ACER3_MOUSE
ID ACER3_MOUSE Reviewed; 267 AA.
AC Q9D099; Q542R2; Q9D0X4; Q9D3J4;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Alkaline ceramidase 3;
DE Short=AlkCDase 3;
DE Short=Alkaline CDase 3;
DE EC=3.5.1.- {ECO:0000269|PubMed:26474409};
DE EC=3.5.1.23 {ECO:0000269|PubMed:26474409};
DE AltName: Full=Alkaline phytoceramidase;
DE Short=aPHC;
GN Name=Acer3; Synonyms=Aphc, Phca;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Diencephalon, Embryo, Head, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26474409; DOI=10.1371/journal.pgen.1005591;
RA Wang K., Xu R., Schrandt J., Shah P., Gong Y.Z., Preston C., Wang L.,
RA Yi J.K., Lin C.L., Sun W., Spyropoulos D.D., Rhee S., Li M., Zhou J.,
RA Ge S., Zhang G., Snider A.J., Hannun Y.A., Obeid L.M., Mao C.;
RT "Alkaline Ceramidase 3 Deficiency Results in Purkinje Cell Degeneration and
RT Cerebellar Ataxia Due to Dyshomeostasis of Sphingolipids in the Brain.";
RL PLoS Genet. 11:E1005591-E1005591(2015).
RN [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26938296; DOI=10.1038/cddis.2016.36;
RA Wang K., Xu R., Snider A.J., Schrandt J., Li Y., Bialkowska A.B., Li M.,
RA Zhou J., Hannun Y.A., Obeid L.M., Yang V.W., Mao C.;
RT "Alkaline ceramidase 3 deficiency aggravates colitis and colitis-associated
RT tumorigenesis in mice by hyperactivating the innate immune system.";
RL Cell Death Dis. 7:E2124-E2124(2016).
CC -!- FUNCTION: Endoplasmic reticulum and Golgi ceramidase that catalyzes the
CC hydrolysis of unsaturated long-chain C18:1-, C20:1- and C20:4-
CC ceramides, dihydroceramides and phytoceramides into sphingoid bases
CC like sphingosine and free fatty acids at alkaline pH (PubMed:26474409).
CC Ceramides, sphingosine, and its phosphorylated form sphingosine-1-
CC phosphate are bioactive lipids that mediate cellular signaling pathways
CC regulating several biological processes including cell proliferation,
CC apoptosis and differentiation (PubMed:26474409). Controls the
CC generation of sphingosine in erythrocytes, and thereby sphingosine-1-
CC phosphate in plasma (By similarity). Through the regulation of
CC ceramides and sphingosine-1-phosphate homeostasis in the brain may play
CC a role in neurons survival and function (PubMed:26474409). By
CC regulating the levels of pro-inflammatory ceramides in immune cells and
CC tissues, may modulate the inflammatory response (PubMed:26938296).
