KI106_MEDTR
ID KI106_MEDTR Reviewed; 204 AA.
AC G7LCV1;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Kunitz type trypsin inhibitor 106 {ECO:0000303|PubMed:23662629};
DE Flags: Precursor;
GN Name=KPI106 {ECO:0000303|PubMed:23662629};
GN OrderedLocusNames=MTR_8g059790 {ECO:0000312|EMBL:AET02976.1};
GN ORFNames=MtrunA17_Chr8g0359161 {ECO:0000312|EMBL:RHN40828.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=30397259; DOI=10.1038/s41477-018-0286-7;
RA Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S.,
RA Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M.,
RA Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W.,
RA Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F.,
RA Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F.,
RA Benhamed M., Crespi M., Gouzy J., Gamas P.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 4:1017-1025(2018).
RN [4]
RP FUNCTION, MUTAGENESIS OF LYS-173, TISSUE SPECIFICITY, INDUCTION BY
RP ARBUSCULAR MYCORRHIZAL FUNGI, INTERACTION WITH SCP1 AND CP, DISULFIDE BOND,
RP 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 -!- FUNCTION: Protease inhibitor that, together with SCP1, controls
CC mycorrhiza establishment and arbuscule development during root
CC colonization by arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus
CC irregularis), probably by degrading SCP1 in the apoplast of the
CC periarbuscular region. {ECO:0000269|PubMed:23662629}.
CC -!- SUBUNIT: Interacts with SCP1 and CP. {ECO:0000269|PubMed:23662629}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23662629}. Secreted,
CC extracellular space, apoplast {ECO:0000269|PubMed:23662629}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in non-mycorrhizal roots.
CC {ECO:0000269|PubMed:23662629}.
CC -!- INDUCTION: Accumulates in roots during colonization by arbuscular
CC mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis).
CC {ECO:0000269|PubMed:23662629}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
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DR EMBL; CM001224; AET02976.1; -; Genomic_DNA.
DR EMBL; PSQE01000008; RHN40828.1; -; Genomic_DNA.
DR RefSeq; XP_003628500.1; XM_003628452.1.
DR AlphaFoldDB; G7LCV1; -.
DR SMR; G7LCV1; -.
DR MEROPS; I03.029; -.
DR EnsemblPlants; AET02976; AET02976; MTR_8g059790.
DR GeneID; 11409843; -.
DR Gramene; AET02976; AET02976; MTR_8g059790.
DR KEGG; mtr:MTR_8g059790; -.
DR eggNOG; ENOG502S0HP; Eukaryota.
DR HOGENOM; CLU_090145_3_0_1; -.
DR OMA; NESCPLH; -.
DR OrthoDB; 1481039at2759; -.
DR Proteomes; UP000002051; Chromosome 8.
DR Proteomes; UP000265566; Chromosome 8.
DR GO; GO:0048046; C:apoplast; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0036377; P:arbuscular mycorrhizal association; IMP:UniProtKB.
DR GO; GO:0009610; P:response to symbiotic fungus; IEP:UniProtKB.
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; Glycoprotein; Protease inhibitor;
KW Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..204
FT /note="Kunitz type trypsin inhibitor 106"
FT /id="PRO_5014574211"
FT SITE 173
FT /note="Important in determining the strength and
FT specificity of the interaction with its subsrate"
FT /evidence="ECO:0000269|PubMed:23662629"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 65..112
FT /evidence="ECO:0000305|PubMed:23662629"
FT DISULFID 164..176
FT /evidence="ECO:0000305|PubMed:23662629"
FT DISULFID 169..172
FT /evidence="ECO:0000305|PubMed:23662629"
FT MUTAGEN 173
FT /note="K->E: Stronger interaction with SCP1."
FT /evidence="ECO:0000269|PubMed:23662629"
SQ SEQUENCE 204 AA; 22663 MW; 27D840CF72AB413A CRC64;
MSMRLSIRTL IILAHVCLFI TTTTIAQFVL DTVGEPVEGD EEYFIRPVIT NKGGRSTMVS
RNESCPLHVG LELTGLGRGL VVKFTPFAPH HDFDDVRVNR DLRITFQASS SCVQSTEWRL
GEKDTKSGRR LIITGTDSAT NGSYGNFFRI VETPLEGMYN IQWCPTEVCP SCKFECGTVD
MLNENGKILL ALDGGPLPLV FQKE
