ID A0A4W3JZ29_CALMI Unreviewed; 309 AA.
AC A0A4W3JZ29;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Pro-cathepsin H {ECO:0000256|ARBA:ARBA00039372};
GN Name=ctsh {ECO:0000313|Ensembl:ENSCMIP00000044296.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|Ensembl:ENSCMIP00000044296.1, ECO:0000313|Proteomes:UP000314986};
RN [1] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17185593; DOI=10.1126/science.1130708;
RA Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA Brenner S.;
RT "Ancient noncoding elements conserved in the human genome.";
RL Science 314:1892-1892(2006).
RN [2] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17407382;
RA Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA Brenner S.;
RT "Survey sequencing and comparative analysis of the elephant shark
RT (Callorhinchus milii) genome.";
RL PLoS Biol. 5:E101-E101(2007).
RN [3] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
RN [4] {ECO:0000313|Ensembl:ENSCMIP00000044296.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Important for the overall degradation of proteins in
CC lysosomes. {ECO:0000256|ARBA:ARBA00037522}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins, acting as an aminopeptidase (notably,
CC cleaving Arg-|-Xaa bonds) as well as an endopeptidase.; EC=3.4.22.16;
CC Evidence={ECO:0000256|ARBA:ARBA00036517};
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR AlphaFoldDB; A0A4W3JZ29; -.
DR Ensembl; ENSCMIT00000044932.1; ENSCMIP00000044296.1; ENSCMIG00000018300.1.
DR GeneTree; ENSGT00940000160227; -.
DR Proteomes; UP000314986; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
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; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR PANTHER; PTHR12411:SF642; PRO-CATHEPSIN H; 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:UP000314986};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 15..64
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 90..306
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 309 AA; 34798 MW; F5413AFB370CEC61 CRC64;
FGYSWTTEMG FRVCQHNKHY SSEEYSYRLR TFIQNKRKVE EHNSGQHSYR MGLNQFSDMT
FSEFKKLYLL REPQNCSATR GNHVLSMGPY PDFVDWRTKG NYVTPVKNQG GCGSCWTFST
TGCLESAIAI KTGKLLSLAE QQLVDCAGAY KNHGCNGGLP SQAFEYIKYN GGLEAEKDYP
YTAQDQHCQY QPNKAVAFVK EVVNITQYDE NGIVDAVARL NPVSIAFEVT DDFFQYEGGV
YSNSNCDSTP DKVNHAVLAV GYGVQNGTKY WIVKNSWGPE WGLNGYFYII RGKNMCGLAA
CPSYPIPLL
//
