ACER2_MOUSE
ID ACER2_MOUSE Reviewed; 275 AA.
AC Q8VD53; Q6PB92; Q8BUG3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Alkaline ceramidase 2 {ECO:0000305};
DE Short=AlkCDase 2;
DE Short=Alkaline CDase 2;
DE Short=maCER2;
DE EC=3.5.1.- {ECO:0000269|PubMed:29401619};
DE EC=3.5.1.23 {ECO:0000269|PubMed:29401619};
DE AltName: Full=Acylsphingosine deacylase 3-like;
DE AltName: Full=Cancer-related gene liver 1 protein;
DE Short=CRG-L1;
DE AltName: Full=N-acylsphingosine amidohydrolase 3-like;
GN Name=Acer2 {ECO:0000312|MGI:MGI:1920932}; Synonyms=Asah3l;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Hepatoma;
RX PubMed=11420682; DOI=10.1038/sj.onc.1204391;
RA Graveel C.R., Jatkoe T., Madore S.J., Holt A.L., Farnham P.J.;
RT "Expression profiling and identification of novel genes in hepatocellular
RT carcinomas.";
RL Oncogene 20:2704-2712(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=16940153; DOI=10.1096/fj.05-5689com;
RA Xu R., Jin J., Hu W., Sun W., Bielawski J., Szulc Z., Taha T., Obeid L.M.,
RA Mao C.;
RT "Golgi alkaline ceramidase regulates cell proliferation and survival by
RT controlling levels of sphingosine and S1P.";
RL FASEB J. 20:1813-1825(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-215.
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=29401619; DOI=10.1096/fj.201700445rr;
RA Li F., Xu R., Low B.E., Lin C.L., Garcia-Barros M., Schrandt J., Mileva I.,
RA Snider A., Luo C.K., Jiang X.C., Li M.S., Hannun Y.A., Obeid L.M.,
RA Wiles M.V., Mao C.;
RT "Alkaline ceramidase 2 is essential for the homeostasis of plasma sphingoid
RT bases and their phosphates.";
RL FASEB J. 32:3058-3069(2018).
CC -!- FUNCTION: Golgi ceramidase that catalyzes the hydrolysis of ceramides
CC into sphingoid bases like sphingosine and free fatty acids at alkaline
CC pH (PubMed:29401619). Ceramides, sphingosine, and its phosphorylated
CC form sphingosine-1-phosphate are bioactive lipids that mediate cellular
CC signaling pathways regulating several biological processes including
CC cell proliferation, apoptosis and differentiation (PubMed:29401619).
CC Has a better catalytic efficiency towards unsaturated long-chain
CC ceramides, including C18:1-, C20:1- and C24:1-ceramides (By similarity)
CC (PubMed:29401619). Saturated long-chain ceramides and unsaturated very
CC long-chain ceramides are also good substrates, whereas saturated very
CC long-chain ceramides and short-chain ceramides are poor substrates.
CC Also hydrolyzes dihydroceramides to produce dihydrosphingosine (By
CC similarity). It is the ceramidase that controls the levels of
CC circulating sphingosine-1-phosphate and dihydrosphingosine-1-phosphate
CC in plasma through their production by hematopoietic cells
CC (PubMed:29401619). Regulates cell proliferation, autophagy and
CC apoptosis by the production of sphingosine and sphingosine-1-phosphate.
CC As part of a p53/TP53-dependent pathway, promotes for instance
CC autophagy and apoptosis in response to DNA damage. Through the
CC production of sphingosine, may also regulate the function of the Golgi
CC complex and regulate the glycosylation of proteins (By similarity).
CC {ECO:0000250|UniProtKB:Q5QJU3, ECO:0000269|PubMed:29401619,
CC ECO:0000303|PubMed:29401619}.
