MPPE1_MACFA
ID MPPE1_MACFA Reviewed; 396 AA.
AC Q9GMS6; Q4R6J3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=QccE-17977, QtsA-17896;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex, and Testis;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (JUN-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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB047842; BAB12268.1; -; mRNA.
DR EMBL; AB169190; BAE01282.1; -; mRNA.
DR RefSeq; NP_001270651.1; NM_001283722.1.
DR AlphaFoldDB; Q9GMS6; -.
DR STRING; 9541.XP_005587257.1; -.
DR GeneID; 102138710; -.
DR CTD; 65258; -.
DR eggNOG; KOG3662; Eukaryota.
DR OrthoDB; 1094620at2759; -.
DR Proteomes; UP000233100; 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..396
FT /note="Metallophosphoesterase 1"
FT /id="PRO_0000315728"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
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 249
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 26
FT /note="L -> F (in Ref. 1; BAE01282)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="L -> F (in Ref. 1; BAE01282)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="D -> N (in Ref. 1; BAE01282)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="T -> M (in Ref. 1; BAE01282)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 45254 MW; 387FA46A133113FF CRC64;
MAMIEVGFER QNFYPLKRKS ALLLKLIAVV FAVLLFCEFL IYYLAIFQCN WPEVKTTAYD
GEQASHEPVL KAMFLADTHL LGEFLGHWLD KLRREWQMER ALQTALWLLQ PEVVFILGDV
FDEGKWSTPE AWADDVERFQ KMFRHPSHVQ LKVVAGNHDI GFHYEMNTYK VERFEKVFSS
ERLFSWKGIN FVMVNSVAMN GDGCGICSEA EAELIEVSHR LNCSREARGS RRCGPGPLLP
VSAPVLLQHY PLYRRSDANC SGDDAAPPEE RDIPFKENYD VLSREASQKL LWWLQPRLVL
SGHTHSACEV HHGGRVPEFS VPSFSWRNRN NPSFIMGSIT PTDYALSKCY LPREDVVLVI
YCGAVGFLVV LTLSHLGLLA SPFLSGLNLL RKRKTR
