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Database: UniProt
Entry: A0A072VNU8_MEDTR
LinkDB: A0A072VNU8_MEDTR
Original site: A0A072VNU8_MEDTR 
ID   A0A072VNU8_MEDTR        Unreviewed;       627 AA.
AC   A0A072VNU8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Wall-associated receptor kinase-like protein, putative {ECO:0000313|EMBL:KEH39810.1};
GN   OrderedLocusNames=MTR_1g010250 {ECO:0000313|EMBL:KEH39810.1};
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 {ECO:0000313|EMBL:KEH39810.1, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:KEH39810.1, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:KEH39810.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:KEH39810,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA   Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA   Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA   Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA   Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA   Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA   Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA   Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA   Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA   Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA   Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA   Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA   Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA   Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA   Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA   Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA   Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA   Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA   Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA   Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA   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] {ECO:0000313|EMBL:KEH39810.1, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=A17 {ECO:0000313|EMBL:KEH39810.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:KEH39810,
RC   ECO:0000313|Proteomes:UP000002051};
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] {ECO:0000313|EnsemblPlants:KEH39810}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH39810};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00000327};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00000671};
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DR   EMBL; CM001217; KEH39810.1; -; Genomic_DNA.
DR   RefSeq; XP_013465774.1; XM_013610320.1.
DR   AlphaFoldDB; A0A072VNU8; -.
DR   EnsemblPlants; KEH39810; KEH39810; MTR_1g010250.
DR   Gramene; KEH39810; KEH39810; MTR_1g010250.
DR   HOGENOM; CLU_000288_43_5_1; -.
DR   Proteomes; UP000002051; Chromosome 1.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045274; WAK-like.
DR   InterPro; IPR025287; WAK_GUB.
DR   PANTHER; PTHR27005:SF470; ASSOCIATED KINASE-LIKE PROTEIN, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR27005; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 21; 1.
DR   Pfam; PF13947; GUB_WAK_bind; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KEH39810.1};
KW   Receptor {ECO:0000313|EMBL:KEH39810.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:KEH39810.1}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..627
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014500833"
FT   DOMAIN          296..578
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   627 AA;  69678 MW;  C8C48913956762C1 CRC64;
     MKVLQVLIIL AALAHLIEAV AFTLASDQPK QVLPGCNYTC GGVKVPYPFG IGNSTAQDHT
     PCYINSKFML TCTDNSKLIY GKNIQVLDIN PQGQMEMRFF VSHLCTNSSS NSNNNTEKAN
     KPSLRVSSLA ISSTDNKFIT VGCDSFGYLN SNFKGATYST GCLTRCYDFD TKMVIGNNTG
     KCTGLGCCEV DIPPLMKNIT IQAFKFSPST LSMENSCSYS FIAKQGSYNF SVEHIKKLPY
     NTFPMVVNWV VTNESCRIAQ TTNSYACKEN SECVDKDSDY DGYRCKCLAG FEGNPYVPGG
     CRGKGGFGTV YKGELDDNRI VAIKKSKTID KSQIEQFINE VDVVSQINHR NVVKLLGCCL
     ETEVPLLVYE FVSNGTLSEF IHTKGKTNDP TWKTRLKIAA EVAEALSYLH SYASTPIIHR
     DVKSDNILLD GTNTAKVSDF GASRLVPLDQ TEIATMVQGT IGYLDPEYMQ TSQLTEKSDV
     YSFGVVLVEL LTGEKPFCFG RPEERRSLAM HFLSCLKKDN VFEVIQDGLW NEENKQEIKE
     VAVLAAKCLR LRGEERPSMK EVAMELEGMR LMNKHSWIKD DSNVEESRYL LHESSSSIYE
     PGDSNKHGDI GYDSLKDHVL ITLDDGR
//
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