MPPE1_CRIGR
ID MPPE1_CRIGR Reviewed; 391 AA.
AC C7G3A0;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 51.
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 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH GPI-ANCHOR PROTEINS AND TMED10.
RX PubMed=19837036; DOI=10.1016/j.cell.2009.08.040;
RA Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T.;
RT "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored
RT proteins from the ER to the Golgi.";
RL Cell 139:352-365(2009).
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:0000269|PubMed:19837036}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:19837036};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000305|PubMed:19837036};
CC -!- SUBUNIT: Interacts with GPI-anchor proteins. Interacts with TMED10.
CC {ECO:0000269|PubMed:19837036}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000269|PubMed:19837036}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:19837036}. Golgi apparatus, cis-Golgi
CC network membrane {ECO:0000269|PubMed:19837036}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:19837036}. Note=Also localizes to
CC endoplasmic reticulum exit site.
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; AB490159; BAI23309.1; -; mRNA.
DR RefSeq; NP_001233645.1; NM_001246716.1.
DR RefSeq; XP_007643621.1; XM_007645431.1.
DR AlphaFoldDB; C7G3A0; -.
DR STRING; 10029.NP_001233645.1; -.
DR PRIDE; C7G3A0; -.
DR Ensembl; ENSCGRT00001029832; ENSCGRP00001025586; ENSCGRG00001023143.
DR GeneID; 100689457; -.
DR KEGG; cge:100689457; -.
DR CTD; 65258; -.
DR eggNOG; KOG3662; Eukaryota.
DR GeneTree; ENSGT00390000013236; -.
DR OMA; SRTLHCM; -.
DR OrthoDB; 1094620at2759; -.
DR GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA: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:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0034235; F:GPI anchor binding; IDA:UniProtKB.
DR GO; GO:0062050; F:GPI-mannose ethanolamine phosphate phosphodiesterase activity; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP: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 1: Evidence at protein level;
KW ER-Golgi transport; Golgi apparatus; GPI-anchor biosynthesis; Hydrolase;
KW Manganese; Membrane; Metal-binding; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..391
FT /note="Metallophosphoesterase 1"
FT /id="PRO_0000395804"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 72
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 391 AA; 45368 MW; 15A06F22B4DC59C7 CRC64;
MALVRWRLRR GNFHLLSRVL LLKLTVVIIS VLLFCEYFIY HLVIFQCHWP EVKTLAHGDR
QKPVLKAMFL ADTHLLGEIR GHWLDKLRRE WQMERAFQTA LWWLQPEVIF ILGDIFDEGK
WSTTEAWADD VQRFRKIFRH GSHVQLKVVI GNHDIGFHYQ MSKYRIKRFE KVFSSERLFS
WKGVNFVMVN SVAMEGDGCS ICSEAEAELR EISRKLNCSR EVQGSSQCEG EQRLPFSAPV
LLQHYPLYRA SDANCSGEDA APPEERNVPF EEKYDVLSRE ASQKLLWWLQ PRLVLSGHTH
SACEVLHPGG VPEVSVPSFS WRNRNNPSFI MGSLTSKDYA LSKCYLPFED RVLATYGAAA
VFLVVLILAH LERLPSSFLF GWKLRKMHMR G
