CATB_MEDTR
ID CATB_MEDTR Reviewed; 350 AA.
AC A0A072UTP9; A0A396IJR2; I3T8K3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Pro-cathepsin H {ECO:0000305};
DE AltName: Full=Cysteine protease {ECO:0000303|PubMed:23662629};
DE Contains:
DE RecName: Full=Cathepsin H mini chain {ECO:0000305};
DE Contains:
DE RecName: Full=Cathepsin H {ECO:0000305};
DE EC=3.4.22.16 {ECO:0000305};
DE Contains:
DE RecName: Full=Cathepsin H heavy chain {ECO:0000305};
DE Contains:
DE RecName: Full=Cathepsin H light chain {ECO:0000305};
DE Flags: Precursor;
GN Name=CP {ECO:0000303|PubMed:23662629};
GN OrderedLocusNames=MTR_4g125300 {ECO:0000312|EMBL:KEH32433.1};
GN ORFNames=MtrunA17_Chr0c27g0493921 {ECO:0000312|EMBL:RHN38409.1},
GN MtrunA17_Chr4g0070441 {ECO:0000312|EMBL:RHN64564.1};
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 [MRNA].
RA Krishnakumar V., Cheung F., Xiao Y., Chan A., Moskal W.A., Town C.D.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
RP INTERACTION WITH KPI104 AND KPI106.
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: May play a role in proteolysis leading to mobilization of
CC nitrogen during senescence and starvation. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins, acting as an aminopeptidase (notably,
CC cleaving Arg-|-Xaa bonds) as well as an endopeptidase.; EC=3.4.22.16;
CC Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with KPI104 and KPI106 (PubMed:23662629). Composed
CC of a mini chain and a large chain. The large chain may be split into
CC heavy and light chain. All chains are held together by disulfide bonds.
CC {ECO:0000269|PubMed:23662629}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250|UniProtKB:Q8H166}. Lysosome
CC {ECO:0000250|UniProtKB:P07688}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
CC -!- SEQUENCE CAUTION:
CC Sequence=RHN64564.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BT149051; AFK48845.1; -; mRNA.
DR EMBL; CM001220; KEH32433.1; -; Genomic_DNA.
DR EMBL; PSQE01000026; RHN38409.1; -; Genomic_DNA.
DR EMBL; PSQE01000004; RHN64564.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_013458402.1; XM_013602948.1.
DR AlphaFoldDB; A0A072UTP9; -.
DR SMR; A0A072UTP9; -.
DR EnsemblPlants; KEH32433; KEH32433; MTR_4g125300.
DR GeneID; 25494167; -.
DR Gramene; KEH32433; KEH32433; MTR_4g125300.
DR KEGG; mtr:MTR_4g125300; -.
DR HOGENOM; CLU_012184_1_1_1; -.
DR OrthoDB; 1275401at2759; -.
DR Proteomes; UP000002051; Chromosome 4.
DR Proteomes; UP000265566; Chromosome 4.
DR ExpressionAtlas; A0A072UTP9; differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; 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 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; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW Reference proteome; Signal; Thiol protease; Vacuole; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..113
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P09668"
FT /id="PRO_0000450047"
FT PEPTIDE 114..121
FT /note="Cathepsin H mini chain"
FT /evidence="ECO:0000250|UniProtKB:P09668"
FT /id="PRO_0000450048"
FT PROPEP 122..132
FT /evidence="ECO:0000250|UniProtKB:P09668"
FT /id="PRO_0000450049"
FT CHAIN 133..350
FT /note="Cathepsin H"
FT /id="PRO_5014483351"
FT CHAIN 133..308
FT /note="Cathepsin H heavy chain"
FT /evidence="ECO:0000250|UniProtKB:P09668"
FT /id="PRO_0000450050"
FT CHAIN 309..350
FT /note="Cathepsin H light chain"
FT /evidence="ECO:0000250|UniProtKB:P09668"
FT /id="PRO_0000450051"
FT ACT_SITE 157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT ACT_SITE 297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 154..197
FT /evidence="ECO:0000250|UniProtKB:P07688"
FT DISULFID 188..230
FT /evidence="ECO:0000250|UniProtKB:P07688"
FT DISULFID 288..338
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT CONFLICT 46..52
FT /note="Missing (in Ref. 1; AFK48845)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="A -> V (in Ref. 1; AFK48845)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="S -> G (in Ref. 1; AFK48845)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 38752 MW; 58E04B5758D60A70 CRC64;
MAQWTLLIVF FCVATAAAGL SFHDSNPIRM VSDMEEQLLQ VIGESRHAVS FARFANRYGK
RYDTVDEMKR RFKIFSENLQ LIKSTNKKRL GYTLGVNHFA DWTWEEFRSH RLGAAQNCSA
TLKGNHRITD VVLPAEKDWR KEGIVSEVKD QGHCGSCWTF STTGALESAY AQAFGKNISL
SEQQLVDCAG AYNNFGCNGG LPSQAFEYIK YNGGLETEEA YPYTGQNGLC KFTSENVAVQ
VLGSVNITLG AEDELKHAVA FARPVSVAFQ VVDDFRLYKK GVYTSTTCGS TPMDVNHAVL
AVGYGIEDGV PYWLIKNSWG GEWGDHGYFK MEMGKNMCGV ATCSSYPVVA
