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MPPE1_RAT
ID   MPPE1_RAT               Reviewed;         394 AA.
AC   B1WC86;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 88.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; CH473971; EDM14719.1; -; Genomic_DNA.
DR   EMBL; BC162043; AAI62043.1; -; mRNA.
DR   RefSeq; NP_001101905.1; NM_001108435.2.
DR   RefSeq; XP_006254941.1; XM_006254879.3.
DR   AlphaFoldDB; B1WC86; -.
DR   STRING; 10116.ENSRNOP00000025164; -.
DR   PhosphoSitePlus; B1WC86; -.
DR   PaxDb; B1WC86; -.
DR   PeptideAtlas; B1WC86; -.
DR   Ensembl; ENSRNOT00000025164; ENSRNOP00000025164; ENSRNOG00000018648.
DR   GeneID; 361344; -.
DR   KEGG; rno:361344; -.
DR   UCSC; RGD:1309184; rat.
DR   CTD; 65258; -.
DR   RGD; 1309184; Mppe1.
DR   eggNOG; KOG3662; Eukaryota.
DR   GeneTree; ENSGT00390000013236; -.
DR   HOGENOM; CLU_047168_2_0_1; -.
DR   InParanoid; B1WC86; -.
DR   OMA; SRTLHCM; -.
DR   OrthoDB; 1094620at2759; -.
DR   PhylomeDB; B1WC86; -.
DR   TreeFam; TF314437; -.
DR   PRO; PR:B1WC86; -.
DR   Proteomes; UP000002494; Chromosome 18.
DR   Proteomes; UP000234681; Chromosome 18.
DR   Bgee; ENSRNOG00000018648; Expressed in liver and 19 other tissues.
DR   Genevisible; B1WC86; RN.
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..394
FT                   /note="Metallophosphoesterase 1"
FT                   /id="PRO_0000355204"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         74
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
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="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   394 AA;  45654 MW;  C2C8F762424CECE6 CRC64;
     MALVRWGLRR QNFHLLRRRR VLLLKLTVVV ISVLLFCEYF IYYLVLFRCH WPEVKMPARG
     GRQEPVLKAM FLADTHLLGE IRGHWLDKLR REWQMERAFQ TALWLLQPEV VFILGDVFDE
     GKWSSAQAWA DDLHRFQRMF RHGSHVQLKV VIGNHDIGFH YQMSKYRINR FEKVFGSERL
     FSLKGVNFVM VNSVAMEGDG CTICSEAEAE LREISRKLNC SQEQVQGSSQ CDHEPRLPLS
     APVLLQHYPL YRASDANCSG EDAAPPEERS VPFEEKYDVL SREASQKLLW WLRPRLILSG
     HTHSACEVLH PGGAPEVSVP SFSWRNRNNP SFIMGSLTSR DYALSKCYLP CEDTVLTTYC
     AAAAFLLVLI LAHFERLPSS FLFGWKLCRS HLRR
 
 
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