CYTB_OPLFA
ID CYTB_OPLFA Reviewed; 100 AA.
AC J7FQE8;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Cystatin-B {ECO:0000250|UniProtKB:P04080, ECO:0000312|EMBL:AFP50145.1};
DE AltName: Full=RbCyt-B {ECO:0000250|UniProtKB:P04080, ECO:0000303|PubMed:22626887};
DE AltName: Full=Stefin-B {ECO:0000250|UniProtKB:B2Z449, ECO:0000250|UniProtKB:P04080};
OS Oplegnathus fasciatus (Barred knifejaw) (Scaradon fasciatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Centrarchiformes; Terapontoidei; Oplegnathidae; Oplegnathus.
OX NCBI_TaxID=163134;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION,
RP AND PHYLOGENETIC ANALYSIS.
RC TISSUE=Blood {ECO:0000303|PubMed:22626887};
RX PubMed=22626887; DOI=10.1016/j.cbpb.2012.05.012;
RA Premachandra H.K., Whang I., Lee Y.D., Lee S., De Zoysa M., Oh M.J.,
RA Jung S.J., Lim B.S., Noh J.K., Park H.C., Lee J.;
RT "Cystatin B homolog from rock bream Oplegnathus fasciatus: Genomic
RT characterization, transcriptional profiling and protease-inhibitory
RT activity of recombinant protein.";
RL Comp. Biochem. Physiol. 163:138-146(2012).
CC -!- FUNCTION: Thiol protease inhibitor. Has papain inhibitory activity in
CC vitro. May be involved in immune responses against invading Gram-
CC negative bacteria. {ECO:0000269|PubMed:22626887}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04080}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in liver and to
CC a lesser extent in spleen, gill, brain, intestine, kidney, head kidney
CC and blood. Lowest level in muscle. {ECO:0000269|PubMed:22626887}.
CC -!- INDUCTION: By bacterial infection. E.tarda bacteria causes significant
CC up-regulation in head kidney between 12 hours and 24 hours post-
CC infection and in spleen between 24 hours and 48 hours post-infection.
CC {ECO:0000269|PubMed:22626887}.
CC -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
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DR EMBL; JQ287496; AFP50145.1; -; Genomic_DNA.
DR AlphaFoldDB; J7FQE8; -.
DR SMR; J7FQE8; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0071220; P:cellular response to bacterial lipoprotein; IPI:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0010951; P:negative regulation of endopeptidase 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 InterPro; IPR001713; Prot_inh_stefin.
DR PANTHER; PTHR11414; PTHR11414; 1.
DR Pfam; PF00031; Cystatin; 1.
DR PRINTS; PR00295; STEFINA.
DR SMART; SM00043; CY; 1.
DR SUPFAM; SSF54403; SSF54403; 1.
DR PROSITE; PS00287; CYSTATIN; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Immunity; Protease inhibitor; Thiol protease inhibitor.
FT CHAIN 1..100
FT /note="Cystatin-B"
FT /id="PRO_0000434648"
FT DOMAIN 6..88
FT /note="Cystatin"
FT /evidence="ECO:0000255"
FT MOTIF 48..52
FT /note="Secondary area of contact"
FT /evidence="ECO:0000250|UniProtKB:P04080"
FT SITE 6
FT /note="Reactive site"
FT /evidence="ECO:0000250|UniProtKB:P04080"
SQ SEQUENCE 100 AA; 11046 MW; 7A2CC3DC0486A87A CRC64;
MSMMCGGISA PLDADEDIQK MCDNVKPHAE EKAGKKYDVF TAKTYTTQIV SGTNYFIKIH
VGGDDHVHLR VYKKLPCHGG GLELSGMQHS KSLQDPIAYF
