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GPI8_DROME
ID   GPI8_DROME              Reviewed;         355 AA.
AC   Q8T4E1; O46047; Q9W538;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Putative GPI-anchor transamidase;
DE            Short=GPI transamidase;
DE            EC=3.-.-.-;
DE   AltName: Full=Phosphatidylinositol glycan anchor biosynthesis protein class K {ECO:0000312|FlyBase:FBgn0023545};
DE   Flags: Precursor;
GN   Name=PIG-K {ECO:0000312|FlyBase:FBgn0023545};
GN   ORFNames=CG4406 {ECO:0000312|FlyBase:FBgn0023545};
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] {ECO:0000312|EMBL:AAF45703.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305, ECO:0000312|EMBL:AAF45703.2}
RP   GENOME REANNOTATION.
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] {ECO:0000305, ECO:0000312|EMBL:CAA15687.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oregon-R {ECO:0000269|PubMed:10731137};
RX   PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA   Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA   Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA   Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA   Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA   Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA   Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA   McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA   Glover D.M.;
RT   "From sequence to chromosome: the tip of the X chromosome of D.
RT   melanogaster.";
RL   Science 287:2220-2222(2000).
RN   [4] {ECO:0000305, ECO:0000312|EMBL:AAL89972.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC   TISSUE=Testis {ECO:0000269|PubMed:12537569};
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: Mediates GPI anchoring in the endoplasmic reticulum, by
CC       replacing a protein's C-terminal GPI attachment signal peptide with a
CC       pre-assembled GPI. During this transamidation reaction, the GPI
CC       transamidase forms a carbonyl intermediate with the substrate protein
CC       (By similarity). {ECO:0000250|UniProtKB:Q92643}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA15687.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AE014298; AAF45703.2; -; Genomic_DNA.
DR   EMBL; AL009192; CAA15687.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY089234; AAL89972.1; -; mRNA.
DR   PIR; T13411; T13411.
DR   RefSeq; NP_569968.2; NM_130612.4.
DR   AlphaFoldDB; Q8T4E1; -.
DR   SMR; Q8T4E1; -.
DR   BioGRID; 57708; 1.
DR   STRING; 7227.FBpp0070333; -.
DR   MEROPS; C13.005; -.
DR   PaxDb; Q8T4E1; -.
DR   PRIDE; Q8T4E1; -.
DR   DNASU; 31163; -.
DR   EnsemblMetazoa; FBtr0070347; FBpp0070333; FBgn0023545.
DR   GeneID; 31163; -.
DR   KEGG; dme:Dmel_CG4406; -.
DR   UCSC; CG4406-RA; d. melanogaster.
DR   CTD; 31163; -.
DR   FlyBase; FBgn0023545; PIG-K.
DR   VEuPathDB; VectorBase:FBgn0023545; -.
DR   eggNOG; KOG1349; Eukaryota.
DR   GeneTree; ENSGT00940000156273; -.
DR   HOGENOM; CLU_044656_1_0_1; -.
DR   InParanoid; Q8T4E1; -.
DR   OMA; PGHTNNW; -.
DR   OrthoDB; 1259741at2759; -.
DR   PhylomeDB; Q8T4E1; -.
DR   UniPathway; UPA00196; -.
DR   BioGRID-ORCS; 31163; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 31163; -.
DR   PRO; PR:Q8T4E1; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0023545; Expressed in secondary oocyte and 21 other tissues.
DR   Genevisible; Q8T4E1; DM.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR   GO; GO:0042765; C:GPI-anchor transamidase complex; IDA:FlyBase.
DR   GO; GO:0003923; F:GPI-anchor transamidase activity; ISS:UniProtKB.
DR   GO; GO:0016255; P:attachment of GPI anchor to protein; IBA:GO_Central.
DR   GO; GO:0034394; P:protein localization to cell surface; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR028361; GPI_transamidase.
DR   InterPro; IPR001096; Peptidase_C13.
DR   PANTHER; PTHR48067; PTHR48067; 1.
DR   Pfam; PF01650; Peptidase_C13; 1.
DR   PIRSF; PIRSF500138; GPI8; 1.
DR   PIRSF; PIRSF019663; Legumain; 1.
DR   PRINTS; PR00776; HEMOGLOBNASE.
PE   2: Evidence at transcript level;
KW   GPI-anchor biosynthesis; Hydrolase; Protease; Reference proteome; Signal;
KW   Thiol protease.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..355
FT                   /note="Putative GPI-anchor transamidase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000043371"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000250|UniProtKB:Q92643"
FT   ACT_SITE        207
FT                   /evidence="ECO:0000250|UniProtKB:Q92643"
SQ   SEQUENCE   355 AA;  40368 MW;  0F0EAE94F5E840A9 CRC64;
     MFNIMLVKFV VIFALILASC RVEADNTSVL PEGFVDAAQR STHTNNWAVL VDASRFWFNY
     RHVANVLSIY RSVKRLGIPD SQIILMIADD MACNARNPRP GQVYNNANQH INVYGDDVEV
     DYRGYEVTVE NFVRLLTGRT QNGTARSKKL LSDAGSNVLI YLTGHGGDGF LKFQDSEEIT
     SQELADGIQQ MWEKKRYNEL FFMVDTCQAA SLYEKFTSPN VLAVASSLVG EDSLSHHVDP
     SIGVYMIDRY TYYALEFLEK VQPFSKRTIG EFLQVCPKRV CISTVGVRKD LYPRDPHKVP
     ITDFFGAIRP TRVSTDRINV TLANEDDFIF DKDKMVTKKP FKIVMESQFP SELFK
 
 
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