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Database: UniProt
Entry: Q812A7_MESAU
LinkDB: Q812A7_MESAU
Original site: Q812A7_MESAU 
ID   Q812A7_MESAU            Unreviewed;       333 AA.
AC   Q812A7;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=Cathepsin L {ECO:0000313|EMBL:AAO33585.1, ECO:0000313|RefSeq:NP_001268616.1};
GN   Name=Ctsv {ECO:0000313|RefSeq:NP_001268616.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|EMBL:AAO33585.1};
RN   [1] {ECO:0000313|EMBL:AAO33585.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Placenta {ECO:0000313|EMBL:AAO33585.1};
RA   Frenck J., Sol-Church K.;
RT   "Gerbil and Hamster Homologs of Mouse Cathepsin P.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|RefSeq:NP_001268616.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18463158; DOI=10.1093/molehr/gan026;
RA   Sireesha G.V., Mason R.W., Hassanein M., Tonack S., Navarrete Santos A.,
RA   Fischer B., Seshagiri P.B.;
RT   "Role of cathepsins in blastocyst hatching in the golden hamster.";
RL   Mol. Hum. Reprod. 14:337-346(2008).
RN   [3] {ECO:0000313|RefSeq:NP_001268616.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28071753;
RA   McCann K.E., Sinkiewicz D.M., Norvelle A., Huhman K.L.;
RT   "De novo assembly, annotation, and characterization of the whole brain
RT   transcriptome of male and female Syrian hamsters.";
RL   Sci. Rep. 7:40472-40472(2017).
RN   [4] {ECO:0000313|RefSeq:NP_001268616.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
CC       {ECO:0000256|ARBA:ARBA00008455}.
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DR   EMBL; AF479267; AAO33585.1; -; mRNA.
DR   RefSeq; NP_001268616.1; NM_001281687.1.
DR   STRING; 10036.ENSMAUP00000000845; -.
DR   MEROPS; C01.032; -.
DR   GeneID; 101825242; -.
DR   KEGG; maua:101825242; -.
DR   CTD; 1515; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   OrthoDB; 5472948at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0042583; C:chromaffin granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:SF57; CATHEPSIN L2; 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   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW   Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001268616.1};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..333
FT                   /evidence="ECO:0000256|SAM:SignalP,
FT                   ECO:0000313|RefSeq:NP_001268616.1"
FT                   /id="PRO_5009993619"
FT   DOMAIN          29..88
FT                   /note="Cathepsin propeptide inhibitor"
FT                   /evidence="ECO:0000259|SMART:SM00848"
FT   DOMAIN          114..332
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00645"
SQ   SEQUENCE   333 AA;  37234 MW;  14ABC90DA01A9A5F CRC64;
     MNLLLLLATL CLGTASATPK FNQTFNAQWH KWKSTHRRLY DTNEEEWRRA VWEKNMKMIE
     LHNGEYSEGK HGFTMEMNAF GDMTNEEFRQ LVNGYKHQKH RKGKLFQEPL MLQLPKSVDW
     REKGCVTPVK NQGQCGSCWA FSACGALEGQ MCLKTGVLVS LSEQNLVDCS RGEGNQGCNG
     GLMDFAFQYV LNNKGLDSEE SYPYEAKDGT CKYKPEFAAA NDTGYVDIPQ LEKALMKAVA
     TVGPIAVAID ASHPSFQFYS SGIYFEPNCS SKDLDHGVLV IGYGFEGTDS NKKKYWIVKN
     SWGTGWGMGG FFHIAKDKNN HCGIATAASY PTV
//
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