ID F1STN0_PIG Unreviewed; 395 AA.
AC F1STN0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 3.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Sphingomyelin phosphodiesterase acid like 3B {ECO:0000313|Ensembl:ENSSSCP00000003886.3};
GN Name=SMPDL3B {ECO:0000313|Ensembl:ENSSSCP00000003886.3,
GN ECO:0000313|VGNC:VGNC:93266};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000003886.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000003886.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000003886.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000003886.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the acid sphingomyelinase family.
CC {ECO:0000256|ARBA:ARBA00008234}.
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DR AlphaFoldDB; F1STN0; -.
DR PaxDb; 9823-ENSSSCP00000003886; -.
DR PeptideAtlas; F1STN0; -.
DR Ensembl; ENSSSCT00000003977.5; ENSSSCP00000003886.3; ENSSSCG00000003582.5.
DR VGNC; VGNC:93266; SMPDL3B.
DR eggNOG; KOG3770; Eukaryota.
DR GeneTree; ENSGT00950000183182; -.
DR HOGENOM; CLU_014743_0_2_1; -.
DR OMA; DSPWHLI; -.
DR TreeFam; TF313674; -.
DR Proteomes; UP000008227; Chromosome 6.
DR Bgee; ENSSSCG00000003582; Expressed in right lobe of liver and 30 other cell types or tissues.
DR ExpressionAtlas; F1STN0; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 PANTHER; PTHR10340:SF25; ACID SPHINGOMYELINASE-LIKE PHOSPHODIESTERASE 3B; 1.
DR PANTHER; PTHR10340; SPHINGOMYELIN PHOSPHODIESTERASE; 1.
DR Pfam; PF19272; ASMase_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 1: Evidence at protein level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1STN0};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..395
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014571382"
FT DOMAIN 38..293
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 307..382
FT /note="Sphingomyelin phosphodiesterase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19272"
SQ SEQUENCE 395 AA; 44724 MW; B9B542E48C19ABD7 CRC64;
MTAPGGPHVS VRQAPRMRLP VLLIFLAHWG VTRAGQGKFW HISDLHLDPD YKVSQDPLQV
CPSAGSRPVL NAGPWGDYLC DSPWILINSS IYAMKEIEPK PDFILWTGDD TPHVPDEKLG
EAAVLQIMER LSKLIREVFP DTQVYAALGN HDFHPKHQLP AGSNNIYNQV AELWRPWLNN
ESIALFKEGA FYSEKLPSGA GRIVVLNTNL YYSKNEQTAN MADPSQQFQW LDDVLSNASR
AGEMVYIIGH VPPGFFEKTR NKAWFREDFN KEYLKLIHKH HRVIAGQFFG HQHLDSFRMF
YDDAGAPISV MFLTPGVTPW KTTLAGVVNG ANNPGIRMFE YDQSTLSLKD MVTYFLNLSQ
ANEQGTPRWE PEYRLTEAYG VPTQGPVPCT RRWAA
//
