ID A0A1B6P5Q3_SORBI Unreviewed; 371 AA.
AC A0A1B6P5Q3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 2.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXG21060.2};
GN ORFNames=SORBI_3009G008800 {ECO:0000313|EMBL:KXG21060.2};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG21060.2, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:KXG21060.2, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000768; KXG21060.2; -; Genomic_DNA.
DR RefSeq; XP_002439128.1; XM_002439083.1.
DR AlphaFoldDB; A0A1B6P5Q3; -.
DR STRING; 4558.A0A1B6P5Q3; -.
DR EnsemblPlants; KXG21060; KXG21060; SORBI_3009G008800.
DR GeneID; 8068658; -.
DR Gramene; KXG21060; KXG21060; SORBI_3009G008800.
DR KEGG; sbi:8068658; -.
DR eggNOG; KOG1543; Eukaryota.
DR InParanoid; A0A1B6P5Q3; -.
DR OMA; ETWGNKG; -.
DR OrthoDB; 5472443at2759; -.
DR Proteomes; UP000000768; Chromosome 9.
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 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:SF1012; CYSTEINE PROTEASE CP1; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
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; Cysteine proteinases; 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 Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..371
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018521651"
FT DOMAIN 66..122
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 152..368
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 371 AA; 40537 MW; C3ECF902EDFE8884 CRC64;
MASSSARPVV AAVLLLCLLC GGSAWLQAAA EARPPHHMDS DSDDFFSIVG YSPEDLVHHD
RLIKLFEEWV AKYRKAYASF EEKLHRFEVF KDNLHHIDEA NKKVTTYWLG LNAFADLTHD
EFKATYLGLR QPETKKTTDS RFRYGGVADD DVPASVDWRK KGAVTDVKNQ GQCGSCWAFS
TVAAVEGINQ IVTGNLTSLS EQELVDCSTD GNNGCNGGVM DNAFSYIASS GGLRTEEAYP
YLMEEGDCDD KARDGEQVVT ISGYEDVPAN DEQALVKALA HQPLSVAIEA SGRHFQFYSG
GVFNGPCGSE LDHGVAAVGY GSSKGQDYII VKNSWGSHWG EKGYIRMKRG TGKPEGLCGI
NKMASYPTKD Q
//
