SGMB_DICDI
ID SGMB_DICDI Reviewed; 637 AA.
AC Q54C16;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Sphingomyelin phosphodiesterase B;
DE EC=3.1.4.-;
DE AltName: Full=Acid sphingomyelinase B;
DE Short=aSMase B;
DE Flags: Precursor;
GN Name=sgmB; ORFNames=DDB_G0293210;
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; AAFI02000200; EAL60804.1; -; Genomic_DNA.
DR RefSeq; XP_629250.1; XM_629248.1.
DR AlphaFoldDB; Q54C16; -.
DR SMR; Q54C16; -.
DR STRING; 44689.DDB0232049; -.
DR PaxDb; Q54C16; -.
DR EnsemblProtists; EAL60804; EAL60804; DDB_G0293210.
DR GeneID; 8629132; -.
DR KEGG; ddi:DDB_G0293210; -.
DR dictyBase; DDB_G0293210; sgmB.
DR eggNOG; KOG3770; Eukaryota.
DR HOGENOM; CLU_014743_3_0_1; -.
DR InParanoid; Q54C16; -.
DR OMA; YSIEEHL; -.
DR PhylomeDB; Q54C16; -.
DR Reactome; R-DDI-1660662; Glycosphingolipid metabolism.
DR PRO; PR:Q54C16; -.
DR Proteomes; UP000002195; Chromosome 6.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..637
FT /note="Sphingomyelin phosphodiesterase B"
FT /id="PRO_0000328188"
FT DOMAIN 73..155
FT /note="Saposin B-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
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 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 279
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 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 77..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 80..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 108..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 212..233
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT DISULFID 582..595
FT /evidence="ECO:0000250|UniProtKB:Q92484"
SQ SEQUENCE 637 AA; 72204 MW; BFA4F7BDC836F575 CRC64;
MKVKAPILLL FVFLINFCFS IKQTQQQNFD ITIDNNNYNN NNNNNKNEII NNNNKNNNNL
NDEYFEKLGY DTNGTKCDIC KFGINQVQKM IASKQGIEDI SKYAIDLCTY LHIEKAEVCN
GLIPLFANMT YNVLSYPTVT GEYVCGFVGF CPYVPRNSSN IINFPKPKPP HVPPVAPSPN
SPTMKILHIS DIHVDPVYES GMNADCGEPL CCRAPNGPGV GEKAAGEWGH YLCDINMKMV
ESMFEFIDQE FGEDIDIVFW TGDNPPHDIW EQTYDSQINA SQLVTNLVKK YFGSTAKVFP
AIGNHESLPV NSFPLPPGSS WIFNALSYDW SDWVNVDEQV ANLQYGGYYT LPVQSGLRVI
SLNMNWCNNG NLYLAENSTD PANMLQWIVD TLQASEDIGE KVYLVGHIPP GIPDCIDSWS
EQLLQIVNRY EDTILASFYG HTHRDEFSVY YTQSDENDPS SPMRASNVIY TTPSVTTYQH
QNPSFRIFTV DSNTGYLMES STYHTDLSQA NLNGKPTWLL EYNTTNTYNI PNLTPISMDL
AIQNINSSNS MLEDYHVHYY SASPYPESKP CTSISCKLDY ICKMKSAAYL KYYECIHHEV
NNYLLNESDD DSIKSHKKLN ILLDLNNYLN NEVLKSC