CC {ECO:0000250|UniProtKB:Q9NUN7, ECO:0000269|PubMed:26474409,
CC ECO:0000269|PubMed:26938296, ECO:0000303|PubMed:26474409}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-(4R)-4-hydroxysphinganine + H2O = (4R)-
CC hydroxysphinganine + a fatty acid; Xref=Rhea:RHEA:33555,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28868, ChEBI:CHEBI:31998,
CC ChEBI:CHEBI:64124; Evidence={ECO:0000269|PubMed:26474409};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33556;
CC Evidence={ECO:0000305|PubMed:26474409};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sphing-4-enine =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + sphing-4-enine;
CC Xref=Rhea:RHEA:45348, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:57756, ChEBI:CHEBI:85198;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45349;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sphinganine =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + sphinganine;
CC Xref=Rhea:RHEA:45376, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:57817, ChEBI:CHEBI:85206;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45377;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-(4R)-
CC hydroxysphinganine = (4R)-hydroxysphinganine + (5Z,8Z,11Z,14Z)-
CC eicosatetraenoate; Xref=Rhea:RHEA:45380, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:64124, ChEBI:CHEBI:85207;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45381;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(11Z-eicosenoyl)-sphing-4-enine = (11Z)-eicosenoate +
CC sphing-4-enine; Xref=Rhea:RHEA:45356, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32426, ChEBI:CHEBI:57756, ChEBI:CHEBI:85284;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45357;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(11Z-eicosenoyl)-sphinganine = (11Z)-eicosenoate +
CC sphinganine; Xref=Rhea:RHEA:45360, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32426, ChEBI:CHEBI:57817, ChEBI:CHEBI:85285;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45361;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(11Z-eicosenoyl)-(4R)-hydroxysphinganine = (11Z)-
CC eicosenoate + (4R)-hydroxysphinganine; Xref=Rhea:RHEA:45364,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:32426, ChEBI:CHEBI:64124,
CC ChEBI:CHEBI:85286; Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45365;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-sphing-4-enine = (9Z)-octadecenoate
CC + sphing-4-enine; Xref=Rhea:RHEA:41299, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57756, ChEBI:CHEBI:77996;
CC Evidence={ECO:0000269|PubMed:26474409};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41300;
CC Evidence={ECO:0000305|PubMed:26474409};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-sphinganine = (9Z)-octadecenoate +
CC sphinganine; Xref=Rhea:RHEA:45372, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57817, ChEBI:CHEBI:74100;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45373;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-(4R)-hydroxysphinganine = (4R)-
CC hydroxysphinganine + (9Z)-octadecenoate; Xref=Rhea:RHEA:45368,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:64124,
CC ChEBI:CHEBI:85204; Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45369;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine;
CC Xref=Rhea:RHEA:20856, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:57756; EC=3.5.1.23;
CC Evidence={ECO:0000269|PubMed:26474409};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20857;
CC Evidence={ECO:0000305|PubMed:26474409};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphinganine + H2O = a fatty acid + sphinganine;
CC Xref=Rhea:RHEA:33551, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:31488, ChEBI:CHEBI:57817;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33552;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC -!- ACTIVITY REGULATION: Activated by Ca(2+) and inhibited by Zn(2+).
CC {ECO:0000250|UniProtKB:Q9NUN7}.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:26474409}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NUN7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9NUN7}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9NUN7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9NUN7}.
CC -!- TISSUE SPECIFICITY: Up-regulated with age in cerebeLlum and cerebrum.
CC {ECO:0000269|PubMed:26474409}.
CC -!- INDUCTION: Down-regulated in immune cells and colonic epithelial cells
CC by lipopolysaccharides/LPS. {ECO:0000269|PubMed:26938296}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice are viable and do not
CC display overt phenotype with regard to fertility, body weight and
CC anatomy (PubMed:26474409). They exhibit a decrease in ceramidase
CC activity in brain, liver and lung tissues leading to the age-dependent
CC accumulation of unsaturated long-chain C18:1-ceramides and the
CC concomitant decrease in sphingosine and sphingosine-1-phosphate
CC (PubMed:26474409). This is associated with a premature degeneration of
CC Purkinje cells and age-dependent defects in motor coordination, skilled
CC hindlimb function and balance capabilities (PubMed:26474409). Knockout
CC mice also display exacerbated systemic inflammatory response
CC (PubMed:26938296). {ECO:0000269|PubMed:26474409,
CC ECO:0000269|PubMed:26938296}.
CC -!- SIMILARITY: Belongs to the alkaline ceramidase family. {ECO:0000305}.
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DR EMBL; AK004287; BAB23250.1; -; mRNA.
DR EMBL; AK011668; BAB27768.1; -; mRNA.
DR EMBL; AK017361; BAB30708.1; -; mRNA.
DR EMBL; AK080977; BAC38101.1; -; mRNA.
DR EMBL; AK150629; BAE29719.1; -; mRNA.
