PHL1_LEPIN
ID PHL1_LEPIN Reviewed; 597 AA.
AC P59115;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Sphingomyelinase C 1;
DE EC=3.1.4.12;
DE AltName: Full=Sphingomyelin phosphodiesterase 1;
DE Short=SMase 1;
DE Flags: Precursor;
GN Name=sph1; OrderedLocusNames=LA_1027;
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=AAN48226.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE010300; AAN48226.2; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_711208.2; NC_004342.2.
DR RefSeq; WP_000629004.1; NC_004342.2.
DR AlphaFoldDB; P59115; -.
DR SMR; P59115; -.
DR EnsemblBacteria; AAN48226; AAN48226; LA_1027.
DR KEGG; lil:LA_1027; -.
DR PATRIC; fig|189518.3.peg.1024; -.
DR HOGENOM; CLU_489836_0_0_12; -.
DR InParanoid; P59115; -.
DR OMA; WPIEEKV; -.
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..37
FT /evidence="ECO:0000255"
FT CHAIN 38..597
FT /note="Sphingomyelinase C 1"
FT /id="PRO_0000022050"
FT REGION 64..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 68192 MW; 2601745BC37DCEE9 CRC64;
MITKRNIPPC KKNWKYKKKS ISLTLITICY MFLFLTSCKP GKKNSINLLL LLLNTLDNKN
VNEKIEDSTN TDPSSNVNEE DENSINANAN DNAPSDSDSS NPRSPDKNPV NPTSPNSSSA
DIGIKILSHS IFMAPTNLSS WGDLGQEERA QRIASSSYIK NQDIIVFEGL SHNNAEKILL
EKIRSEYPYQ TNVVGRTKKG WNATLGAYTT SPMANGGVII VSKWPIEEKV QYIFNNSNCG
QDQYYNKGFA YVKINKDGKK FHVIGTQLQA REPDCFNSGE TIRKLQLNDI KSFIDSKDIP
KDETVLITGD LNIIKGSNEY FDMISKLNVN EPRYVGVPFT LDTKTNALAA YYYEKEKPIY
LDYILVSKLH AQPPVWQNLA YDPISNTTWK RSDGYTSYEF SDRYPVYGFI YADSSTPTKS
GHKRKYDQVS FQSTFNRKFI QADHNKKDGW LKADTRIKTD FTKFNLLQEN VSESNPSCMN
SGSVRIESSY YLNYYWNWFI GAASGDYGYY TKFNNGSDSL GIKNLDNGCL KDGSRVAFYD
WDTIGGGYYY LTVWDKGSWK EHLFLWVQSF LSSREIFYLH LDSNPPKDWS KDLIYHH