KI104_MEDTR
ID KI104_MEDTR Reviewed; 201 AA.
AC A0A072TH68;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Kunitz type trypsin inhibitor 104 {ECO:0000303|PubMed:23662629};
DE Flags: Precursor;
GN Name=KPI104 {ECO:0000303|PubMed:23662629};
GN ORFNames=MTR_0100s0150 {ECO:0000312|EMBL:KEH16752.1},
GN MtrunA17_Chr1g0173431 {ECO:0000312|EMBL:RHN79110.1};
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-155, AND INDUCTION BY ARBUSCULAR
RP MYCORRHIZAL FUNGI.
RC STRAIN=cv. Jemalong A17;
RX PubMed=12744459; DOI=10.1094/mpmi.2003.16.4.306;
RA Wulf A., Manthey K., Doll J., Perlick A.M., Linke B., Bekel T., Meyer F.,
RA Franken P., Kuester H., Krajinski F.;
RT "Transcriptional changes in response to arbuscular mycorrhiza development
RT in the model plant Medicago truncatula.";
RL Mol. Plant Microbe Interact. 16:306-314(2003).
RN [5]
RP FUNCTION, MUTAGENESIS OF LYS-170, INDUCTION BY ARBUSCULAR MYCORRHIZAL
RP FUNGI, INTERACTION WITH CP, DISULFIDE BOND, 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 involved in the control of mycorrhiza
CC establishment and arbuscule development during root colonization by
CC arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis).
CC {ECO:0000269|PubMed:23662629}.
CC -!- SUBUNIT: Interacts with CP. {ECO:0000269|PubMed:23662629}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23662629}. Secreted,
CC extracellular space, apoplast {ECO:0000269|PubMed:23662629}.
CC -!- INDUCTION: Accumulates in roots during colonization by arbuscular
CC mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis and Glomus
CC intraradices). {ECO:0000269|PubMed:12744459,
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; KL402825; KEH16752.1; -; Genomic_DNA.
DR EMBL; PSQE01000001; RHN79110.1; -; Genomic_DNA.
DR EMBL; AJ500250; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_013442727.1; XM_013587273.1.
DR AlphaFoldDB; A0A072TH68; -.
DR SMR; A0A072TH68; -.
DR MEROPS; I03.029; -.
DR EnsemblPlants; KEH16752; KEH16752; MTR_0100s0150.
DR GeneID; 25480281; -.
DR Gramene; KEH16752; KEH16752; MTR_0100s0150.
DR KEGG; mtr:MTR_0100s0150; -.
DR HOGENOM; CLU_090145_3_0_1; -.
DR OrthoDB; 1481039at2759; -.
DR Proteomes; UP000002051; Unassembled WGS sequence.
DR Proteomes; UP000265566; Chromosome 1.
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 CDD; cd00178; STI; 1.
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 PRINTS; PR00291; KUNITZINHBTR.
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..201
FT /note="Kunitz type trypsin inhibitor 104"
FT /id="PRO_5014498701"
FT SITE 170
FT /note="Important in determining the strength and
FT specificity of the interaction with its subsrate"
FT /evidence="ECO:0000269|PubMed:23662629"
FT DISULFID 63..110
FT /evidence="ECO:0000305|PubMed:23662629"
FT DISULFID 161..173
FT /evidence="ECO:0000305|PubMed:23662629"
FT DISULFID 166..169
FT /evidence="ECO:0000305|PubMed:23662629"
FT MUTAGEN 170
FT /note="K->E: Enables interaction with SCP1."
FT /evidence="ECO:0000269|PubMed:23662629"
SQ SEQUENCE 201 AA; 21624 MW; D4140A42C8A6ADB4 CRC64;
MSTRSLTIFI LAHVWLLMAT TSIAQFVIDT SGEPVEDDEE YFIRPAITGN GGGSTLVTGN
GPCPLHVGLD NTEGTLGVAV KFTPFAPQHD DDDVRLNRDL RVTFLTSTSC GQSTDWRLGE
KDATSGRRLI VTGRDNGAGS QGNFFRIVQT QTGGTYNIQW CPTEACPSCK VQCGTVGVIR
ENGKNLLALD GDALPVVFQK E
