CYTC_PAROL
ID CYTC_PAROL Reviewed; 126 AA.
AC B2Z450;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Cystatin-C {ECO:0000250|UniProtKB:P04080, ECO:0000312|EMBL:ACC86115.1};
DE AltName: Full=PoCystatin-C {ECO:0000250|UniProtKB:P04080, ECO:0000303|PubMed:23649306};
DE Flags: Precursor;
OS Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Paralichthyidae;
OC Paralichthys.
OX NCBI_TaxID=8255;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND PHYLOGENETIC ANALYSIS.
RC TISSUE=Muscle {ECO:0000303|PubMed:23649306};
RX PubMed=23649306; DOI=10.1007/s12010-013-0248-5;
RA Ahn S.J., Bak H.J., Park J.H., Lee J.Y., Kim N.Y., Han J.W., Jo H.I.,
RA Chung J.K., Lee H.H.;
RT "Olive flounder (Paralichthys olivaceus) cystatin C: cloning, mRNA
RT expression, and enzymatic characterization of olive flounder cystatin C.";
RL Appl. Biochem. Biotechnol. 170:1216-1228(2013).
CC -!- FUNCTION: Thiol protease inhibitor. Has high papain inhibitory activity
CC and inhibits to a lesser extent fish cathepsins L, S, K, F, X and
CC bovine cathepsin B in vitro. {ECO:0000269|PubMed:23649306}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5-6 and pH 6-8 for papain and bovine cathepsin B,
CC respectively. {ECO:0000269|PubMed:23649306};
CC Temperature dependence:
CC Stable between 20-40 degrees Celsius. {ECO:0000269|PubMed:23649306};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q98967}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in normal tissues including
CC brain, eye, gill, heart, gullet, liver, spleen, stomach, pyloric ceca,
CC intestine, kidney and muscle. Expressed, but not up-regulated, in
CC lipopolysaccharide (LPS)-stimulated tissues including kidney, spleen,
CC muscle and gill. {ECO:0000269|PubMed:23649306}.
CC -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
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DR EMBL; EU597233; ACC86115.1; -; mRNA.
DR RefSeq; XP_019948069.1; XM_020092510.1.
DR AlphaFoldDB; B2Z450; -.
DR SMR; B2Z450; -.
DR GeneID; 109632944; -.
DR KEGG; pov:109632944; -.
DR CTD; 1471; -.
DR OrthoDB; 1565344at2759; -.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR CDD; cd00042; CY; 1.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR046350; Cystatin_sf.
DR InterPro; IPR018073; Prot_inh_cystat_CS.
DR Pfam; PF00031; Cystatin; 1.
DR SMART; SM00043; CY; 1.
DR SUPFAM; SSF54403; SSF54403; 1.
DR PROSITE; PS00287; CYSTATIN; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Protease inhibitor; Secreted; Signal;
KW Thiol protease inhibitor.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..126
FT /note="Cystatin-C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434650"
FT DOMAIN 22..115
FT /note="Cystatin"
FT /evidence="ECO:0000255"
FT MOTIF 64..68
FT /note="Secondary area of contact"
FT /evidence="ECO:0000250|UniProtKB:P04080"
FT SITE 22
FT /note="Reactive site"
FT /evidence="ECO:0000250|UniProtKB:P04080"
FT DISULFID 82..92
FT /evidence="ECO:0000250|UniProtKB:Q98967"
FT DISULFID 106..126
FT /evidence="ECO:0000250|UniProtKB:Q98967"
SQ SEQUENCE 126 AA; 14027 MW; F425D7BFB3750E95 CRC64;
MKMLVFPVLA ALFAVGLGNL VGAPRDINIS EAQDALDFAV AKHNSGTNDM FLRQVAEVVR
VQRQVVSGNK YIITVKMAKT PCRKDRVVNE VCEIHKDPAL AQPYECTFSV WSRPWIPDLQ
LVGEKC
