ID   TURM_CURLO              Reviewed;          85 AA.
AC   P85278;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Turmerin;
DE   Flags: Fragments;
OS   Curcuma longa (Turmeric) (Curcuma domestica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Zingiberaceae;
OC   Curcuma.
OX   NCBI_TaxID=136217;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Rhizome {ECO:0000269|Ref.1};
RA   Srinivas L., Chethankumar M., Sampathkumar S.;
RT   "BGS turmerin a unique antioxidant protein from Turmeric (Curcuma longa
RT   L.).";
RL   Submitted (OCT-2007) to UniProtKB.
RN   [2] {ECO:0000305}
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND BLOCKAGE OF N-TERMINUS.
RX   PubMed=1731625; DOI=10.1016/0003-9861(92)90040-4;
RA   Srinivas L., Shalini V.K., Shylaja M.;
RT   "Turmerin: a water soluble antioxidant peptide from turmeric [Curcuma
RT   longa].";
RL   Arch. Biochem. Biophys. 292:617-623(1992).
RN   [3] {ECO:0000305}
RP   FUNCTION, AND MASS SPECTROMETRY.
RX   PubMed=18177267; DOI=10.1515/bc.2008.024;
RA   Chethankumar M., Srinivas L.;
RT   "New biological activity against phospholipase A2 by Turmerin, a protein
RT   from Curcuma longa L.";
RL   Biol. Chem. 389:299-303(2008).
CC   -!- FUNCTION: Inhibition of trypsin (By similarity). Has anticarcinogenic
CC       activity, prevents transformation of DMBA-treated JB6 cells. Has
CC       antipromoter activity, prevents promotion by tetradecanoyl phorbal
CC       acetate (TPA) in JB6 cells. Prevents tertiary butyl hydroperoxide-
CC       induced mutagenesis. Protects AT base pairs and shows antimutagenesis
CC       activity in TA102 and TA104 S.typhimurium mutagenesis tests. Inhibits
CC       paw edema formation induced by phospholipase A2 in Swiss Wistar mice.
CC       Prevents the release of arachidonate, the parent compound for the
CC       synthesis of prostaglandins and prostacyclins. Has antimalarial
CC       activity, kills P.falciparum. Has antivenom activity, nullifies the
CC       lethal effects of N.naja venom and inhibits phospholipase A2 present in
CC       N.naja venom. Has antifungal activity, inhibits cilia formation by
CC       A.niger. Is not toxic or allergenic. {ECO:0000250|UniProtKB:P01070,
CC       ECO:0000269|PubMed:1731625, ECO:0000269|PubMed:18177267,
CC       ECO:0000269|Ref.1}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Stable for 7 days at room temperature and for 30 days at 4 degrees
CC         Celsius. Remains active after incubation at 100 degrees Celsius for 3
CC         hours. {ECO:0000269|PubMed:1731625};
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:1731625}.
CC   -!- MASS SPECTROMETRY: Mass=14177.135; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18177267};
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000255}.
CC   -!- CAUTION: The order of the first peptide shown is unknown.
CC       {ECO:0000269|Ref.1}.
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DR   AlphaFoldDB; P85278; -.
DR   GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR   SUPFAM; SSF50386; SSF50386; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Antioxidant; Direct protein sequencing; Fungicide;
KW   Protease inhibitor; Serine protease inhibitor.
FT   CHAIN           <1..>85
FT                   /note="Turmerin"
FT                   /id="PRO_0000310822"
FT   SITE            57..?
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250|UniProtKB:P01070"
FT   UNSURE          26
FT                   /note="I OR L"
FT                   /evidence="ECO:0000269|Ref.1"
FT   UNSURE          30
FT                   /note="I OR L"
FT                   /evidence="ECO:0000269|Ref.1"
FT   UNSURE          36
FT                   /note="I OR L"
FT                   /evidence="ECO:0000269|Ref.1"
FT   UNSURE          39
FT                   /note="P OR T"
FT                   /evidence="ECO:0000269|Ref.1"
FT   UNSURE          48
FT                   /note="I OR L"
FT                   /evidence="ECO:0000269|Ref.1"
FT   UNSURE          51
FT                   /note="I OR L"
FT                   /evidence="ECO:0000269|Ref.1"
FT   UNSURE          52
FT                   /note="I OR L"
FT                   /evidence="ECO:0000269|Ref.1"
FT   UNSURE          59
FT                   /note="I OR L"
FT                   /evidence="ECO:0000269|Ref.1"
FT   UNSURE          64
FT                   /note="P OR T"
FT                   /evidence="ECO:0000269|Ref.1"
FT   NON_CONS        25..26
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_CONS        37..38
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_CONS        46..47
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_CONS        57..58
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_CONS        68..69
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_CONS        75..76
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_TER         85
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   85 AA;  9417 MW;  08BDB2AD292FCC40 CRC64;
     LCPLDVLQLS SELLDIDGNE VEASRILSDI TAFGGIRCPL TVVQSRGIGT IISSPYRFIA
     EGHPLSLKDM DGWFRVSDDE FNNYK