MPPE1_XENLA
ID MPPE1_XENLA Reviewed; 405 AA.
AC Q0IHA5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, 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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) 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; BC123239; AAI23240.1; -; mRNA.
DR RefSeq; NP_001090362.1; NM_001096893.1.
DR AlphaFoldDB; Q0IHA5; -.
DR DNASU; 779273; -.
DR GeneID; 779273; -.
DR KEGG; xla:779273; -.
DR CTD; 779273; -.
DR Xenbase; XB-GENE-987931; mppe1.L.
DR OMA; SRTLHCM; -.
DR OrthoDB; 1094620at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 779273; Expressed in muscle tissue and 18 other tissues.
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..405
FT /note="Metallophosphoesterase 1"
FT /id="PRO_0000315733"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 78
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 405 AA; 46756 MW; A611D1FEF26CD5E6 CRC64;
MMFKHLVPLR NGFNKERTSR LKARLFFLST IFGSILLVFF FCEFLVYYLV IVKCSWPEVK
GAHKEDSTPV LKVMFLADTH LLGEIRGHWL DKLRREWQME RSYQSALWLL QPDIVFILGD
VFDEGKWSIP QAWSSDVARF QKMFRHPPHT QLIVLVGNHD IGFHYDMTVY KLSRFEKTFN
FTSGKLVSPK GINHILSSSF VLLNSMALEG DDCHICRAAE DQLRRISIKL NCSRMREHPD
FQKKCKNVEK TPVSAPILLQ HYPLYRISDS ECTGEDSASP EEKKVLFKEK YDVLSQDASE
KLLQLLQPRL ILSGHTHSAC EVLHQGKIPE ISVPSFSWRN RNNPSFIMGS ITATKYSLAK
CFLPTENTII YIYCTASVLL TGYVLACLWL CICQRIHSGR KQKPI
