SGMD_DICDI
ID SGMD_DICDI Reviewed; 438 AA.
AC Q55GC7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Sphingomyelinase phosphodiesterase D;
DE EC=3.1.4.-;
DE AltName: Full=ASM-like phosphodiesterase D;
DE Flags: Precursor;
GN Name=sgmD; ORFNames=DDB_G0268330;
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; AAFI02000003; EAL73618.1; -; Genomic_DNA.
DR RefSeq; XP_647257.1; XM_642165.1.
DR AlphaFoldDB; Q55GC7; -.
DR SMR; Q55GC7; -.
DR STRING; 44689.DDB0232051; -.
DR PaxDb; Q55GC7; -.
DR EnsemblProtists; EAL73618; EAL73618; DDB_G0268330.
DR GeneID; 8616062; -.
DR KEGG; ddi:DDB_G0268330; -.
DR dictyBase; DDB_G0268330; sgmD.
DR eggNOG; KOG3770; Eukaryota.
DR HOGENOM; CLU_014743_0_2_1; -.
DR InParanoid; Q55GC7; -.
DR OMA; WYTTSED; -.
DR PhylomeDB; Q55GC7; -.
DR PRO; PR:Q55GC7; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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: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; 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 SUPFAM; SSF56300; SSF56300; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Glycosidase; Hydrolase; Metal-binding; Reference proteome;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..438
FT /note="Sphingomyelinase phosphodiesterase D"
FT /id="PRO_0000328195"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 111
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 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 438 AA; 49248 MW; 9D8601443EA19DDF CRC64;
MKIILILVLV LVVSINALNN QFLHISDVHY SSAMNSLLYN ASVMCIGPTV TKEFDHKEHE
DLIEDTERLN LPTNGLYGRY GCDTNQLLLS EVISEMLNVN SNPDFIIYTG DGAGHGLPNG
PWSESQSTLA KSLYGAYPNT QFIPTIGNND VFPDYNSQCN DSNLQFLYET WAQWIPTNQV
SSFLYRGSFV VSPVSGLTII SLNTILYSVK NKNTFSTPQD PCGQFAWLEQ QLIAAKQAGN
SVYIIGHIFP GLDPFYLQGT WKSQYQTAFF NITSDYQTTI TAGFFGHIHR DEIRSIQFDN
PSLTNNHYFP MFIGSSITPV YFNNPTFKQF TYDSQSKNIT DITAYFSDVY ISNLKGHMNW
TEEYDFVSIY DIDNQYGIGG DQLNSLMERM VSSNSIFNNY DNFRSGSYLS DSPSMTCLIN
AATIDELNAC TYIAANVA
