MPPE1_CAEEL
ID MPPE1_CAEEL Reviewed; 365 AA.
AC Q95X35; G8JXZ3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2019, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Metallophosphoesterase 1 homolog;
DE EC=3.1.-.-;
GN Name=mppe-1 {ECO:0000312|WormBase:B0511.13b};
GN ORFNames=B0511.13 {ECO:0000312|WormBase:B0511.13b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Metallophosphoesterase required for transport of GPI-anchor
CC proteins from the endoplasmic reticulum to the Golgi. Acts in lipid
CC remodeling steps of GPI-anchor maturation by mediating the removal of a
CC side-chain ethanolamine-phosphate (EtNP) from the second Man (Man2) of
CC the GPI intermediate, an essential step for efficient transport of GPI-
CC anchor proteins. {ECO:0000250|UniProtKB:Q53F39}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q53F39};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:Q53F39};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000250|UniProtKB:Q53F39}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:Q53F39}. Golgi apparatus, cis-
CC Golgi network membrane {ECO:0000250|UniProtKB:Q53F39}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:Q53F39}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:B0511.13b};
CC IsoId=Q95X35-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:B0511.13a};
CC IsoId=Q95X35-2; Sequence=VSP_060217;
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. MPPE1
CC family. {ECO:0000305}.
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DR EMBL; BX284601; CCD62113.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD62114.1; -; Genomic_DNA.
DR RefSeq; NP_001251442.2; NM_001264513.2. [Q95X35-2]
DR RefSeq; NP_001251443.1; NM_001264514.1. [Q95X35-1]
DR AlphaFoldDB; Q95X35; -.
DR SMR; Q95X35; -.
DR STRING; 6239.B0511.13a; -.
DR EPD; Q95X35; -.
DR PaxDb; Q95X35; -.
DR EnsemblMetazoa; B0511.13a.1; B0511.13a.1; WBGene00015238. [Q95X35-2]
DR EnsemblMetazoa; B0511.13b.1; B0511.13b.1; WBGene00015238. [Q95X35-1]
DR GeneID; 172956; -.
DR KEGG; cel:CELE_B0511.13; -.
DR UCSC; B0511.13; c. elegans. [Q95X35-1]
DR CTD; 172956; -.
DR WormBase; B0511.13a; CE50716; WBGene00015238; mppe-1. [Q95X35-2]
DR WormBase; B0511.13b; CE46132; WBGene00015238; mppe-1. [Q95X35-1]
DR eggNOG; KOG3662; Eukaryota.
DR GeneTree; ENSGT00390000013236; -.
DR HOGENOM; CLU_047168_2_0_1; -.
DR InParanoid; Q95X35; -.
DR OMA; SRTLHCM; -.
DR OrthoDB; 1094620at2759; -.
DR PhylomeDB; Q95X35; -.
DR PRO; PR:Q95X35; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00015238; Expressed in embryo and 3 other tissues.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR033308; PGAP5/Cdc1/Ted1.
DR PANTHER; PTHR13315; PTHR13315; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 3: Inferred from homology;
KW Alternative splicing; ER-Golgi transport; Golgi apparatus;
KW GPI-anchor biosynthesis; Hydrolase; Manganese; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..365
FT /note="Metallophosphoesterase 1 homolog"
FT /id="PRO_0000315734"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 54
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53F39"
FT BINDING 96
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53F39"
FT BINDING 96
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53F39"
FT BINDING 132
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53F39"
FT BINDING 208
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53F39"
FT BINDING 262
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53F39"
FT BINDING 264
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53F39"
FT VAR_SEQ 1..141
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_060217"
SQ SEQUENCE 365 AA; 42901 MW; 90742531BC6ADA71 CRC64;
MIWLKNLRVP ILLAIILVVY NEYFIFFIAF SSCQWPCKYG RCSESSVKAF MISDTHLLGK
INGHWLDKLK REWQMYQSFW ISTWIHSPDV TFFLGDLMDE GKWAGRPVFE AYAERFKKLF
GDNEKVITLA GNHDLGFHYA IMPETLEMFK KEFRRGLIDE MKIKKHRFVL INSMAMHGDG
CRLCHEAELI LEKIKSRNPK NRPIVLQHFP LYRKSDAECD QVDEQHEIDL KEMYREQWDT
LSKESSLQII DSLNPKAVFG GHTHKMCKKK WNKTGNSEYF YEYTVNSFSW RNGDVPAMLL
VVIDGDNVLV SSCRLPSEIL QIMVYIFGGI GIVILAFILI SRRVRIFKRR PSYSLLMYRS
QEKCD
