KI111_MEDTR
ID KI111_MEDTR Reviewed; 200 AA.
AC G7LCV7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Kunitz type trypsin inhibitor 111 {ECO:0000303|PubMed:23662629};
DE Flags: Precursor;
GN Name=KPI111 {ECO:0000312|EnsemblPlants:AET02982};
GN OrderedLocusNames=MTR_8g060550 {ECO:0000312|EMBL:AET02982.1},
GN MTR_8g461690 {ECO:0000312|EMBL:KEH19505.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3]
RP INTERACTION WITH SCP1, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=23662629; DOI=10.1111/tpj.12242;
RA Rech S.S., Heidt S., Requena N.;
RT "A tandem Kunitz protease inhibitor (KPI106)-serine carboxypeptidase (SCP1)
RT controls mycorrhiza establishment and arbuscule development in Medicago
RT truncatula.";
RL Plant J. 75:711-725(2013).
CC -!- SUBUNIT: Interacts with SCP1. {ECO:0000269|PubMed:23662629}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:G7LCV1}.
CC Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:G7LCV1}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
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DR EMBL; CM001224; AET02982.1; -; Genomic_DNA.
DR EMBL; CM001224; KEH19505.1; -; Genomic_DNA.
DR RefSeq; XP_003628506.1; XM_003628458.2.
DR RefSeq; XP_013445479.1; XM_013590025.1.
DR AlphaFoldDB; G7LCV7; -.
DR SMR; G7LCV7; -.
DR MEROPS; I03.029; -.
DR EnsemblPlants; AET02982; AET02982; MTR_8g060550.
DR EnsemblPlants; KEH19505; KEH19505; MTR_8g461690.
DR GeneID; 11406267; -.
DR Gramene; AET02982; AET02982; MTR_8g060550.
DR Gramene; KEH19505; KEH19505; MTR_8g461690.
DR KEGG; mtr:MTR_8g060550; -.
DR KEGG; mtr:MTR_8g461690; -.
DR eggNOG; ENOG502S0HP; Eukaryota.
DR HOGENOM; CLU_090145_3_0_1; -.
DR OMA; TICITGT; -.
DR OrthoDB; 1481039at2759; -.
DR Proteomes; UP000002051; Chromosome 8.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR InterPro; IPR002160; Prot_inh_Kunz-lg.
DR PANTHER; PTHR33107; PTHR33107; 1.
DR Pfam; PF00197; Kunitz_legume; 1.
DR SMART; SM00452; STI; 1.
DR SUPFAM; SSF50386; SSF50386; 1.
PE 1: Evidence at protein level;
KW Apoplast; Disulfide bond; Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..200
FT /note="Kunitz type trypsin inhibitor 111"
FT /id="PRO_5014574217"
FT SITE 169
FT /note="Important in determining the strength and
FT specificity of the interaction with its subsrate"
FT /evidence="ECO:0000250|UniProtKB:G7LCV1"
FT DISULFID 62..108
FT /evidence="ECO:0000250|UniProtKB:G7LCV1"
FT DISULFID 160..172
FT /evidence="ECO:0000250|UniProtKB:G7LCV1"
FT DISULFID 165..168
FT /evidence="ECO:0000250|UniProtKB:G7LCV1"
SQ SEQUENCE 200 AA; 21895 MW; 73E1DA9C82ACBA8D CRC64;
MSTISFTIFI LANVWLLVVT TSIAQFVIDT SGEPVENDED YFIRPAITGN GGSLTLVTRN
SCPFNVGLDP DAPQGFAVLL SPFVSNREED EVRLGRDLRV IFQAGTSCGQ STEWRLGERD
ATTGRRFIIT GRDDSTVGSY GNFFRIVQTP SRGIFNIQWC PTEVCPSCKF ECGTVGIVRE
NGKILLALDG SALPVAFQKE
