SMD_COCIM
ID SMD_COCIM Reviewed; 303 AA.
AC J3K844; A0A0E1S1R9;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Sphingomyelinase D {ECO:0000303|PubMed:24223912};
DE Short=SMase D {ECO:0000303|PubMed:24223912};
DE EC=3.1.4.41 {ECO:0000250|UniProtKB:B8NQ51};
DE Flags: Precursor;
GN ORFNames=CIMG_06182;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
RN [3]
RP IDENTIFICATION.
RX PubMed=24223912; DOI=10.1371/journal.pone.0079240;
RA Dias-Lopes C., Neshich I.A., Neshich G., Ortega J.M., Granier C.,
RA Chavez-Olortegui C., Molina F., Felicori L.;
RT "Identification of new sphingomyelinases D in pathogenic fungi and other
RT pathogenic organisms.";
RL PLoS ONE 8:E79240-E79240(2013).
CC -!- FUNCTION: Catalyzes the hydrolysis of sphingomyelin. Sphingomyelinases
CC D are produced by some spider in their venoms, but also by arthropods
CC such as ticks, or pathogenic bacteria and fungi. They might play a role
CC in pathogenicity through different mechanisms, such as membrane
CC destabilization and host cell penetration, but also pulmonary
CC inflammation and cutaneous lesions. {ECO:0000250|UniProtKB:B8NQ51}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine 1-phosphate +
CC choline + H(+); Xref=Rhea:RHEA:20984, ChEBI:CHEBI:15354,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636,
CC ChEBI:CHEBI:57674; EC=3.1.4.41;
CC Evidence={ECO:0000250|UniProtKB:B8NQ51};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8I914};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8I914};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DOMAIN: The SMD-tail motif is highly conserved and may be responsible
CC for structural stabilization. {ECO:0000303|PubMed:24223912}.
CC -!- SIMILARITY: Belongs to the sphingomyelinase D/phospholipase D family.
CC {ECO:0000305}.
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DR EMBL; GG704912; EAS30703.1; -; Genomic_DNA.
DR RefSeq; XP_001242286.1; XM_001242285.1.
DR AlphaFoldDB; J3K844; -.
DR SMR; J3K844; -.
DR EnsemblFungi; EAS30703; EAS30703; CIMG_06182.
DR GeneID; 4561714; -.
DR KEGG; cim:CIMG_06182; -.
DR VEuPathDB; FungiDB:CIMG_06182; -.
DR OrthoDB; 1048800at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050290; F:sphingomyelin phosphodiesterase D activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR SUPFAM; SSF51695; SSF51695; 1.
PE 3: Inferred from homology;
KW Hydrolase; Lipid degradation; Lipid metabolism; Magnesium; Metal-binding;
KW Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..303
FT /note="Sphingomyelinase D"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431990"
FT MOTIF 296..303
FT /note="SMD-tail"
FT /evidence="ECO:0000255"
FT ACT_SITE 50
FT /evidence="ECO:0000250|UniProtKB:Q8I914"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8I914"
FT BINDING 72
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8I914"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8I914"
SQ SEQUENCE 303 AA; 33481 MW; 235442FC2C3DA984 CRC64;
MVSLSLLLCS ALAGLLHVAS CIDVPDQAPL TVDECKCKPT SPKPVYAIAH RVLTEEGIQA
AIAHGANAIE IDMTAWKSGW WADHDGLPTS GNVTAKAMFR EVARLREDGA HLSFVWLDIK
NPDWAISGRS SVAYLRKLAR EYLEPAGVRV LYGFSNPRNS WGFKEIRNFL NANESVSVWM
DSGDAKKIYA GVGRSIPVAQ RVVDNGLFSL FWKPYIFDDL RRSSEARDCC TVGKAFGWTI
LAGQDRYVDK LLGYSGVDGL IYGTMASAYE DSEDTRAAAA LISNWIKNHP DTHRVPTQDD
KPW
