ID A0A093BMS3_CHAPE Unreviewed; 323 AA.
AC A0A093BMS3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Cathepsin K {ECO:0000256|ARBA:ARBA00015572};
DE EC=3.4.22.38 {ECO:0000256|ARBA:ARBA00012474};
DE Flags: Fragment;
GN ORFNames=M959_14877 {ECO:0000313|EMBL:KFU86655.1};
OS Chaetura pelagica (Chimney swift) (Hirundo pelagica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes; Apodidae;
OC Apodinae; Chaetura.
OX NCBI_TaxID=8897 {ECO:0000313|EMBL:KFU86655.1, ECO:0000313|Proteomes:UP000031515};
RN [1] {ECO:0000313|EMBL:KFU86655.1, ECO:0000313|Proteomes:UP000031515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M959 {ECO:0000313|EMBL:KFU86655.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000031515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25504712; DOI=10.1126/science.1251385;
RG Avian Genome Consortium;
RA Zhang G., Li C., Li Q., Li B., Larkin D.M., Lee C., Storz J.F., Antunes A.,
RA Greenwold M.J., Meredith R.W., Odeen A., Cui J., Zhou Q., Xu L., Pan H.,
RA Wang Z., Jin L., Zhang P., Hu H., Yang W., Hu J., Xiao J., Yang Z., Liu Y.,
RA Xie Q., Yu H., Lian J., Wen P., Zhang F., Li H., Zeng Y., Xiong Z., Liu S.,
RA Zhou L., Huang Z., An N., Wang J., Zheng Q., Xiong Y., Wang G., Wang B.,
RA Wang J., Fan Y., da Fonseca R.R., Alfaro-Nunez A., Schubert M., Orlando L.,
RA Mourier T., Howard J.T., Ganapathy G., Pfenning A., Whitney O., Rivas M.V.,
RA Hara E., Smith J., Farre M., Narayan J., Slavov G., Romanov M.N.,
RA Borges R., Machado J.P., Khan I., Springer M.S., Gatesy J., Hoffmann F.G.,
RA Opazo J.C., Hastad O., Sawyer R.H., Kim H., Kim K.W., Kim H.J., Cho S.,
RA Li N., Huang Y., Bruford M.W., Zhan X., Dixon A., Bertelsen M.F.,
RA Derryberry E., Warren W., Wilson R.K., Li S., Ray D.A., Green R.E.,
RA O'Brien S.J., Griffin D., Johnson W.E., Haussler D., Ryder O.A.,
RA Willerslev E., Graves G.R., Alstrom P., Fjeldsa J., Mindell D.P.,
RA Edwards S.V., Braun E.L., Rahbek C., Burt D.W., Houde P., Zhang Y.,
RA Yang H., Wang J., Jarvis E.D., Gilbert M.T., Wang J.;
RT "Comparative genomics reveals insights into avian genome evolution and
RT adaptation.";
RL Science 346:1311-1320(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Broad proteolytic activity. With small-molecule substrates and
CC inhibitors, the major determinant of specificity is P2, which is
CC preferably Leu, Met > Phe, and not Arg.; EC=3.4.22.38;
CC Evidence={ECO:0000256|ARBA:ARBA00001773};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004296};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004296};
CC Extracellular side {ECO:0000256|ARBA:ARBA00004296}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; KN126093; KFU86655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093BMS3; -.
DR MEROPS; C01.036; -.
DR Proteomes; UP000031515; Unassembled WGS sequence.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02248; Peptidase_C1A; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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:SF741; CATHEPSIN K; 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; 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.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000031515};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 22..82
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 111..323
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFU86655.1"
FT NON_TER 323
FT /evidence="ECO:0000313|EMBL:KFU86655.1"
SQ SEQUENCE 323 AA; 36086 MW; BD42C00A0C4736D0 CRC64;
LALLVHRVVA QLLPQPELDA QWDLWKKTHR KQYNGEADEV ERRLIWEKNL KYINTHNLEH
SLGIHTFELA MNHLGDMTSE EVVRTMTGLK VPRGHPRHNE TLYVPNWAER APAAVDWRKK
GYVTPVKNQG QCGSCWAFSS VGALEGQLKR KTGKRLTLSP QNLVDCVANN DGCGGGYMTN
AFEYVRRNRG IDSEDSYPYI GQDESCMYSP TGKAAKCRGY REIPEGNEKA LKRAVARIGP
ISVGIDASLP SFQFYSRGVY YDESCNGANI NHAVLAVGYG AQKGTKHWII KNSWGEEWGN
KGYVLLARNA DNACGVANLA SFP
//
