCSCiuc009ikg.1. mouse.

Organism-specific databases

CTDi55331.
MGIiMGI:1913440. Acer3.

Phylogenomic databases

eggNOGiKOG2329. Eukaryota.
ENOG4111RPN. LUCA.
GeneTreeiENSGT00730000111189.
HOGENOMiHOG000192011.
InParanoidiQ9D099.
KOiK04711.
OMAiVYIVLWV.
OrthoDBiEOG7K9K3J.
PhylomeDBiQ9D099.
TreeFamiTF313019.

Enzyme and pathway databases

BRENDAi3.5.1.23. 3474.
ReactomeiR-MMU-1660661. Sphingolipid de novo biosynthesis.

Miscellaneous databases

NextBioi320899.
PROiQ9D099.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D099.
CleanExiMM_PHCA.
ExpressionAtlasiQ9D099. baseline and differential.
GenevisibleiQ9D099. MM.

Family and domain databases

InterProiIPR008901. Ceramidase.
[Graphical view]
PfamiPF05875. Ceramidase. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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: Bone marrow, Diencephalon, Embryo, Head and Thymus.

Entry informationi

Entry nameiACER3_MOUSE
AccessioniPrimary (citable) accession number: Q9D099
Secondary accession number(s): Q542R2, Q9D0X4, Q9D3J4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: June 1, 2001
Last modified: November 11, 2015
This is version 104 of the entry and version 1 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.