CYT_CHICK
ID CYT_CHICK Reviewed; 139 AA.
AC P01038;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Cystatin;
DE AltName: Full=Egg-white cystatin;
DE AltName: Full=Ovocystatin;
DE Flags: Precursor;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2793849; DOI=10.1016/s0021-9258(18)71473-7;
RA Colella R., Sakaguchi Y., Nagase H., Bird J.W.C.;
RT "Chicken egg white cystatin. Molecular cloning, nucleotide sequence, and
RT tissue distribution.";
RL J. Biol. Chem. 264:17164-17169(1989).
RN [2]
RP PROTEIN SEQUENCE OF 24-139.
RX PubMed=6712597; DOI=10.1042/bj2170813;
RA Schwabe C., Anastasi A., Crow H., McDonald J.K., Barrett A.J.;
RT "Cystatin. Amino acid sequence and possible secondary structure.";
RL Biochem. J. 217:813-817(1984).
RN [3]
RP PROTEIN SEQUENCE OF 24-139.
RX PubMed=6662498; DOI=10.1515/bchm2.1983.364.2.1487;
RA Turk V., Brzin J., Longer M., Ritonja A., Eropkin M., Borchart U.,
RA Machleidt W.;
RT "Protein inhibitors of cysteine proteinases. III. Amino-acid sequence of
RT cystatin from chicken egg white.";
RL Hoppe-Seyler's Z. Physiol. Chem. 364:1487-1496(1983).
RN [4]
RP CHARACTERIZATION OF PROTEIN.
RX PubMed=6409085; DOI=10.1042/bj2110129;
RA Anastasi A., Brown M.A., Kembhavi A.A., Nicklin M.J.H., Sayers C.A.,
RA Sunter D.C., Barrett A.J.;
RT "Cystatin, a protein inhibitor of cysteine proteinases. Improved
RT purification from egg white, characterization, and detection in chicken
RT serum.";
RL Biochem. J. 211:129-138(1983).
RN [5]
RP DISULFIDE BONDS.
RA Grubb A., Loefberg H., Barrett A.J.;
RT "The disulphide bridges of human cystatin C (gamma-trace) and chicken
RT cystatin.";
RL FEBS Lett. 170:370-374(1984).
RN [6]
RP PHOSPHORYLATION AT SER-103.
RX PubMed=2721673; DOI=10.1016/0014-5793(89)80453-3;
RA Laber B., Krieglstein K., Henschen A., Kos J., Turk V., Huber R., Bode W.;
RT "The cysteine proteinase inhibitor chicken cystatin is a phosphoprotein.";
RL FEBS Lett. 248:162-168(1989).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=3191914; DOI=10.1002/j.1460-2075.1988.tb03109.x;
RA Bode W., Engh R., Musil D., Thiele U., Huber R., Karshikov A., Brzin J.,
RA Kos J., Turk V.;
RT "The 2.0 A X-ray crystal structure of chicken egg white cystatin and its
RT possible mode of interaction with cysteine proteinases.";
RL EMBO J. 7:2593-2599(1988).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=8263912; DOI=10.1006/jmbi.1993.1658;
RA Dieckmann T., Mitschang L., Hofmann M., Kos J., Turk V., Auerswald E.A.,
RA Jeanicke R., Oschkinat H.;
RT "The structures of native phosphorylated chicken cystatin and of a
RT recombinant unphosphorylated variant in solution.";
RL J. Mol. Biol. 234:1048-1059(1993).
CC -!- FUNCTION: This protein binds tightly to and inhibits a variety of thiol
CC proteases including ficin, papain, and cathepsins B, C, H, and L.
CC Although isolated from egg white, it is also present in serum.
CC -!- INTERACTION:
CC P01038; Q9N6S8; Xeno; NbExp=2; IntAct=EBI-15593412, EBI-15593394;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J05077; AAA48744.1; -; mRNA.
DR PIR; A34456; UDCH.
DR RefSeq; NP_990831.2; NM_205500.2.
DR PDB; 1A67; NMR; -; A=32-139.
DR PDB; 1A90; NMR; -; A=32-139.
DR PDB; 1CEW; X-ray; 2.00 A; I=32-139.
DR PDB; 1YVB; X-ray; 2.70 A; I=29-139.
DR PDBsum; 1A67; -.
DR PDBsum; 1A90; -.
DR PDBsum; 1CEW; -.
DR PDBsum; 1YVB; -.
DR AlphaFoldDB; P01038; -.
DR SMR; P01038; -.
DR DIP; DIP-61237N; -.
DR IntAct; P01038; 1.
DR STRING; 9031.ENSGALP00000043172; -.
DR MEROPS; I25.011; -.
DR iPTMnet; P01038; -.
DR PaxDb; P01038; -.
DR ABCD; P01038; 1 sequenced antibody.
DR GeneID; 396497; -.
DR KEGG; gga:396497; -.
DR CTD; 1471; -.
DR VEuPathDB; HostDB:geneid_396497; -.
DR eggNOG; ENOG502SC50; Eukaryota.
DR HOGENOM; CLU_118168_0_1_1; -.
DR InParanoid; P01038; -.
DR OrthoDB; 1565344at2759; -.
DR PhylomeDB; P01038; -.
DR EvolutionaryTrace; P01038; -.
DR PRO; PR:P01038; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IBA:GO_Central.
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 3D-structure; Direct protein sequencing; Disulfide bond; Phosphoprotein;
KW Protease inhibitor; Reference proteome; Secreted; Signal;
KW Thiol protease inhibitor.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:6662498,
FT ECO:0000269|PubMed:6712597"
FT CHAIN 24..139
FT /note="Cystatin"
FT /id="PRO_0000006663"
FT MOTIF 76..80
FT /note="Secondary area of contact"
FT SITE 32
FT /note="Reactive site"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2721673"
FT DISULFID 94..104
FT /evidence="ECO:0000269|Ref.5"
FT DISULFID 118..138
FT /evidence="ECO:0000269|Ref.5"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:1CEW"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:1CEW"
FT STRAND 62..95
FT /evidence="ECO:0007829|PDB:1CEW"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:1YVB"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:1CEW"
FT STRAND 115..125
FT /evidence="ECO:0007829|PDB:1CEW"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:1CEW"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:1CEW"
SQ SEQUENCE 139 AA; 15287 MW; D92D1131C4D37891 CRC64;
MAGARGCVVL LAAALMLVGA VLGSEDRSRL LGAPVPVDEN DEGLQRALQF AMAEYNRASN
DKYSSRVVRV ISAKRQLVSG IKYILQVEIG RTTCPKSSGD LQSCEFHDEP EMAKYTTCTF
VVYSIPWLNQ IKLLESKCQ
