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   27-MAR-2024, entry version 174.
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}, Larva
RC   {ECO:0000269|PubMed:12537569}, and Pupae
RC   {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; 7227-FBpp0078465; -.
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   AGR; FB:FBgn0260462; -.
DR   CTD; 8722; -.
DR   FlyBase; FBgn0260462; CG12163.
DR   VEuPathDB; VectorBase:FBgn0260462; -.
DR   eggNOG; KOG1542; Eukaryota.
DR   GeneTree; ENSGT00940000164681; -.
DR   InParanoid; Q9VN93; -.
DR   OMA; GEHKPYD; -.
DR   OrthoDB; 1085298at2759; -.
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 cell types or tissues.
DR   ExpressionAtlas; Q9VN93; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0045169; C:fusome; IDA:FlyBase.
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   Gene3D; 3.10.450.10; -; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 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; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411:SF959; CATHEPSIN F; 1.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
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; SSF54403; Cystatin/monellin; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
DR   Genevisible; Q9VN93; DM.
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
//