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Cathepsin L (EC 3.4.22.15) (Cysteine proteinase 1) [Cleaved into: Cathepsin L heavy chain; Cathepsin L light chain]

 CATL_DROME              Reviewed;         371 AA.
Q95029; O97431; Q5U121;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
28-NOV-2006, sequence version 2.
12-SEP-2018, entry version 156.
RecName: Full=Cathepsin L;
EC=3.4.22.15;
AltName: Full=Cysteine proteinase 1;
Contains:
RecName: Full=Cathepsin L heavy chain;
Contains:
RecName: Full=Cathepsin L light chain;
Flags: Precursor;
Name=Cp1; Synonyms=fs(2)50Ca; ORFNames=CG6692;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND SUBCELLULAR
LOCATION.
TISSUE=Hemocyte;
PubMed=9099581; DOI=10.1111/j.1365-2583.1997.tb00085.x;
Tryselius Y., Hultmark D.;
"Cysteine proteinase 1 (CP1), a cathepsin L-like enzyme expressed in
the Drosophila melanogaster haemocyte cell line mbn-2.";
Insect Mol. Biol. 6:173-181(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9662479; DOI=10.1046/j.1365-2583.1998.00070.x;
Gray Y.H.M., Sved J.A., Preston C.R., Engels W.R.;
"Structure and associated mutational effects of the cysteine
proteinase (CP1) gene of Drosophila melanogaster.";
Insect Mol. Biol. 7:291-293(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley; TISSUE=Larva, and Pupae;
Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-371, FUNCTION, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=Canton-S;
PubMed=7851441; DOI=10.1111/j.1432-1033.1995.tb20428.x;
Matsumoto I., Watanabe H., Abe K., Arai S., Emori Y.;
"A putative digestive cysteine proteinase from Drosophila melanogaster
is predominantly expressed in the embryonic and larval midgut.";
Eur. J. Biochem. 227:582-587(1995).
-!- FUNCTION: Important for the overall degradation of proteins in
lysosomes. Essential for adult male and female fertility. May play
a role in digestion. {ECO:0000269|PubMed:7851441,
ECO:0000269|PubMed:9099581, ECO:0000269|PubMed:9662479}.
-!- CATALYTIC ACTIVITY: Specificity close to that of papain. As
compared to cathepsin B, cathepsin L exhibits higher activity
toward protein substrates, but has little activity on Z-Arg-Arg-
NHMec, and no peptidyl-dipeptidase activity.
-!- SUBUNIT: Dimer of a heavy and a light chain linked by disulfide
bonds.
-!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:9099581}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=C;
IsoId=Q95029-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=A; Synonyms=B;
IsoId=Q95029-2; Sequence=VSP_021771;
-!- TISSUE SPECIFICITY: In the embryo, predominantly expressed in the
midgut. Also expressed in larval alimentary organs such as
salivary gland and midgut including gastric caeca.
{ECO:0000269|PubMed:7851441}.
-!- DEVELOPMENTAL STAGE: Expressed in embryo, larva, pupa and adult.
{ECO:0000269|PubMed:7851441}.
-!- DISRUPTION PHENOTYPE: Flies exhibit wing and pigmentation defects.
Females are sterile, males are partially sterile.
{ECO:0000269|PubMed:9662479}.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
-!- SEQUENCE CAUTION:
Sequence=BAA06738.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U75652; AAB18345.1; -; mRNA.
EMBL; AF012089; AAB65749.1; -; Genomic_DNA.
EMBL; AE013599; AAF58311.1; -; Genomic_DNA.
EMBL; AE013599; AAM68565.1; -; Genomic_DNA.
EMBL; BT016071; AAV36956.1; -; mRNA.
EMBL; D31970; BAA06738.1; ALT_SEQ; Genomic_DNA.
RefSeq; NP_523735.2; NM_079011.3. [Q95029-1]
RefSeq; NP_725347.1; NM_166026.3. [Q95029-2]
UniGene; Dm.7400; -.
ProteinModelPortal; Q95029; -.
SMR; Q95029; -.
BioGrid; 62300; 41.
IntAct; Q95029; 2.
STRING; 7227.FBpp0086719; -.
MEROPS; C01.092; -.
PaxDb; Q95029; -.
PRIDE; Q95029; -.
EnsemblMetazoa; FBtr0087592; FBpp0086718; FBgn0013770. [Q95029-2]
EnsemblMetazoa; FBtr0087593; FBpp0086719; FBgn0013770. [Q95029-1]
GeneID; 36546; -.
