EQSTC_ACTEQ
ID EQSTC_ACTEQ Reviewed; 231 AA.
AC P81439; Q9U4R8; Q9U6K8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Equistatin {ECO:0000303|PubMed:10720485, ECO:0000303|PubMed:9153250};
DE Short=EI {ECO:0000303|PubMed:10720485};
DE AltName: Full=Cysteine proteinase inhibitor {ECO:0000303|PubMed:10720485, ECO:0000303|PubMed:9153250};
DE Flags: Precursor;
OS Actinia equina (Beadlet anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Actinia.
OX NCBI_TaxID=6106;
RN [1] {ECO:0000312|EMBL:AAF24173.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND RECOMBINANT EXPRESSION.
RX PubMed=10720485; DOI=10.1006/bbrc.2000.2356;
RA Strukelj B., Lenarcic B., Gruden K., Pungercar J., Rogelj B., Turk V.,
RA Bosch D., Jongsma M.A.;
RT "Equistatin, a protease inhibitor from the sea anemone actinia equina, is
RT composed of three structural and functional domains.";
RL Biochem. Biophys. Res. Commun. 269:732-736(2000).
RN [2] {ECO:0000312|EMBL:AAF02722.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND RECOMBINANT EXPRESSION.
RX PubMed=10722055; DOI=10.1515/bc.2000.012;
RA Galesa K., Strukelj B., Bavec S., Turk V., Lenarcic B.;
RT "Cloning and expression of functional equistatin.";
RL Biol. Chem. 381:85-88(2000).
RN [3]
RP PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9153250; DOI=10.1074/jbc.272.21.13899;
RA Lenarcic B., Ritonja A., Strukelj B., Turk B., Turk V.;
RT "Equistatin, a new inhibitor of cysteine proteinases from Actinia equina,
RT is structurally related to thyroglobulin type-1 domain.";
RL J. Biol. Chem. 272:13899-13903(1997).
RN [4]
RP SEQUENCE REVISION.
RA Lenarcic B., Ritonja A., Strukelj B., Turk B., Turk V.;
RL J. Biol. Chem. 273:12682-12682(1998).
CC -!- FUNCTION: Potent inhibitor of papain-like cysteine proteinases
CC (Ki=0.18-0.57 nM on papain), as well as of the aspartic proteinase
CC cathepsin D (Ki=0.3-05 nM). {ECO:0000269|PubMed:10720485,
CC ECO:0000269|PubMed:9153250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9153250}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I31 family.
CC {ECO:0000305}.
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DR EMBL; AF156179; AAF24173.1; -; mRNA.
DR EMBL; AF184891; AAF02722.1; -; mRNA.
DR AlphaFoldDB; P81439; -.
DR MEROPS; I31.003; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00191; TY; 3.
DR Gene3D; 4.10.800.10; -; 3.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR Pfam; PF00086; Thyroglobulin_1; 3.
DR SMART; SM00211; TY; 3.
DR SUPFAM; SSF57610; SSF57610; 3.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 2.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 3.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor; Repeat;
KW Secreted; Signal; Thiol protease inhibitor.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..231
FT /note="Equistatin"
FT /evidence="ECO:0000269|Ref.4"
FT /id="PRO_0000195900"
FT DOMAIN 34..95
FT /note="Thyroglobulin type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 102..163
FT /note="Thyroglobulin type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 167..231
FT /note="Thyroglobulin type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 37..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 67..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 76..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 105..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 135..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 144..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 170..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 202..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 211..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT VARIANT 35
FT /note="T -> S"
FT VARIANT 74
FT /note="C -> V"
FT VARIANT 162
FT /note="T -> S"
FT VARIANT 169
FT /note="E -> P"
FT VARIANT 175..176
FT /note="IK -> LQ"
FT VARIANT 188
FT /note="V -> L"
FT VARIANT 216
FT /note="G -> D"
FT CONFLICT 51
FT /note="A -> T (in Ref. 2; AAF02722)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="Q -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="E -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="F -> L (in Ref. 2; AAF02722 and 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 231 AA; 25410 MW; 07E256877D3356E9 CRC64;
MALSQNQAKF SKGFVVMIWV LFIACAITST EASLTKCQQL QASANSGLIG AYVPQCKETG
EFEEKQCWGS TGYCWCVDED GKEILGTKIR GSPDCSRRKA ALTLCQMMQA IIVNVPGWCG
PPSCKADGSF DEVQCCASNG ECYCVDKKGK ELEGTRQQGR PTCERHLSEC EEARIKAHSN
SLRVEMFVPE CFEDGSYNPV QCWPSTGYCW CVDEGGVKVP GSDVRFKRPT C
