PHL1_LEPIC
ID PHL1_LEPIC Reviewed; 596 AA.
AC Q72P44;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=LIC_12632;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS (strain Fiocruz L1-130).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=267671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fiocruz L1-130;
RX PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT insights into physiology and pathogenesis.";
RL J. Bacteriol. 186:2164-2172(2004).
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}.
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DR EMBL; AE016823; AAS71192.1; -; Genomic_DNA.
DR RefSeq; WP_000629003.1; NC_005823.1.
DR AlphaFoldDB; Q72P44; -.
DR SMR; Q72P44; -.
DR PaxDb; Q72P44; -.
DR EnsemblBacteria; AAS71192; AAS71192; LIC_12632.
DR GeneID; 61142510; -.
DR KEGG; lic:LIC_12632; -.
DR HOGENOM; CLU_489836_0_0_12; -.
DR OMA; WPIEEKV; -.
DR Proteomes; UP000007037; 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; Secreted; Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..596
FT /note="Sphingomyelinase C 1"
FT /id="PRO_0000022049"
FT REGION 63..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 68095 MW; 05A979DB24D16F6C CRC64;
MITKRNIPCK KNWKYKKKSI SLTLITICYM FLFLTSCKPG KQNSINLLLL LLNTLDNKNV
NEKIEDSTNT DPSSNVNEED ENSINANAND NAPSDSDSSN PRSPDKNPVN PTSPNSSSAD
IGIKILSHSI FMAPTNLSSW GDLGQEERAQ RIASSSYIKN QDIIVFEGLS HNNAEKILLE
KIRSEYPYQT NVVGRTKKGW NATLGAYTTS PMANGGVIIV SKWPIEEKVQ YIFNNSNCGQ
DQYYNKGFAY VKINKDGKKF HVIGTQLQAR EPDCFNSGET IRKLQLNDIK SFIDSKDIPK
DETVLITGDL NIIKGSNEYF DMISKLNVNE PRYVGVPFTL DTKTNALAAY YYEKEKPIYL
DYILVSKLHA QPPVWQNLAY DPISNTTWKR SDGYTSYEFS DRYPVYGFIY ADSSTPTKSG
HKRKYDQVSF QSTFNRKFIQ ADHNKKDGWL KADTRIKTDF TKFNLLQENV SESNPSCMNS
GSVRIESSYY LNYYWNWFIG AASGDYGYYT KFNNGSDSLG IKNLDNGCLK DGSRVAFYDW
DTIGGGYYYL TVWDKGSWKE HLFLWVQSFL SSREIFYLHL DSNPPKDWSK DLIYHH