CPR1_DROME
ID CPR1_DROME Reviewed; 614 AA.
AC Q9VN93; Q867H7; Q9VN92;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Putative cysteine proteinase CG12163;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN ORFNames=CG12163;
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 {ECO:0000312|EMBL:AAF52055.2};
RN [1] {ECO:0000305}
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}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537572};
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}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Head {ECO:0000269|PubMed:12537569},
RC Larva {ECO:0000269|PubMed:12537569}, and
RC Pupae {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).
RN [4] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=12593804; DOI=10.1016/s0960-9822(03)00082-4;
RA Gorski S.M., Chittaranjan S., Pleasance E.D., Freeman J.D., Anderson C.L.,
RA Varhol R.J., Coughlin S.M., Zuyderduyn S.D., Jones S.J.M., Marra M.A.;
RT "A SAGE approach to discovery of genes involved in autophagic cell death.";
RL Curr. Biol. 13:358-363(2003).
CC -!- FUNCTION: May have a role in autophagic cell death.
CC {ECO:0000303|PubMed:12593804}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000303|PubMed:10731132};
CC IsoId=Q9VN93-1; Sequence=Displayed;
CC Name=B {ECO:0000303|PubMed:10731132};
CC IsoId=Q9VN93-2; Sequence=VSP_050566;
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; AE014297; AAF52055.2; -; Genomic_DNA.
DR EMBL; AE014297; AAN13266.1; -; Genomic_DNA.
DR EMBL; AY121614; AAM51941.1; ALT_SEQ; mRNA.
DR EMBL; BT003231; AAO24986.1; -; mRNA.
DR RefSeq; NP_649521.1; NM_141264.4. [Q9VN93-2]
DR RefSeq; NP_730901.1; NM_169033.4. [Q9VN93-1]
DR RefSeq; NP_730902.2; NM_169034.4.
DR AlphaFoldDB; Q9VN93; -.
DR SMR; Q9VN93; -.
DR BioGRID; 65841; 10.
DR DIP; DIP-17491N; -.
DR IntAct; Q9VN93; 3.
DR STRING; 7227.FBpp0078465; -.
DR MEROPS; C01.A27; -.
DR GlyGen; Q9VN93; 3 sites.
DR PaxDb; Q9VN93; -.
DR DNASU; 40628; -.
DR EnsemblMetazoa; FBtr0078822; FBpp0078464; FBgn0260462. [Q9VN93-2]
DR EnsemblMetazoa; FBtr0078823; FBpp0078465; FBgn0260462. [Q9VN93-1]
DR GeneID; 40628; -.
DR KEGG; dme:Dmel_CG12163; -.
DR UCSC; CG12163-RA; d. melanogaster. [Q9VN93-1]
DR FlyBase; FBgn0260462; CG12163.
DR VEuPathDB; VectorBase:FBgn0260462; -.
DR eggNOG; KOG1542; Eukaryota.
DR GeneTree; ENSGT00940000164681; -.
DR InParanoid; Q9VN93; -.
DR OMA; RGHMQAC; -.
DR PhylomeDB; Q9VN93; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-2132295; MHC class II antigen presentation.
DR BioGRID-ORCS; 40628; 0 hits in 1 CRISPR screen.
DR ChiTaRS; CG12163; fly.
DR GenomeRNAi; 40628; -.
DR PRO; PR:Q9VN93; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0260462; Expressed in eye disc (Drosophila) and 29 other tissues.
DR ExpressionAtlas; Q9VN93; baseline and differential.
DR Genevisible; Q9VN93; DM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0045169; C:fusome; IDA:FlyBase.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0098595; C:perivitelline space; HDA:FlyBase.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:FlyBase.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR046350; Cystatin_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54403; SSF54403; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..393
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026368"
FT CHAIN 394..614
FT /note="Putative cysteine proteinase CG12163"
FT /id="PRO_0000026369"
FT REGION 25..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 418
FT /evidence="ECO:0000250"
FT ACT_SITE 555
FT /evidence="ECO:0000250"
FT ACT_SITE 581
FT /evidence="ECO:0000250"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 415..456
FT /evidence="ECO:0000250"
FT DISULFID 449..489
FT /evidence="ECO:0000250"
FT DISULFID 548..602
FT /evidence="ECO:0000250"
FT VAR_SEQ 37..175
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_050566"
SQ SEQUENCE 614 AA; 68961 MW; C44D32383375E032 CRC64;
MRLFAAATVA LVLLLGQAAG EELAEERAGQ AQGDAESTES SETTTDQAVS EPPITLVHVL
NPGEREYLSP NLIGVQNIAM TFLPLSMNFV NIIDAFREIT AGVRYEILLN ALDTKAIQPA
EADIVCRLVI LEKPWLRTQW GDKHRELVTS NCTDPAVNSV AGDPAEKARL LNEKYVHRSR
RSANDILGRH KPYDEEAAKA QLQKSLDKLT AGEGPHYKIV KVYSASRQVD SGILTRIDAD
LIDGSEEQHR CIVDIWTKVW VRKDEHEITF KCRNQPVVQA RHTRSVEWAE KKTHKKHSHR
FDKVDHLFYK FQVRFGRRYV STAERQMRLR IFRQNLKTIE ELNANEMGSA KYGITEFADM
TSSEYKERTG LWQRDEAKAT GGSAAVVPAY HGELPKEFDW RQKDAVTQVK NQGSCGSCWA
FSVTGNIEGL YAVKTGELKE FSEQELLDCD TTDSACNGGL MDNAYKAIKD IGGLEYEAEY
PYKAKKNQCH FNRTLSHVQV AGFVDLPKGN ETAMQEWLLA NGPISIGINA NAMQFYRGGV
SHPWKALCSK KNLDHGVLVV GYGVSDYPNF HKTLPYWIVK NSWGPRWGEQ GYYRVYRGDN
TCGVSEMATS AVLA
