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IBB3_MACAX
ID   IBB3_MACAX              Reviewed;          76 AA.
AC   P01057;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Bowman-Birk type proteinase inhibitor DE-3;
OS   Macrotyloma axillare (Perennial horse gram) (Dolichos axillaris).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Macrotyloma.
OX   NCBI_TaxID=3876;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=477675; DOI=10.1111/j.1432-1033.1979.tb13088.x;
RA   Joubert F.J., Kruger H., Townshend G.S., Botes D.P.;
RT   "Purification, some properties and the complete primary structures of two
RT   protease inhibitors (DE-3 and DE-4) from Macrotyloma axillare seed.";
RL   Eur. J. Biochem. 97:85-91(1979).
CC   -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor
CC       family. {ECO:0000305}.
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DR   PIR; A01296; TIAM3.
DR   AlphaFoldDB; P01057; -.
DR   SMR; P01057; -.
DR   MEROPS; I12.001; -.
DR   TCDB; 8.A.77.3.1; the sheddase (sheddase) family.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd00023; BBI; 1.
DR   Gene3D; 2.10.69.10; -; 1.
DR   InterPro; IPR035995; Bowman-Birk_prot_inh.
DR   InterPro; IPR000877; Prot_inh_BBI.
DR   Pfam; PF00228; Bowman-Birk_leg; 1.
DR   SMART; SM00269; BowB; 1.
DR   SUPFAM; SSF57247; SSF57247; 1.
DR   PROSITE; PS00281; BOWMAN_BIRK; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Serine protease inhibitor.
FT   CHAIN           1..76
FT                   /note="Bowman-Birk type proteinase inhibitor DE-3"
FT                   /id="PRO_0000105841"
FT   SITE            24..25
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   SITE            51..52
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        16..70
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        17..32
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        20..66
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        22..30
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        40..47
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        44..59
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
FT   DISULFID        49..57
FT                   /evidence="ECO:0000250|UniProtKB:P80321"
SQ   SEQUENCE   76 AA;  8292 MW;  2B08F93647974028 CRC64;
     DHHHSTDEPS ESSKPCCDEC ACTKSIPPQC RCTDVRLNSC HSACSSCVCT FSIPAQCVCV
     DMKDFCYAPC KSSHDD
 
 
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