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MPPE1_DROME
ID   MPPE1_DROME             Reviewed;         370 AA.
AC   Q9VLR9; M9PF55; Q8T3Q1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 4.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Metallophosphoesterase 1 homolog;
DE            EC=3.1.-.-;
DE   AltName: Full=Post-GPI attachment to proteins 5 ortholog;
GN   Name=PGAP5; ORFNames=CG8455;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Berkeley; TISSUE=Testis;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: Metallophosphoesterase. {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: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9VLR9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9VLR9-2; Sequence=VSP_030687;
CC   -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. MPPE1
CC       family. {ECO:0000305}.
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DR   EMBL; AE014134; AAF52615.3; -; Genomic_DNA.
DR   EMBL; AE014134; AAN11155.1; -; Genomic_DNA.
DR   EMBL; AE014134; AGB92767.1; -; Genomic_DNA.
DR   EMBL; AY094655; AAM11008.1; -; mRNA.
DR   RefSeq; NP_001260231.1; NM_001273302.1. [Q9VLR9-2]
DR   RefSeq; NP_609191.1; NM_135347.3. [Q9VLR9-1]
DR   RefSeq; NP_723359.1; NM_164798.3. [Q9VLR9-2]
DR   AlphaFoldDB; Q9VLR9; -.
DR   BioGRID; 60245; 29.
DR   IntAct; Q9VLR9; 28.
DR   STRING; 7227.FBpp0079209; -.
DR   PaxDb; Q9VLR9; -.
DR   PRIDE; Q9VLR9; -.
DR   DNASU; 34116; -.
DR   EnsemblMetazoa; FBtr0079587; FBpp0079208; FBgn0031997. [Q9VLR9-2]
DR   EnsemblMetazoa; FBtr0079588; FBpp0079209; FBgn0031997. [Q9VLR9-1]
DR   EnsemblMetazoa; FBtr0335190; FBpp0307180; FBgn0031997. [Q9VLR9-2]
DR   GeneID; 34116; -.
DR   KEGG; dme:Dmel_CG8455; -.
DR   UCSC; CG8455-RA; d. melanogaster. [Q9VLR9-1]
DR   CTD; 34116; -.
DR   FlyBase; FBgn0031997; PGAP5.
DR   VEuPathDB; VectorBase:FBgn0031997; -.
DR   eggNOG; KOG3662; Eukaryota.
DR   GeneTree; ENSGT00390000013236; -.
DR   InParanoid; Q9VLR9; -.
DR   OMA; SRTLHCM; -.
DR   PhylomeDB; Q9VLR9; -.
DR   SignaLink; Q9VLR9; -.
DR   BioGRID-ORCS; 34116; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 34116; -.
DR   PRO; PR:Q9VLR9; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0031997; Expressed in testis and 19 other tissues.
DR   Genevisible; Q9VLR9; DM.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:InterPro.
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; Hydrolase; Manganese; Membrane; Metal-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..370
FT                   /note="Metallophosphoesterase 1 homolog"
FT                   /id="PRO_0000315735"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        328..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         52
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         275
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         368..370
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_030687"
SQ   SEQUENCE   370 AA;  43319 MW;  0E2EEA9A77036272 CRC64;
     MRFLYACFVI VLCALIFCEY VADFVVLQKC KWPEIKRKKY VDDPLRAMIL ADPHLLGPHR
     GHWLDKLYRE WHMTRAFQAA SRLFQPDVVF VLGDLFDEGD MVSDKQFQEY VWRYLKMFHL
     PPGIPLISVA GNHDVGFHYK MHPFFMSRFE SYLNNSSVNL YTIKQIHFVV INSMAMEGDG
     CMFCTQAEDQ LKNISRTLYC MKYPLEAECA RTRRHPYSQP ILLQHFPTYR ISDTMCEEHD
     APYIEAFRER FHVLSKDATD MLGELLKPRL AFAGHSHHFC HSVNRLGIDE YTVASFSWRN
     KVNPSFMLAT ITPDDYVVSK CKMLPQQFVF NSYLSAGILC LIVIGFQLRK CIQSRRQSSA
     VDHRKVNYLD
 
 
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