GenomeNet

Database: UniProt
Entry: M3ZL60_XIPMA
LinkDB: M3ZL60_XIPMA
Original site: M3ZL60_XIPMA 
ID   M3ZL60_XIPMA            Unreviewed;       325 AA.
AC   M3ZL60;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Pro-cathepsin H {ECO:0000256|ARBA:ARBA00039372};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000002952.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000002952.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000002952.1};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_005798276.1; XM_005798219.2.
DR   AlphaFoldDB; M3ZL60; -.
DR   STRING; 8083.ENSXMAP00000002952; -.
DR   MEROPS; I29.003; -.
DR   Ensembl; ENSXMAT00000002957.2; ENSXMAP00000002952.1; ENSXMAG00000002937.2.
DR   GeneID; 102227764; -.
DR   KEGG; xma:102227764; -.
DR   CTD; 1512; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   GeneTree; ENSGT00940000160227; -.
DR   HOGENOM; CLU_012184_1_1_1; -.
DR   InParanoid; M3ZL60; -.
DR   OMA; AYNNFGC; -.
DR   OrthoDB; 5472948at2759; -.
DR   Proteomes; UP000002852; 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:UP000002852};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..325
FT                   /note="Pro-cathepsin H"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018566924"
FT   DOMAIN          27..82
FT                   /note="Cathepsin propeptide inhibitor"
FT                   /evidence="ECO:0000259|SMART:SM00848"
FT   DOMAIN          108..324
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00645"
SQ   SEQUENCE   325 AA;  36882 MW;  867C08FD4A15F77C CRC64;
     MTSVWLLLSF VSLTSAFYLT KRDEFRFKSW MAQYNKAYDF EEYYQRLQIF TENKRRIDKH
     NEGNHSFTMG LNQFSDMTFK EFRKSFLLSE PQNCSATKGN YFSSNGPHPD SIDWRKKGDY
     ITPVKNQGPC GSCWTFSTTG CLESVTAIST GKLLPLSEQQ LVDCAQDFNN HGCKGGLPSQ
     AFEYIMYNKG LMTEKDYPYT SVEGVCYYKP SMAAAFVKEV RNITAYDEMG MVDAVGTLNP
     VSFAFEVTSD FMHYHQGVYT STTCHNTTDK VNHAVLAVGY GQENGTPYWI VKNSWGPYWG
     IDGYFLIERG KNMCGLAGCS SFPVV
//
DBGET integrated database retrieval system