SGMA_DICDI
ID SGMA_DICDI Reviewed; 583 AA.
AC Q55C09;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Sphingomyelin phosphodiesterase A;
DE EC=3.1.4.-;
DE AltName: Full=Acid sphingomyelinase A;
DE Short=aSMase A;
DE Flags: Precursor;
GN Name=sgmA; ORFNames=DDB_G0270834;
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 -!- FUNCTION: Converts sphingomyelin to ceramide. {ECO:0000250}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the acid sphingomyelinase family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72767.1; -; Genomic_DNA.
DR RefSeq; XP_646672.1; XM_641580.1.
DR AlphaFoldDB; Q55C09; -.
DR SMR; Q55C09; -.
DR STRING; 44689.DDB0216178; -.
DR PaxDb; Q55C09; -.
DR EnsemblProtists; EAL72767; EAL72767; DDB_G0270834.
DR GeneID; 8617646; -.
DR KEGG; ddi:DDB_G0270834; -.
DR dictyBase; DDB_G0270834; sgmA.
DR eggNOG; KOG3770; Eukaryota.
DR HOGENOM; CLU_014743_3_0_1; -.
DR InParanoid; Q55C09; -.
DR OMA; WPTEACA; -.
DR PhylomeDB; Q55C09; -.
DR PRO; PR:Q55C09; -.
DR Proteomes; UP000002195; Chromosome 1.
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; IPR045473; ASM_C.
DR InterPro; IPR041805; ASMase/PPN1_MPP.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR007856; SapB_1.
DR InterPro; IPR011001; Saposin-like.
DR InterPro; IPR008139; SaposinB_dom.
DR InterPro; IPR011160; Sphingomy_PDE.
DR Pfam; PF19272; ASMase_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF05184; SapB_1; 1.
DR PIRSF; PIRSF000948; Sphingomy_PDE; 1.
DR SMART; SM00741; SapB; 1.
DR SUPFAM; SSF47862; SSF47862; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS50015; SAP_B; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..583
FT /note="Sphingomyelin phosphodiesterase A"
FT /id="PRO_0000327564"
FT DOMAIN 51..133
FT /note="Saposin B-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 55..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 58..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 86..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 214..229
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT DISULFID 567..580
FT /evidence="ECO:0000250|UniProtKB:Q92484"
SQ SEQUENCE 583 AA; 65327 MW; EBB513384F61EE99 CRC64;
MKSIPIILLV LIGLLLASVY SHDILITEKG QKSLDKLDKA AATTLQHGEN IQLSCDVCQI
GASLLEDFIK KNASLTEIIK GLSDLCIASK EEQPEVCTGI LNNYVPIIVD VLIQSDFTPS
QLCGYFKICS ATGSSESSSI SNSFDNEYRQ ESFNKPTMKV NKKPQYKDLS NQEPLVKKFK
GNDSIGYILQ ISDVHFDPDY KVGSNPNCGR PLCCRDGVGS AGPIGHYLCD IPFSTVELIF
QHLATLTDQL DFIVWTGDNP PHNVWEQSQA QQELATATLA QVIQKTFPNT PVLPSLGNHE
AYPADQYVLP NSQWLLDSIY TYWAPWLDAD ALELVKERGY YTSLIKPGLR VMSLNTLEND
MINFYNLLPT YLKGPNNQSD WMINTLEQAQ SNGEKVLIIG HIPCTVKSAS TDGWCAMYEQ
VVGQFSDVII GQLYGHTHYD QFSVFSDVAT HTIPTGMNYI VPSLTTYQNH EPGYRIYQFD
YSTNQIVNYY QYHANITEAN ETGALNFQLT YSAKELYNMD DLSPTSWTKV ANQMKTNSTM
FNSYFENLSS SPIKESCDQA CQTKWICQIF GITSSEFDKC YGV
