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MPPE1_MOUSE
ID   MPPE1_MOUSE             Reviewed;         396 AA.
AC   Q80XL7; Q3T9I6; Q3TYP9; Q3U4F5; Q8BLU5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 122.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-237 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Aorta, Inner ear, Spleen, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor, and Olfactory epithelium;
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80XL7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80XL7-2; Sequence=VSP_030686;
CC       Name=3;
CC         IsoId=Q80XL7-3; Sequence=VSP_030684, VSP_030685;
CC   -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. MPPE1
CC       family. {ECO:0000305}.
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DR   EMBL; AK041262; BAC30883.1; -; mRNA.
DR   EMBL; AK154265; BAE32476.1; -; mRNA.
DR   EMBL; AK158446; BAE34513.1; -; mRNA.
DR   EMBL; AK172496; BAE43034.1; -; mRNA.
DR   EMBL; BC045146; AAH45146.1; -; mRNA.
DR   EMBL; BC086456; AAH86456.1; -; mRNA.
DR   CCDS; CCDS29319.1; -. [Q80XL7-2]
DR   RefSeq; NP_766218.1; NM_172630.2. [Q80XL7-2]
DR   RefSeq; XP_006525953.1; XM_006525890.2.
DR   AlphaFoldDB; Q80XL7; -.
DR   BioGRID; 230417; 2.
DR   STRING; 10090.ENSMUSP00000072808; -.
DR   iPTMnet; Q80XL7; -.
DR   PhosphoSitePlus; Q80XL7; -.
DR   EPD; Q80XL7; -.
DR   MaxQB; Q80XL7; -.
DR   PaxDb; Q80XL7; -.
DR   PRIDE; Q80XL7; -.
DR   ProteomicsDB; 295588; -. [Q80XL7-1]
DR   ProteomicsDB; 295589; -. [Q80XL7-2]
DR   ProteomicsDB; 295590; -. [Q80XL7-3]
DR   Antibodypedia; 1617; 135 antibodies from 22 providers.
DR   Ensembl; ENSMUST00000073054; ENSMUSP00000072808; ENSMUSG00000062526. [Q80XL7-2]
DR   GeneID; 225651; -.
DR   KEGG; mmu:225651; -.
DR   UCSC; uc008flv.1; mouse. [Q80XL7-2]
DR   UCSC; uc008flw.1; mouse. [Q80XL7-1]
DR   UCSC; uc008flx.1; mouse. [Q80XL7-3]
DR   CTD; 65258; -.
DR   MGI; MGI:2661311; Mppe1.
DR   VEuPathDB; HostDB:ENSMUSG00000062526; -.
DR   eggNOG; KOG3662; Eukaryota.
DR   GeneTree; ENSGT00390000013236; -.
DR   HOGENOM; CLU_047168_2_0_1; -.
DR   InParanoid; Q80XL7; -.
DR   OMA; SRTLHCM; -.
DR   OrthoDB; 1094620at2759; -.
DR   PhylomeDB; Q80XL7; -.
DR   TreeFam; TF314437; -.
DR   BioGRID-ORCS; 225651; 2 hits in 70 CRISPR screens.
DR   ChiTaRS; Mppe1; mouse.
DR   PRO; PR:Q80XL7; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q80XL7; protein.
DR   Bgee; ENSMUSG00000062526; Expressed in granulocyte and 215 other tissues.
DR   ExpressionAtlas; Q80XL7; 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:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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   Alternative splicing; ER-Golgi transport; Golgi apparatus;
KW   GPI-anchor biosynthesis; Hydrolase; Manganese; Membrane; Metal-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..396
FT                   /note="Metallophosphoesterase 1"
FT                   /id="PRO_0000315729"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..376
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         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   VAR_SEQ         188
FT                   /note="N -> K (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030684"
FT   VAR_SEQ         189..396
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030685"
FT   VAR_SEQ         224
FT                   /note="E -> EQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030686"
FT   CONFLICT        384
FT                   /note="L -> P (in Ref. 1; BAE32476)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   396 AA;  46012 MW;  8C246D289E05350B CRC64;
     MALVRWGLKR QNFHPLRRRR RALLLKLTVV IISVLLFCEY FIYYLVLFRC HWPEVKTLAH
     GGRQEPVLKA MFLADTHLLG EIRGHWLDKL RREWQMERAF QTALWLLQPE VVFILGDIFD
     EGKWSSDQAW ADDVQRFQRM FRHDSHVQLK VVIGNHDVGF HYQMSKYRIK RFEKVFGSER
     LLSLKGVNFV MVNSVAMEGD GCIICSEEEA ELREISRKLN CSQEVPGSSQ CDREPEPRLP
     LSAPVLLQHY PLYRASDANC SGEDAAPPEE RNVPFEEKYD VLSREASQKL LWWLRPRLVL
     SGHTHSACEV LHPGGAPEVS VPSFSWRNRN NPSFIMGSLT SRDYALSKCY LPFEDTVLTM
     YGAAAGFLMI LILVHFEHLP SPFLCGWKLC RLHMRR
 
 
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