KEGG; dme:Dmel_CG6692; -.
CTD; 36546; -.
FlyBase; FBgn0013770; Cp1.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
GeneTree; ENSGT00900000140823; -.
InParanoid; Q95029; -.
KO; K01365; -.
OrthoDB; EOG091G0AKT; -.
PhylomeDB; Q95029; -.
Reactome; R-DME-1442490; Collagen degradation.
Reactome; R-DME-1474228; Degradation of the extracellular matrix.
Reactome; R-DME-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-DME-1679131; Trafficking and processing of endosomal TLR.
Reactome; R-DME-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-DME-2132295; MHC class II antigen presentation.
Reactome; R-DME-6798695; Neutrophil degranulation.
GenomeRNAi; 36546; -.
PRO; PR:Q95029; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0013770; Expressed in 40 organ(s), highest expression level in prepupa.
ExpressionAtlas; Q95029; baseline and differential.
Genevisible; Q95029; DM.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0045169; C:fusome; IDA:FlyBase.
GO; GO:0005764; C:lysosome; IDA:FlyBase.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:FlyBase.
GO; GO:0008233; F:peptidase activity; IDA:FlyBase.
GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0006508; P:proteolysis; IDA:FlyBase.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central.
CDD; cd02248; Peptidase_C1A; 1.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR025661; Pept_asp_AS.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR025660; Pept_his_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
InterPro; IPR039417; Peptidase_C1A_papain-like.
InterPro; IPR013201; Prot_inhib_I29.
PANTHER; PTHR12411; PTHR12411; 1.
Pfam; PF08246; Inhibitor_I29; 1.
Pfam; PF00112; Peptidase_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00848; Inhibitor_I29; 1.
SMART; SM00645; Pept_C1; 1.
SUPFAM; SSF54001; SSF54001; 1.
PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Developmental protein;
Digestion; Disulfide bond; Glycoprotein; Hydrolase; Lysosome;
Protease; Reference proteome; Signal; Thiol protease; Zymogen.
SIGNAL 1 48 {ECO:0000255}.
PROPEP 49 153 Activation peptide.
/FTId=PRO_0000026265.
CHAIN 154 326 Cathepsin L heavy chain.
/FTId=PRO_0000026266.
PROPEP 327 329
/FTId=PRO_0000026267.
CHAIN 330 371 Cathepsin L light chain.
/FTId=PRO_0000026268.
ACT_SITE 178 178 {ECO:0000250}.
ACT_SITE 317 317 {ECO:0000250}.
ACT_SITE 338 338 {ECO:0000250}.
CARBOHYD 127 127 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 175 218 {ECO:0000250}.
DISULFID 209 251 {ECO:0000250}.
DISULFID 310 360 Interchain (between heavy and light
chains). {ECO:0000250}.
VAR_SEQ 2 31 Missing (in isoform A).
{ECO:0000303|PubMed:9099581,
ECO:0000303|Ref.5}.
/FTId=VSP_021771.
CONFLICT 228 228 R -> P (in Ref. 6; BAA06738).
{ECO:0000305}.
CONFLICT 255 257 KGT -> RAQ (in Ref. 6; BAA06738).
{ECO:0000305}.
CONFLICT 277 281 AEAVA -> PEPVP (in Ref. 6; BAA06738).
{ECO:0000305}.
CONFLICT 365 365 A -> P (in Ref. 6; BAA06738).
{ECO:0000305}.
SEQUENCE 371 AA; 41601 MW; 01955EB4735316D7 CRC64;
MNHLGVFETR FRPRTRHKSQ RAQLIPEQIT MRTAVLLPLL ALLAVAQAVS FADVVMEEWH
TFKLEHRKNY QDETEERFRL KIFNENKHKI AKHNQRFAEG KVSFKLAVNK YADLLHHEFR
QLMNGFNYTL HKQLRAADES FKGVTFISPA HVTLPKSVDW RTKGAVTAVK DQGHCGSCWA
FSSTGALEGQ HFRKSGVLVS LSEQNLVDCS TKYGNNGCNG GLMDNAFRYI KDNGGIDTEK
SYPYEAIDDS CHFNKGTVGA TDRGFTDIPQ GDEKKMAEAV ATVGPVSVAI DASHESFQFY
SEGVYNEPQC DAQNLDHGVL VVGFGTDESG EDYWLVKNSW GTTWGDKGFI KMLRNKENQC
GIASASSYPL V


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