SGMC_DICDI
ID SGMC_DICDI Reviewed; 446 AA.
AC Q54SR8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Sphingomyelinase phosphodiesterase C;
DE EC=3.1.4.-;
DE AltName: Full=ASM-like phosphodiesterase C;
DE Flags: Precursor;
GN Name=sgmC; ORFNames=DDB_G0282265;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q92484};
CC Note=Binds 2 Zn(2+) per subunit. {ECO:0000250|UniProtKB:Q92484};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the acid sphingomyelinase family. {ECO:0000305}.
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DR EMBL; AAFI02000046; EAL66338.1; -; Genomic_DNA.
DR RefSeq; XP_640317.1; XM_635225.1.
DR AlphaFoldDB; Q54SR8; -.
DR SMR; Q54SR8; -.
DR STRING; 44689.DDB0232050; -.
DR PaxDb; Q54SR8; -.
DR EnsemblProtists; EAL66338; EAL66338; DDB_G0282265.
DR GeneID; 8623493; -.
DR KEGG; ddi:DDB_G0282265; -.
DR dictyBase; DDB_G0282265; sgmC.
DR eggNOG; KOG3770; Eukaryota.
DR HOGENOM; CLU_014743_0_2_1; -.
DR InParanoid; Q54SR8; -.
DR OMA; DSPWHLI; -.
DR PhylomeDB; Q54SR8; -.
DR PRO; PR:Q54SR8; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central.
DR GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; ISS:dictyBase.
DR GO; GO:0046513; P:ceramide biosynthetic process; ISS:dictyBase.
DR GO; GO:0006685; P:sphingomyelin catabolic process; ISS:dictyBase.
DR CDD; cd00842; MPP_ASMase; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR017064; ASM-like_Pdiesterase_prd.
DR InterPro; IPR045473; ASM_C.
DR InterPro; IPR041805; ASMase/PPN1_MPP.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR Pfam; PF19272; ASMase_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF036767; ASM-like_PDE; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..446
FT /note="Sphingomyelinase phosphodiesterase C"
FT /id="PRO_0000328194"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..78
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT DISULFID 429..442
FT /evidence="ECO:0000250|UniProtKB:Q92484"
SQ SEQUENCE 446 AA; 52035 MW; 456B5FE213452E31 CRC64;
MKFRNNLTLY LIFIIVFTIY ISLTISIPLK NGKFWHITDT HYDFMYIEGG DEDKQCREVT
YKSKYEKGGA SSIGNYKCDT SFELLQSSFE YMVKHEEKPD FIIWTGDDPP HLGNSQLNET
LVLQSITNMT NLIKGYFPDI PIFPSIGNHD SYPQHQIGVG PNWLFENVAQ LWSPFLSNDS
IETFKLGGYY TELVSEGFRI ISLNTVFYYN ENRQCLNLTD PAGQLLWLNE TLANASLAGE
RVWIIGHVPP GYNEKYDVFN FHKQFNDEYL FSFSQYSDII EFHIYGHEHT DTFRLFYDDP
NDHINDIEPT GIMFLSPSLT PWMNQFLPAL PNNPGLRLYE YNITSFALLD YYQFWTNLTD
NIISGNIDWQ LEYRATEFFN TFNLSPVSMY EAYLLIQSVT SQLLKFHFYN SVSYPTKGCD
EICKKIQLCS IRHPFTKGFK ECLVEI
