ID A0A1L7XGG6_9HELO Unreviewed; 648 AA.
AC A0A1L7XGG6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Sphingomyelin phosphodiesterase {ECO:0000256|PIRNR:PIRNR000948};
GN ORFNames=PAC_14032 {ECO:0000313|EMBL:CZR64135.1};
OS Phialocephala subalpina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Mollisiaceae; Phialocephala;
OC Phialocephala fortinii species complex.
OX NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR64135.1, ECO:0000313|Proteomes:UP000184330};
RN [1] {ECO:0000313|EMBL:CZR64135.1, ECO:0000313|Proteomes:UP000184330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR64135.1,
RC ECO:0000313|Proteomes:UP000184330};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts sphingomyelin to ceramide.
CC {ECO:0000256|PIRNR:PIRNR000948}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR000948-1};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR000948-
CC 1};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the acid sphingomyelinase family.
CC {ECO:0000256|ARBA:ARBA00008234, ECO:0000256|PIRNR:PIRNR000948}.
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DR EMBL; FJOG01000025; CZR64135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L7XGG6; -.
DR STRING; 576137.A0A1L7XGG6; -.
DR OrthoDB; 205363at2759; -.
DR Proteomes; UP000184330; Unassembled WGS sequence.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0006685; P:sphingomyelin catabolic process; IEA:UniProtKB-UniRule.
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; IPR011160; Sphingomy_PDE.
DR PANTHER; PTHR10340; SPHINGOMYELIN PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR10340:SF34; SPHINGOMYELIN PHOSPHODIESTERASE; 1.
DR Pfam; PF19272; ASMase_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF000948; Sphingomy_PDE; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000948-2};
KW Glycosidase {ECO:0000256|PIRNR:PIRNR000948};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000948};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000948-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184330};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000948-1}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..648
FT /note="Sphingomyelin phosphodiesterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012656872"
FT DOMAIN 159..423
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 441..566
FT /note="Sphingomyelin phosphodiesterase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19272"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-1"
FT DISULFID 53..129
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 82..93
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 180..185
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 186..210
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
FT DISULFID 553..557
FT /evidence="ECO:0000256|PIRSR:PIRSR000948-2"
SQ SEQUENCE 648 AA; 70289 MW; 24CF7BC2D0F1DE9C CRC64;
MKLSSLFAPV LLVVPAFVSG LAISETTNEA LSAFGKRSTI SDILTDIEDA ASCTACEALL
VVLKVLAHTG NDNFVDVITE ICILAGVDDS DVCTGAIALE GPILAHDLRV MTIGTRTSEL
FCLTVFGLCQ WPDIEAYTVS VTDKPDTTRP APSGQSPIQV VHISDIHVDL SYETGASYNC
TKNICCRPYT ADDEPGVTDF PAGEYGNVAC DSPVTLEESM YAAIESLAPD KSFTIFTGDV
VEGAVWLVTD TEVTNDLNDA YTRMQSIGQT YAVVGNHDTS PVNSFPPAAV DTTISSQWAY
DAMTSDWSTW IGATVSAEAD ANYGSYSTLT SEGLRIISVN TNFWYKQNFW LYEATMERDP
SGQLAWLVTE LEAAETAGER VWLMGHMPLG STDAFHDQSQ YFDQIIQRFD ATISAVFYGH
THKDEFEIAY STPDAPTAAT ANMVSYIAPA LTPTSGNPTF RVYSVDPVTF AILDYTVYYT
NISSPTYQSG PVWEKLYSVK EAYGSLLTPP VTDTAVELTP EFWHNLTVLF EDDDSVYQEW
YARRTRDYSS ATCTGDCKTT SICELRASQS QYNCGTVSAG INFKRDAAAT AQSHSECEGS
AIIPIMTSFT GTGIAAFQSA LVQTMGESFL NTAIPSNYTV AGWNSTTS
//
