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Database: UniProt
Entry: Q2HTQ3_MEDTR
LinkDB: Q2HTQ3_MEDTR
Original site: Q2HTQ3_MEDTR 
ID   Q2HTQ3_MEDTR            Unreviewed;       474 AA.
AC   Q2HTQ3;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 107.
DE   SubName: Full=Granulin; Peptidase C1A, papain {ECO:0000313|EMBL:ABD32628.1};
DE   SubName: Full=Papain family cysteine protease {ECO:0000313|EMBL:AES59384.1};
GN   Name=11414228 {ECO:0000313|EnsemblPlants:AES59384};
GN   OrderedLocusNames=MTR_1g018840 {ECO:0000313|EMBL:AES59384.1};
GN   ORFNames=MtrDRAFT_AC150207g18v2 {ECO:0000313|EMBL:ABD32628.1};
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:ABD32628.1};
RN   [1] {ECO:0000313|EMBL:ABD32628.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Town C.D.;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABD32628.1}
RP   NUCLEOTIDE SEQUENCE.
RG   The International Medicago Genome Annotation Group;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AES59384.1, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:AES59384.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES59384,
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   [4] {ECO:0000313|EMBL:AES59384.1, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES59384,
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   [5] {ECO:0000313|EnsemblPlants:AES59384}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES59384};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
CC       {ECO:0000256|ARBA:ARBA00008455}.
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DR   EMBL; AC150207; ABD32628.1; -; Genomic_DNA.
DR   EMBL; CM001217; AES59384.1; -; Genomic_DNA.
DR   RefSeq; XP_003589133.1; XM_003589085.2.
DR   AlphaFoldDB; Q2HTQ3; -.
DR   STRING; 3880.Q2HTQ3; -.
DR   MEROPS; C01.029; -.
DR   PaxDb; 3880-AES59384; -.
DR   ProMEX; Q2HTQ3; -.
DR   EnsemblPlants; AES59384; AES59384; MTR_1g018840.
DR   GeneID; 11414228; -.
DR   Gramene; AES59384; AES59384; MTR_1g018840.
DR   KEGG; mtr:11414228; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   eggNOG; KOG4296; Eukaryota.
DR   OMA; LYNVPNC; -.
DR   OrthoDB; 5472443at2759; -.
DR   Proteomes; UP000002051; Chromosome 1.
DR   ExpressionAtlas; Q2HTQ3; differential.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF854; ORYZAIN ALPHA CHAIN; 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};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AES59384.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          55..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;  52221 MW;  1CF93099B0755F43 CRC64;
     MDSNTLSPAM KLMIVLIISS FTVSLALDMS IISYDKTHPD KSTSKRTNKE VLTMYEEWLV
     KHGKSYNGLG EKDKRFEIFK DNLKFIDEHN GLNSTYRLGL TRFADLTNEE YRSKFLGTKI
     DPNRRMKKLG GSKSNRYAPR VGDKLPESVD WRKEGAVVGV KDQASCGSCW AFSAIAAVEG
     INKIVTGDLI SLSEQELVDC DTSYNEGCNG GLMDYAFEFI ISNGGIDSED DYPYKAVDGR
     CDQNRKNAKV VTIDDYEDVP AYDELALQKA VANQPIAVAV EGGGREFQLY EYGVFTGRCG
     TALDHGVAAV GYGTENGKDY WIVRNSWGGS WGEQGYIRLE RNLASSRAGK CGIAIEPSYP
     IKNGQNPPNP GPSPPSPIKP PSVCDSYYSC AEGSTCCCIY EYGRSCFEWG CCPLESATCC
     DDHYSCCPHE YPVCDTRAGL CLKGKNNPLG VKSFKRTPAK PHWAFGGKNK MSNA
//
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