ID A0A3P9BCU0_9CICH Unreviewed; 475 AA.
AC A0A3P9BCU0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Cathepsin L {ECO:0000313|Ensembl:ENSMZEP00005007730.1};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005007730.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005007730.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005007730.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR RefSeq; XP_004563245.1; XM_004563188.1.
DR AlphaFoldDB; A0A3P9BCU0; -.
DR STRING; 106582.ENSMZEP00005007730; -.
DR Ensembl; ENSMZET00005008048.1; ENSMZEP00005007730.1; ENSMZEG00005005887.1.
DR GeneID; 101469506; -.
DR KEGG; mze:101469506; -.
DR CTD; 8722; -.
DR GeneTree; ENSGT00940000164681; -.
DR OrthoDB; 1085298at2759; -.
DR Proteomes; UP000265160; LG2.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00042; CY; 1.
DR CDD; cd02248; Peptidase_C1A; 1.
DR Gene3D; 1.10.287.2250; -; 1.
DR Gene3D; 3.10.450.10; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR046350; Cystatin_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
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:SF959; CATHEPSIN F; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR Pfam; PF00031; Cystatin; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00043; CY; 1.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54403; Cystatin/monellin; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 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:UP000265160};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..475
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018545710"
FT DOMAIN 36..145
FT /note="Cystatin"
FT /evidence="ECO:0000259|SMART:SM00043"
FT DOMAIN 177..234
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 262..473
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 475 AA; 53344 MW; 83E2A0A5B735D22C CRC64;
MVVILRCCPL IQWLSLAVLL GSVVGLGEDL DRPLLGPPGS SIRVHESDPG LKKALAFAEE
RYNRVSNAMH LRRVSRVISA NKQLVKGIRY TLTVELSNTQ CKKSTMLRTC DFYPELNQLK
TEVCVFEVWD IPWQGASTLL KQKCQPKVEF EVEESNKVED PSTSQPLEES VELLGRFKEF
MTKYNKVYSS QEEVDRRLRI FHENLKTAEK LQALDQGSAE YGVTKFSDLT EEEFRSTYLN
PLLSQWTLHQ PMKPATPAKG PSPDSWDWRD HGAVSPVKNQ GMCGSCWAFS VIGNIEGQWF
LKNGTLLSLS EQELVDCDGL DQACRGGLPS NAYEAIEKLG GLETESDYSY TGHKQRCDFT
TGKVAAYINS SVELPKEEKE IAAWLAENGP VSVALNAFAM QFYRKGISHP LKIFCNPWMI
DHAVLLVGYG ERKGIPFWAI KNSWGEDYGE QGYYNLYRGS NACGINKMCS SAVVN
//
