UniProt: A0A072V9D5

Database: UniProt
Entry: A0A072V9D5_MEDTR

LinkDB:  A0A072V9D5_MEDTR 
Original site:  A0A072V9D5_MEDTR

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (8)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (1)   
Literature (3)   
   PubMed (3)   
All databases (19)   

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ID   A0A072V9D5_MEDTR        Unreviewed;       457 AA.
AC   A0A072V9D5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Eukaryotic aspartyl protease family protein {ECO:0000313|EMBL:KEH38402.1};
DE   SubName: Full=Putative nepenthesin {ECO:0000313|EMBL:RHN74677.1};
DE            EC=3.4.23.12 {ECO:0000313|EMBL:RHN74677.1};
GN   Name=25487061 {ECO:0000313|EnsemblPlants:KEH38402};
GN   OrderedLocusNames=MTR_2g070430 {ECO:0000313|EMBL:KEH38402.1};
GN   ORFNames=MtrunA17_Chr2g0312941 {ECO:0000313|EMBL:RHN74677.1};
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:KEH38402.1, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:KEH38402.1, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:KEH38402.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:KEH38402,
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:KEH38402.1, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=A17 {ECO:0000313|EMBL:KEH38402.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:KEH38402,
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:KEH38402}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH38402};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
RN   [4] {ECO:0000313|Proteomes:UP000265566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|Proteomes:UP000265566};
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   [5] {ECO:0000313|EMBL:RHN74677.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:RHN74677.1};
RA   Pecrix Y., Gamas P., Carrere S.;
RT   "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL   Nat. Plants 0:0-0(2018).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; CM001218; KEH38402.1; -; Genomic_DNA.
DR   EMBL; PSQE01000002; RHN74677.1; -; Genomic_DNA.
DR   RefSeq; XP_013464367.1; XM_013608913.1.
DR   AlphaFoldDB; A0A072V9D5; -.
DR   EnsemblPlants; KEH38402; KEH38402; MTR_2g070430.
DR   GeneID; 25487061; -.
DR   Gramene; KEH38402; KEH38402; MTR_2g070430.
DR   KEGG; mtr:25487061; -.
DR   HOGENOM; CLU_005738_8_5_1; -.
DR   OrthoDB; 1131437at2759; -.
DR   Proteomes; UP000002051; Chromosome 2.
DR   Proteomes; UP000265566; Chromosome 2.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05476; pepsin_A_like_plant; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR034161; Pepsin-like_plant.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR032799; TAXi_C.
DR   InterPro; IPR032861; TAXi_N.
DR   PANTHER; PTHR47967:SF23; OS04G0448300 PROTEIN; 1.
DR   PANTHER; PTHR47967; OS07G0603500 PROTEIN-RELATED; 1.
DR   Pfam; PF14541; TAXi_C; 1.
DR   Pfam; PF14543; TAXi_N; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW   Hydrolase {ECO:0000313|EMBL:RHN74677.1};
KW   Protease {ECO:0000313|EMBL:KEH38402.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051}.
FT   DOMAIN          88..449
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   457 AA;  50349 MW;  495B25ADD40E7ADF CRC64;
     MASSFSFLTL FVLFCVYIPI GTMSFSMKLI PRVNFDSILF PKNISLEEKH NRLVQLSKIH
     ALKYQMNNTN AISPQTFQPL VPTISNIYAV EMRIGTPPFT TLLMFDTGSS DTWVQCLGCT
     KCFPLKGENF KYQASNTFKE VPCEHPLCDP KKCSDGKCEY AITYADGAKS KGILLFETFN
     FPPGPSNIVI DKRFLSFKGV VFGCGLQSEK MTFGVGVPMT DNNVIGGMFG LGPEPRSFLK
     QLKAETNMRF SYCLGQFLDP QSHNYLHFGP DAKISGDFKT TSLVPTIGSL TLIHYHVVCK
     GISLDGNKLP IDPKLFEVKS DGSGGFILDT GAYATILVQS AYQVLKQRVM AYFQQKGLSP
     STEKKLSLDL CYLNPPPNIV KPTITYHFDG GADFVVAPES GFLSAGDGRN KVFCLAVLGH
     NDFGNILGVI NQADHTFLFD VGKNQVSFTP KAKTCSK
//

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