ITRF_MAIZE
ID ITRF_MAIZE Reviewed; 155 AA.
AC P01088;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Trypsin/factor XIIA inhibitor;
DE AltName: Full=CHFI;
DE AltName: Full=Hageman factor inhibitor;
DE Flags: Precursor;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. A188; TISSUE=Endosperm;
RX PubMed=1558956; DOI=10.1007/bf00020026;
RA Wen L., Huang J.K., Zen K.C., Johnson B.H., Muthukrishnan S., Mackay V.,
RA Manney T.R., Manney M., Reeck G.R.;
RT "Nucleotide sequence of a cDNA clone that encodes the maize inhibitor of
RT trypsin and activated Hageman factor.";
RL Plant Mol. Biol. 18:813-814(1992).
RN [2]
RP PROTEIN SEQUENCE OF 29-138, AND ACTIVE SITE.
RC TISSUE=Seed;
RX PubMed=6610678; DOI=10.1016/s0021-9258(17)39746-6;
RA Mahoney W.C., Hermodson M.A., Jones B., Powers D.D., Corfman R.S.,
RA Reeck G.R.;
RT "Amino acid sequence and secondary structural analysis of the corn
RT inhibitor of trypsin and activated Hageman factor.";
RL J. Biol. Chem. 259:8412-8416(1984).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 33-148, AND DISULFIDE BONDS.
RX PubMed=9799488; DOI=10.1021/bi9812266;
RA Behnke C.A., Yee V.C., le Trong I., Pedersen L.C., Stenkamp R.E.,
RA Kim S.-S., Reeck G.R., Teller D.C.;
RT "Structural determinants of the bifunctional corn Hageman factor inhibitor:
RT X-ray crystal structure at 1.95-A resolution.";
RL Biochemistry 37:15277-15288(1998).
CC -!- FUNCTION: Potent inhibitor of mammalian trypsin and a specific
CC inhibitor of factor XIIa (activated hageman factor).
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MISCELLANEOUS: The sequence heterogeneity suggests that 2 genes exist
CC for this inhibitor. The genes may be alleles, or multiple loci could
CC exist.
CC -!- SIMILARITY: Belongs to the protease inhibitor I6 (cereal trypsin/alpha-
CC amylase inhibitor) family. {ECO:0000305}.
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DR EMBL; X54064; CAA37998.1; -; mRNA.
DR PIR; S20850; TIZM1.
DR PDB; 1BEA; X-ray; 1.95 A; A=29-155.
DR PDB; 1BFA; X-ray; 2.20 A; A=28-154.
DR PDBsum; 1BEA; -.
DR PDBsum; 1BFA; -.
DR AlphaFoldDB; P01088; -.
DR SMR; P01088; -.
DR STRING; 4577.GRMZM2G304548_P01; -.
DR MEROPS; I06.001; -.
DR PaxDb; P01088; -.
DR PRIDE; P01088; -.
DR EnsemblPlants; Zm00001eb095210_T001; Zm00001eb095210_P001; Zm00001eb095210.
DR Gramene; Zm00001eb095210_T001; Zm00001eb095210_P001; Zm00001eb095210.
DR MaizeGDB; 25928; -.
DR eggNOG; ENOG502R3FY; Eukaryota.
DR OMA; AECPWIL; -.
DR EvolutionaryTrace; P01088; -.
DR Proteomes; UP000007305; Chromosome 2.
DR ExpressionAtlas; P01088; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00261; AAI_SS; 1.
DR Gene3D; 1.10.110.10; -; 1.
DR InterPro; IPR044723; AAI_SS_dom.
DR InterPro; IPR006106; Allergen/soft/tryp_amyl_inhib.
DR InterPro; IPR006105; Allergen/tryp_amyl_inhib_CS.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR Pfam; PF00234; Tryp_alpha_amyl; 1.
DR PRINTS; PR00808; AMLASEINHBTR.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
DR PROSITE; PS00426; CEREAL_TRYP_AMYL_INH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:6610678"
FT CHAIN 29..138
FT /note="Trypsin/factor XIIA inhibitor"
FT /id="PRO_0000014357"
FT PROPEP 139..155
FT /note="C-terminal peptide"
FT /id="PRO_0000014358"
FT ACT_SITE 62
FT /evidence="ECO:0000269|PubMed:6610678"
FT DISULFID 34..83
FT /evidence="ECO:0000269|PubMed:9799488,
FT ECO:0007744|PDB:1BEA"
FT DISULFID 48..72
FT /evidence="ECO:0000269|PubMed:9799488,
FT ECO:0007744|PDB:1BEA"
FT DISULFID 57..114
FT /evidence="ECO:0000269|PubMed:9799488,
FT ECO:0007744|PDB:1BEA"
FT DISULFID 73..132
FT /evidence="ECO:0000269|PubMed:9799488,
FT ECO:0007744|PDB:1BEA"
FT DISULFID 85..143
FT /evidence="ECO:0000269|PubMed:9799488,
FT ECO:0007744|PDB:1BEA"
FT VARIANT 117
FT /note="E -> A"
FT CONFLICT 49
FT /note="R -> C (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="T -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="R -> RPR (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="R -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="R -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="R -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="A -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:1BEA"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:1BEA"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:1BEA"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1BEA"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:1BEA"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1BEA"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:1BEA"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:1BEA"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:1BEA"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1BEA"
SQ SEQUENCE 155 AA; 16302 MW; A31A8AA3BA19DE7A CRC64;
MASSSSSSHR RLILAAAVLL SVLAAASASA GTSCVPGWAI PHNPLPSCRW YVTSRTCGIG
PRLPWPELKR RCCRELADIP AYCRCTALSI LMDGAIPPGP DAQLEGRLED LPGCPREVQR
GFAATLVTEA ECNLATISGV AECPWILGGG TMPSK
