ID A0A1S3FI70_DIPOR Unreviewed; 460 AA.
AC A0A1S3FI70;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Cathepsin F {ECO:0000313|RefSeq:XP_012876293.1};
GN Name=Ctsf {ECO:0000313|RefSeq:XP_012876293.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012876293.1};
RN [1] {ECO:0000313|RefSeq:XP_012876293.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012876293.1};
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 RefSeq; XP_012876293.1; XM_013020839.1.
DR AlphaFoldDB; A0A1S3FI70; -.
DR STRING; 10020.ENSDORP00000008613; -.
DR GeneID; 105989033; -.
DR KEGG; dord:105989033; -.
DR CTD; 8722; -.
DR InParanoid; A0A1S3FI70; -.
DR OrthoDB; 1085298at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
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; 1.10.287.2250; -; 1.
DR Gene3D; 3.10.450.10; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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:SF444; CATHEPSIN F; 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; 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 Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..460
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018569177"
FT DOMAIN 163..220
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 247..458
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 460 AA; 50924 MW; 1C738B4AFB167833 CRC64;
MAPWMRLLWL LALLPGAAPR PAGPAVAGAQ AWGPPAPELL EPARFALEMY NRGRTPETRA
VLGAVRGRVR RAGDGSLYSL EATLEEAPCN NPTVCQLPET KSTLLCSFEV LKEEGKQMLL
SRECSPVDTK VTDNRNGTLG TFLSMMKAAH PSQALSSKIS TLFRDFVVTY NKTYETRQEL
ELRMSIFSQN MIQAQKIQAL DRGTAEYGIT KFSDLTEEEF HTIYLNPLLH EMSGKKMNPA
KPVDEAAPPE FDWRSKGAVT EVKNQGMCGS CWAFSVTGNV EGQWFLKQDT LLSLSEQELV
DCDKMDKACL GGLPSNAYTA IKDLGGLETE DDYKYQGHRQ VCNFTAQKAK VYINDSVELS
QDEQKLAAWL AKKGPISVAI NAFGMQFYRH GIAHPLRPLC SPWFIDHAVL IVGYGNRSEI
PFWAIKNSWG ADWGEKGYYY LHRGSGACGV NTMASSAVVI
//
