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Database: UniProt
Entry: A0A3B1IVB6_ASTMX
LinkDB: A0A3B1IVB6_ASTMX
Original site: A0A3B1IVB6_ASTMX 
ID   A0A3B1IVB6_ASTMX        Unreviewed;       333 AA.
AC   A0A3B1IVB6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Pro-cathepsin H {ECO:0000256|ARBA:ARBA00039372};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000034017.1, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000034017.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; A0A3B1IVB6; -.
DR   STRING; 7994.ENSAMXP00000034017; -.
DR   Ensembl; ENSAMXT00000036963.1; ENSAMXP00000034017.1; ENSAMXG00000039984.1.
DR   GeneTree; ENSGT00940000160227; -.
DR   InParanoid; A0A3B1IVB6; -.
DR   OrthoDB; 5472948at2759; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000039984; Expressed in intestine and 14 other cell types or tissues.
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:UP000018467};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..333
FT                   /note="Pro-cathepsin H"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018657378"
FT   DOMAIN          33..88
FT                   /note="Cathepsin propeptide inhibitor"
FT                   /evidence="ECO:0000259|SMART:SM00848"
FT   DOMAIN          114..330
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00645"
SQ   SEQUENCE   333 AA;  37138 MW;  2A75026821D41A2E CRC64;
     MNTAALLTAT ACLAVLHCVC ASPLYTEEDE FVFKTWMSEH NRKYSLDEYY QRLQIFTENK
     RRIDHHNAGN HKFRMGLNQF SDMTFTEFKK QYLLTEPQNC SATKGSHVSS NGPYPDSIDW
     RKKGNFVTAV KNQGSCGSCW TFSTTGCLES VTAIASGKLP LLSEQQLVDC AGDFNNHGCN
     GGLPSQAFEY IKYNKGIMTE DDYPYTARDG PCKYNPKQAA AFVKDVVNIT IYDEMGMVDA
     VARLNPVSFA YQVTSDFMSY TSGVYTSTEC HNTTDTVNHA VLAVGYGEQN GTPYWIVKNS
     WGSSWGMDGY FFIERGKNMC GLAACSSYPL PLV
//
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