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FACE2_DROME
ID   FACE2_DROME             Reviewed;         302 AA.
AC   Q9U1H8; Q8SZZ3; Q9VRM4;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 3.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=CAAX prenyl protease 2;
DE            EC=3.4.-.-;
DE   AltName: Full=Farnesylated proteins-converting enzyme 2;
DE            Short=FACE-2;
DE   AltName: Full=Prenyl protein-specific endoprotease 2;
DE   AltName: Full=Protein severas;
GN   Name=Sras; ORFNames=CG4852;
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 [MRNA].
RA   Weinzierl-Hinum A., Toeroek I., Kiss I., Farkas R., Mechler B.M.;
RT   "The severas gene of Drosophila encodes a CAAX-protease and acts as a
RT   tumour suppressor.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
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: Proteolytically removes the C-terminal three residues of
CC       farnesylated and geranylated proteins. {ECO:0000250|UniProtKB:Q9Y256}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9Y256}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9Y256}.
CC   -!- SIMILARITY: Belongs to the peptidase U48 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB64383.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ252068; CAB64383.1; ALT_INIT; mRNA.
DR   EMBL; AE014296; AAF50770.3; -; Genomic_DNA.
DR   EMBL; AY069692; AAL39837.1; -; mRNA.
DR   RefSeq; NP_524673.3; NM_079934.3.
DR   AlphaFoldDB; Q9U1H8; -.
DR   IntAct; Q9U1H8; 16.
DR   STRING; 7227.FBpp0076791; -.
DR   MEROPS; G05.002; -.
DR   PaxDb; Q9U1H8; -.
DR   PRIDE; Q9U1H8; -.
DR   DNASU; 44002; -.
DR   EnsemblMetazoa; FBtr0077083; FBpp0076791; FBgn0029121.
DR   GeneID; 44002; -.
DR   KEGG; dme:Dmel_CG4852; -.
DR   UCSC; CG4852-RA; d. melanogaster.
DR   CTD; 44002; -.
DR   FlyBase; FBgn0029121; Sras.
DR   VEuPathDB; VectorBase:FBgn0029121; -.
DR   eggNOG; KOG4130; Eukaryota.
DR   GeneTree; ENSGT00390000004124; -.
DR   HOGENOM; CLU_049909_3_0_1; -.
DR   InParanoid; Q9U1H8; -.
DR   OMA; HSFCNWC; -.
DR   OrthoDB; 1607650at2759; -.
DR   PhylomeDB; Q9U1H8; -.
DR   Reactome; R-DME-5689880; Ub-specific processing proteases.
DR   Reactome; R-DME-9648002; RAS processing.
DR   BioGRID-ORCS; 44002; 1 hit in 1 CRISPR screen.
DR   GenomeRNAi; 44002; -.
DR   PRO; PR:Q9U1H8; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0029121; Expressed in embryonic/larval hemocyte (Drosophila) and 27 other tissues.
DR   Genevisible; Q9U1H8; DM.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0071586; P:CAAX-box protein processing; IBA:GO_Central.
DR   InterPro; IPR039731; Rce1.
DR   InterPro; IPR003675; Rce1-like.
DR   PANTHER; PTHR13046; PTHR13046; 1.
DR   Pfam; PF02517; Rce1-like; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Hydrolase; Membrane; Protease; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..302
FT                   /note="CAAX prenyl protease 2"
FT                   /id="PRO_0000194832"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        160
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT   ACT_SITE        193
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT   SITE            245
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT   SITE            249
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT   CONFLICT        94..95
FT                   /note="KL -> NV (in Ref. 1; CAB64383)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="I -> M (in Ref. 1; CAB64383)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="D -> H (in Ref. 1; CAB64383)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   302 AA;  34415 MW;  84A9EE949F1993C3 CRC64;
     MKNLSETEAE VTMQENVVHE SLPQIPVATS VSCCFVLAVL YVGSLYIWST KHNRDHPTTV
     KRRFASVSMV MLAAPFFVYF FSSPELLSRV PFPKLLGLRL EGLWQAVVIP YSLTVLLFLG
     PIFVNMQNES VRSYFDLDYW RGSFGSIIWV RNHVIAPLSE EFVFRACMMP LILQSFSPLV
     AVFITPLFFG VAHLHHIAER LSLGVELSTA LLIGLFQFIY TTLFGFYSAF LFARTGHVMA
     PILVHAFCNH MGLPDLQDLW QQDLWRRVVA IILYLAGFVG WMFLVPLATD PSIYDNTLYW
     NA
 
 
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