ID   PHL2_LEPIN              Reviewed;         623 AA.
AC   P59116;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2002, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Sphingomyelinase C 2;
DE            EC=3.1.4.12;
DE   AltName: Full=Sphingomyelin phosphodiesterase 2;
DE            Short=SMase 2;
DE   Flags: Precursor;
GN   Name=sph2; OrderedLocusNames=LA_1029;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) +
CC         phosphocholine; Xref=Rhea:RHEA:19253, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:52639,
CC         ChEBI:CHEBI:295975; EC=3.1.4.12;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN48228.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE010300; AAN48228.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_711210.2; NC_004342.2.
DR   AlphaFoldDB; P59116; -.
DR   SMR; P59116; -.
DR   EnsemblBacteria; AAN48228; AAN48228; LA_1029.
DR   KEGG; lil:LA_1029; -.
DR   PATRIC; fig|189518.3.peg.1027; -.
DR   HOGENOM; CLU_489836_0_0_12; -.
DR   InParanoid; P59116; -.
DR   OMA; KESNEYY; -.
DR   BRENDA; 3.1.4.12; 2986.
DR   Proteomes; UP000001408; Chromosome I.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IEA:UniProtKB-EC.
DR   CDD; cd09078; nSMase; 1.
DR   Gene3D; 3.60.10.10; -; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR038772; SMPD2-like.
DR   InterPro; IPR017766; Sphingomyelinase/PLipase_C.
DR   PANTHER; PTHR12393; PTHR12393; 1.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   SUPFAM; SSF56219; SSF56219; 1.
DR   TIGRFAMs; TIGR03395; sphingomy; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..623
FT                   /note="Sphingomyelinase C 2"
FT                   /id="PRO_0000022051"
FT   REGION          51..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   623 AA;  71030 MW;  E94B065CC895767C CRC64;
     MINKITKPKL LIGYYLLLFS LIRCLPEKES SYKDLFTSLL FLPNQTNSNQ VNSVSINNDP
     ANPNPVNPAS ANNNQVNAVP ENDDPANLNP VNPASANSNQ VNAAPENGSP ADPNPANLAS
     ANNNQVNAVP ANNYFTKEDS SNNIPKKVNS KNVEIKVLSH NVFMLPTNLP RWGNLGHDER
     AKRISKSDYV KNQDVIVFEE AFDTSARKIL LDNLREEYPY QTDVVGRTKK NWDASLGNFR
     SYSLVNGGVV ILSKWPIEEK IQYIFNDSGC GADWFANKGF VYVKINKEGK KFHVIGTHAQ
     SQDQNCSNLG IPNRANQFDD IRNFIYSKNI PKDETVLIVG DLNVIKESNE YYDMISRLNV
     NEPRYVGVPF TWDAKTNEIA AYYYENEEPV YLDYIFVSKS HAQPPVWQNL AYDPVSKQTW
     TVSGYTSDEF SDHYPIYGFV YADPSTPTKS GHKKKYDQVS FQSAANGKYI QADPNRKNGW
     LKADAVIETD FTKFNLLQEG NLNPSCIKNG LVRIESSRFL NYFWNWWLGG GSGNYGYYSK
     FNDASNQLEI INLSDECLEN GSKIVFKDYD TYSRNHYYLT VWDKGNWNEH LYLWKDSISQ
     REIFYLKLNS TPVRNWSADL IYR