GenomeNet

Database: UniProt
Entry: MPPE1_CHICK
LinkDB: MPPE1_CHICK
Original site: MPPE1_CHICK 
ID   MPPE1_CHICK             Reviewed;         398 AA.
AC   Q5ZK82;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 106.
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=RCJMB04_12i13;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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}.
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; AJ720202; CAG31861.1; -; mRNA.
DR   RefSeq; NP_001034372.1; NM_001039283.2.
DR   RefSeq; XP_015137964.1; XM_015282478.1.
DR   RefSeq; XP_015137965.1; XM_015282479.1.
DR   AlphaFoldDB; Q5ZK82; -.
DR   STRING; 9031.ENSGALP00000045371; -.
DR   PaxDb; 9031-ENSGALP00000022355; -.
DR   Ensembl; ENSGALT00000022395; ENSGALP00000022355; ENSGALG00000013794.
DR   GeneID; 421031; -.
DR   KEGG; gga:421031; -.
DR   CTD; 65258; -.
DR   VEuPathDB; HostDB:geneid_421031; -.
DR   eggNOG; KOG3662; Eukaryota.
DR   HOGENOM; CLU_047168_2_0_1; -.
DR   InParanoid; Q5ZK82; -.
DR   PhylomeDB; Q5ZK82; -.
DR   TreeFam; TF314437; -.
DR   PRO; PR:Q5ZK82; -.
DR   Proteomes; UP000000539; Chromosome 2.
DR   Bgee; ENSGALG00000013794; Expressed in kidney and 14 other cell types or tissues.
DR   ExpressionAtlas; Q5ZK82; baseline and differential.
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: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; METALLO PHOSPHOESTERASE RELATED; 1.
DR   PANTHER; PTHR13315:SF0; METALLOPHOSPHOESTERASE 1; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 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..398
FT                   /note="Metallophosphoesterase 1"
FT                   /id="PRO_0000315731"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        359..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         75
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         251
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="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   398 AA;  45790 MW;  B0C6794A56A1100D CRC64;
     MLSPNLTIVK NLPLKKRICF LLKLVCFVSS VLIFCEFFIY YLVIFQCRWP DVKRDAHTGN
     EETPASVLKA MFLADTHLLG EIKGHWLDKL RREWQMERSF QTALWLLQPD IVFILGDVFD
     EGKWDSPQAW ADDVRRFQKM FKYPVTTELV VIVGNHDIGF HYEMTTYKVH RFEKVFNFTS
     GKLITRKGTN FVLVNSVAME GDGCTLCRTA EAKLVALSHR LNCSLQEPNH PQKRCSDAEK
     PPASQPILLQ HYPLYRKSDA ECSGEDAAPP EEKNIPFKEK YDVLSQEASQ KLLWWFRPRL
     ILSGHTHSAC QVLHTGGIPE ISIPSFSWRN RNNPSFIMGS ITPTDFSLHK CFLPRESRVF
     AIYWAAGALL VVLVLAHFQL LTPPFYFAQR LISKHKAA
//
DBGET integrated database retrieval system