MPPE1_DANRE
ID MPPE1_DANRE Reviewed; 381 AA.
AC Q566Y9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Metallophosphoesterase 1;
DE EC=3.1.-.-;
DE AltName: Full=Post-GPI attachment to proteins factor 5;
GN Name=mppe1; Synonyms=pgap5; ORFNames=zgc:112219;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Larva;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic
CC reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Note=Also localizes to endoplasmic
CC reticulum exit site. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. MPPE1
CC family. {ECO:0000305}.
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DR EMBL; BC093272; AAH93272.1; -; mRNA.
DR RefSeq; NP_001017701.1; NM_001017701.1.
DR AlphaFoldDB; Q566Y9; -.
DR STRING; 7955.ENSDARP00000066782; -.
DR PaxDb; Q566Y9; -.
DR GeneID; 550396; -.
DR KEGG; dre:550396; -.
DR CTD; 65258; -.
DR ZFIN; ZDB-GENE-050417-195; mppe1.
DR eggNOG; KOG3662; Eukaryota.
DR InParanoid; Q566Y9; -.
DR OrthoDB; 1094620at2759; -.
DR PhylomeDB; Q566Y9; -.
DR PRO; PR:Q566Y9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034235; F:GPI anchor binding; ISS:UniProtKB.
DR GO; GO:0062050; F:GPI-mannose ethanolamine phosphate phosphodiesterase activity; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISS:UniProtKB.
DR CDD; cd08165; MPP_MPPE1; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR039541; MPP_MPPE1.
DR InterPro; IPR033308; PGAP5/Cdc1/Ted1.
DR PANTHER; PTHR13315; PTHR13315; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 2: Evidence at transcript level;
KW ER-Golgi transport; Golgi apparatus; GPI-anchor biosynthesis; Hydrolase;
KW Manganese; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..381
FT /note="Metallophosphoesterase 1"
FT /id="PRO_0000315732"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 59
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 381 AA; 44068 MW; A8B1958CA009A025 CRC64;
MTLVFGSSCR LAVTLIFAFV SVFVFCEYVI YYLVILRCSW PLLEIEDSHS PLRALFLSDT
HLLGAIRGHW LDKLRREWQM ERAFQTSMWL LNPEVVFILG DVFDEGKWST SQDWEDDVRR
FKRIFRHPVD TKLVVLVGNH DIGFHHEMTK QKLERFEQVF NVTSARILTI KGVNFLLVNS
VALHGDHCPI CQHVEEELQK LSHALNCSIQ GAQHNGQCKN AARFAPAAPV LLQHYPLYRV
SDAMCTGVDT APLDEQYLLF QERYDVISKN ASKKLLWWFK PRLILSGHTH NGCEVLHEKL
YPEISVPSFS WRNRNNPSFV LGTFSQSEFQ LSKCFLPEER TVLVVYCSSC LIIALITLIH
LKMFRNSLQF TNNLIGKHKT L