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:29401619};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20857;
CC Evidence={ECO:0000269|PubMed:29401619};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(15Z-tetracosenoyl)-sphing-4-enine = (15Z)-
CC tetracosenoate + sphing-4-enine; Xref=Rhea:RHEA:41267,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:32392, ChEBI:CHEBI:57756,
CC ChEBI:CHEBI:74450; Evidence={ECO:0000250|UniProtKB:Q5QJU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41268;
CC Evidence={ECO:0000250|UniProtKB:Q5QJU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-eicosanoyl-sphing-4-enine = eicosanoate + sphing-4-
CC enine; Xref=Rhea:RHEA:41275, ChEBI:CHEBI:15377, ChEBI:CHEBI:32360,
CC ChEBI:CHEBI:57756, ChEBI:CHEBI:72962;
CC Evidence={ECO:0000250|UniProtKB:Q5QJU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41276;
CC Evidence={ECO:0000250|UniProtKB:Q5QJU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-octadecanoylsphing-4-enine = octadecanoate + sphing-4-
CC enine; Xref=Rhea:RHEA:41279, ChEBI:CHEBI:15377, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:57756, ChEBI:CHEBI:72961;
CC Evidence={ECO:0000250|UniProtKB:Q5QJU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41280;
CC Evidence={ECO:0000250|UniProtKB:Q5QJU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoylsphing-4-enine = hexadecanoate + sphing-4-
CC enine; Xref=Rhea:RHEA:38891, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57756, ChEBI:CHEBI:72959;
CC Evidence={ECO:0000250|UniProtKB:Q5QJU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38892;
CC Evidence={ECO:0000250|UniProtKB:Q5QJU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-tetradecanoylsphing-4-enine = sphing-4-enine +
CC tetradecanoate; Xref=Rhea:RHEA:41287, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57756, ChEBI:CHEBI:72957;
CC Evidence={ECO:0000250|UniProtKB:Q5QJU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41288;
CC Evidence={ECO:0000250|UniProtKB:Q5QJU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-dodecanoylsphing-4-enine = dodecanoate + sphing-4-
CC enine; Xref=Rhea:RHEA:41291, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262,
CC ChEBI:CHEBI:57756, ChEBI:CHEBI:72956;
CC Evidence={ECO:0000250|UniProtKB:Q5QJU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41292;
CC Evidence={ECO:0000250|UniProtKB:Q5QJU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-tetracosanoyl-sphing-4-enine = sphing-4-enine +
CC tetracosanoate; Xref=Rhea:RHEA:41283, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:57756, ChEBI:CHEBI:72965;
CC Evidence={ECO:0000250|UniProtKB:Q5QJU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41284;
CC Evidence={ECO:0000250|UniProtKB:Q5QJU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(hexanoyl)sphing-4-enine = hexanoate + sphing-4-enine;
CC Xref=Rhea:RHEA:41295, ChEBI:CHEBI:15377, ChEBI:CHEBI:17120,
CC ChEBI:CHEBI:57756, ChEBI:CHEBI:63867;
CC Evidence={ECO:0000250|UniProtKB:Q5QJU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41296;
CC Evidence={ECO:0000250|UniProtKB:Q5QJU3};
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:0000250|UniProtKB:Q5QJU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41300;
CC Evidence={ECO:0000250|UniProtKB:Q5QJU3};
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:0000269|PubMed:29401619};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33552;
CC Evidence={ECO:0000269|PubMed:29401619};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:29401619}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q5QJU3}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5QJU3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VD53-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VD53-2; Sequence=VSP_020036;
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in lung.
CC {ECO:0000269|PubMed:29401619}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice display no overt
CC phenotype (PubMed:29401619). Reduced levels of sphingosine,
CC dihydrosphingosine, sphingosine-1-phosphate and dihydrosphingosine -1-
CC phosphate are observed in plasma, erythrocytes and platelets
CC (PubMed:29401619). {ECO:0000269|PubMed:29401619}.
CC -!- SIMILARITY: Belongs to the alkaline ceramidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39416.1; Type=Miscellaneous discrepancy; Note=Chimera.; Evidence={ECO:0000305};
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DR EMBL; AF282864; AAL40408.1; -; mRNA.