DR EMBL; AK162403; BAE36897.1; -; mRNA.
DR CCDS; CCDS21468.1; -.
DR RefSeq; NP_079684.2; NM_025408.2.
DR AlphaFoldDB; Q9D099; -.
DR SMR; Q9D099; -.
DR STRING; 10090.ENSMUSP00000033020; -.
DR PhosphoSitePlus; Q9D099; -.
DR MaxQB; Q9D099; -.
DR PaxDb; Q9D099; -.
DR PRIDE; Q9D099; -.
DR ProteomicsDB; 285837; -.
DR Antibodypedia; 53464; 126 antibodies from 25 providers.
DR DNASU; 66190; -.
DR Ensembl; ENSMUST00000033020; ENSMUSP00000033020; ENSMUSG00000030760.
DR GeneID; 66190; -.
DR KEGG; mmu:66190; -.
DR UCSC; uc009ikg.1; mouse.
DR CTD; 55331; -.
DR MGI; MGI:1913440; Acer3.
DR VEuPathDB; HostDB:ENSMUSG00000030760; -.
DR eggNOG; KOG2329; Eukaryota.
DR GeneTree; ENSGT00730000110920; -.
DR HOGENOM; CLU_063293_3_2_1; -.
DR InParanoid; Q9D099; -.
DR OMA; IMFEPLR; -.
DR OrthoDB; 969354at2759; -.
DR PhylomeDB; Q9D099; -.
DR TreeFam; TF313019; -.
DR BRENDA; 3.5.1.23; 3474.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 66190; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Acer3; mouse.
DR PRO; PR:Q9D099; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D099; protein.
DR Bgee; ENSMUSG00000030760; Expressed in humerus cartilage element and 221 other tissues.
DR ExpressionAtlas; Q9D099; baseline and differential.
DR Genevisible; Q9D099; MM.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0102121; F:ceramidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071633; F:dihydroceramidase activity; ISS:UniProtKB.
DR GO; GO:0017040; F:N-acylsphingosine amidohydrolase activity; ISS:UniProtKB.
DR GO; GO:0070774; F:phytoceramidase activity; IMP:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0046514; P:ceramide catabolic process; IMP:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
DR GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR GO; GO:0071602; P:phytosphingosine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0043067; P:regulation of programmed cell death; ISS:UniProtKB.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR008901; ACER.
DR PANTHER; PTHR46187; PTHR46187; 1.
DR Pfam; PF05875; Ceramidase; 1.
PE 1: Evidence at protein level;
KW Calcium; Endoplasmic reticulum; Golgi apparatus; Hydrolase;
KW Lipid metabolism; Membrane; Metal-binding; Reference proteome;
KW Sphingolipid metabolism; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..267
FT /note="Alkaline ceramidase 3"
FT /id="PRO_0000212464"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 34..55
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT TOPO_DOM 56..61
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT TOPO_DOM 83..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT TOPO_DOM 109..118
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT TOPO_DOM 140..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT TOPO_DOM 163..173
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT TOPO_DOM 195..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT TOPO_DOM 237..267
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 22
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT CONFLICT 110
FT /note="C -> F (in Ref. 1; BAB23250)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="E -> D (in Ref. 1; BAB30708)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 31565 MW; 4EF7E912CBB4E9BB CRC64;
MAPAVDRKGY WGPTTSTLDW CEENYVVTLF VAEFWNTVSN LIMIIPPIFG AIQGIRDRLE
KRYIAAYLAL TVVGMGSWCF HMTLKYEMQL LDELPMIYSC CIFVYCMFEC FKTKSSINYH
LLFTLFLYSL TVTTIYLKVK EPIFHQVMYG MLVFTLVLRS IYIVTWVYPW LRGLGYTSLT
VFLLGFLLWN IDNIFCDSLR NFRKRVPPVL GVTTQFHAWW HILTGLGSYL HILFSLYTRT
LYLRYRPKVK FLFGIWPAVM FEPQRKH
