ID G7J6Z3_MEDTR Unreviewed; 474 AA.
AC G7J6Z3;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Papain family cysteine protease {ECO:0000313|EMBL:AES73337.1};
DE SubName: Full=Putative actinidain {ECO:0000313|EMBL:RHN70315.1};
DE EC=3.4.22.14 {ECO:0000313|EMBL:RHN70315.1};
GN Name=11424546 {ECO:0000313|EnsemblPlants:AES73337};
GN OrderedLocusNames=MTR_3g102220 {ECO:0000313|EMBL:AES73337.1};
GN ORFNames=MtrunA17_Chr3g0134231 {ECO:0000313|EMBL:RHN70315.1};
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:AES73337.1, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:AES73337.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:AES73337.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:AES73337,
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:AES73337.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES73337,
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:AES73337}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES73337};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [4] {ECO:0000313|EMBL:RHN70315.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:RHN70315.1};
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 C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; CM001219; AES73337.1; -; Genomic_DNA.
DR EMBL; PSQE01000003; RHN70315.1; -; Genomic_DNA.
DR RefSeq; XP_003603086.1; XM_003603038.2.
DR AlphaFoldDB; G7J6Z3; -.
DR STRING; 3880.G7J6Z3; -.
DR MEROPS; C01.029; -.
DR PaxDb; 3880-AES73337; -.
DR EnsemblPlants; AES73337; AES73337; MTR_3g102220.
DR GeneID; 11424546; -.
DR Gramene; AES73337; AES73337; MTR_3g102220.
DR KEGG; mtr:11424546; -.
DR eggNOG; KOG1543; Eukaryota.
DR eggNOG; KOG4296; Eukaryota.
DR HOGENOM; CLU_012184_0_1_1; -.
DR OMA; NGYRKPC; -.
DR OrthoDB; 5472443at2759; -.
DR Proteomes; UP000002051; Chromosome 3.
DR Proteomes; UP000265566; Chromosome 3.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd02248; Peptidase_C1A; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 2.10.25.160; Granulin; 1.
DR InterPro; IPR000118; Granulin.
DR InterPro; IPR037277; Granulin_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR PANTHER; PTHR12411:SF937; CYSTEINE PROTEINASE RD21A; 1.
DR Pfam; PF00396; Granulin; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00277; GRAN; 1.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57277; Granulin repeat; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RHN70315.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AES73337.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..474
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014485597"
FT DOMAIN 53..111
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 145..361
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
FT DOMAIN 384..441
FT /note="Granulins"
FT /evidence="ECO:0000259|SMART:SM00277"
SQ SEQUENCE 474 AA; 52354 MW; 36D335958E69AC64 CRC64;
MGSNSNRSPM LVILIVFTLF TATFALDMSI ISYDKTHSDK SSRRSDKEVK NIYEEWRVKH
GKLNNNIDGS EKDKRFEIFK DNLKFIDEHN AENRTYKVGL NRFADLSNEE YRSRYLGTKI
DPIGMMMART KTRSNRYAPS VGDKLPKSVD WRSQGAVVQV KDQGSCGSCW AFSTIAAVEG
INKIVTGELV SLSEQELVDC DRTVNAGCDG GLMEYAFEFI INNGGIDSDE DYPYRGVDGK
CDQYKKNARV VSIDDYEQVP AYDELALKKA VANQPISVAI EAGGREFQLY VSGIFTGKCG
TALDHGVTAV GYGTENGVDY WIVRNSWGKS WGESGYVRME RNLAASVAGK CGIVMQSSYP
IKKGQNPPNP GPSPPSPVNP PNVCSRYHSC ASSTTCCCVF GIGKLCFSWG CCPLEAAVCC
KDHSSCCPHN YPICNTRQGT CLRSKDNPFG VKAMKRTPAK LHWPFGDQNK IDVA
//