DR EMBL; AY312515; AAQ85131.1; -; mRNA.
DR EMBL; BC059819; AAH59819.1; -; mRNA.
DR EMBL; AK085306; BAC39416.1; ALT_SEQ; mRNA.
DR CCDS; CCDS18311.1; -. [Q8VD53-1]
DR CCDS; CCDS71417.1; -. [Q8VD53-2]
DR RefSeq; NP_001277470.1; NM_001290541.1. [Q8VD53-2]
DR RefSeq; NP_001277472.1; NM_001290543.1.
DR RefSeq; NP_647467.1; NM_139306.3. [Q8VD53-1]
DR AlphaFoldDB; Q8VD53; -.
DR SMR; Q8VD53; -.
DR STRING; 10090.ENSMUSP00000040048; -.
DR GlyGen; Q8VD53; 1 site.
DR MaxQB; Q8VD53; -.
DR PaxDb; Q8VD53; -.
DR PRIDE; Q8VD53; -.
DR Antibodypedia; 2873; 68 antibodies from 20 providers.
DR Ensembl; ENSMUST00000045224; ENSMUSP00000040048; ENSMUSG00000038007. [Q8VD53-1]
DR Ensembl; ENSMUST00000084433; ENSMUSP00000081473; ENSMUSG00000038007. [Q8VD53-2]
DR GeneID; 230379; -.
DR KEGG; mmu:230379; -.
DR UCSC; uc008tmf.3; mouse. [Q8VD53-1]
DR UCSC; uc012dgs.2; mouse. [Q8VD53-2]
DR CTD; 340485; -.
DR MGI; MGI:1920932; Acer2.
DR VEuPathDB; HostDB:ENSMUSG00000038007; -.
DR eggNOG; KOG2329; Eukaryota.
DR GeneTree; ENSGT00730000110920; -.
DR HOGENOM; CLU_088280_0_0_1; -.
DR InParanoid; Q8VD53; -.
DR OMA; ALFCWIT; -.
DR OrthoDB; 969354at2759; -.
DR PhylomeDB; Q8VD53; -.
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; 230379; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Acer2; mouse.
DR PRO; PR:Q8VD53; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8VD53; protein.
DR Bgee; ENSMUSG00000038007; Expressed in urinary bladder urothelium and 214 other tissues.
DR Genevisible; Q8VD53; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0102121; F:ceramidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071633; F:dihydroceramidase activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017040; F:N-acylsphingosine amidohydrolase activity; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0046514; P:ceramide catabolic process; ISS:UniProtKB.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; ISO:MGI.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0060049; P:regulation of protein glycosylation; IEA:Ensembl.
DR GO; GO:0032526; P:response to retinoic acid; ISO:MGI.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR008901; ACER.
DR PANTHER; PTHR46139; PTHR46139; 1.
DR Pfam; PF05875; Ceramidase; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Glycoprotein; Golgi apparatus; Hydrolase;
KW Lipid metabolism; Membrane; Metal-binding; Reference proteome;
KW Sphingolipid metabolism; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..275
FT /note="Alkaline ceramidase 2"
FT /id="PRO_0000247749"
FT TOPO_DOM 1..32
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..86
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..211
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 18
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 122..167
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020036"
SQ SEQUENCE 275 AA; 31369 MW; 8FCC755B4949B9DF CRC64;
MGAPHWWDHL RAGSSEVDWC EDNYTIVPAI AEFYNTISNV LFFILPPICM CLFRQYATCF
NSGIYLIWTL LVVVGIGSVY FHATLSFLGQ MLDELAILWV LMCALAMWFP RRYLPKIFRN
DRGRFKAVVC VLSAITTCLA FIKPAINNIS LMILGLPCTA LLVAELKRCD NVRVFKLGLF
SGLWWTLALF CWISDQAFCE LLSSFHFPYL HCVWHILICL ASYLGCVCFA YFDAASEIPE
QGPVIRFWPS EKWAFIGVPY VSLLCAHKKS PVKIT
