MPPE1_PONAB
ID MPPE1_PONAB Reviewed; 397 AA.
AC Q5RET5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Metallophosphoesterase 1;
DE EC=3.1.-.-;
DE AltName: Full=Post-GPI attachment to proteins factor 5;
GN Name=MPPE1; Synonyms=PGAP5;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 -!- SUBUNIT: Interacts with GPI-anchor proteins. Interacts with TMED10 (By
CC similarity). {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; CR857431; CAH89722.1; -; mRNA.
DR RefSeq; NP_001124783.1; NM_001131311.1.
DR AlphaFoldDB; Q5RET5; -.
DR STRING; 9601.ENSPPYP00000010093; -.
DR GeneID; 100171636; -.
DR KEGG; pon:100171636; -.
DR CTD; 65258; -.
DR eggNOG; KOG3662; Eukaryota.
DR InParanoid; Q5RET5; -.
DR OrthoDB; 1094620at2759; -.
DR Proteomes; UP000001595; 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..397
FT /note="Metallophosphoesterase 1"
FT /id="PRO_0000315730"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 77
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 397 AA; 45432 MW; BF3480AB83F0AAA7 CRC64;
MAMIELEFGR QNFHPLKKKS PLLLKLIAVV FAVLLFCEFL IYYLAIFQCN WPEVKTTASD
GEQATREPVL KAMFLADTHL LGEVLGHWPD KLRREWQMER AFQTALWLLQ PEVVFILGDI
FDEGKWSTPE AWVNDVERFQ KMFRHPSHVQ LKVVAGNHDI GFHYEMNTYK VERFEKVFSS
ERLFSWKGIN FVMVNSVALN GDGCGICSET EAELIEVSHR LNCSREQARG SSRCGPGPLL
PMSAPVLLQH YPLYRRSDAN CSGEDAAPPE ERDIPFKENY DVLSREASQK LLRWFQPRLV
LSGHTHSACE VHHGGRVPEL SVPSFSWRNR NNPSFIMGSI TPTDYTLSKC YLPREDVVLI
IYCGMVGFLV VLTLTHFGLL ASPFLAGLNL LRKRKTR
