ID U5GKD1_POPTR Unreviewed; 339 AA.
AC U5GKD1;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PNT39725.1};
GN ORFNames=POPTR_004G055900 {ECO:0000313|EMBL:PNT39725.1};
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694 {ECO:0000313|EMBL:PNT39725.1, ECO:0000313|Proteomes:UP000006729};
RN [1] {ECO:0000313|EMBL:PNT39725.1, ECO:0000313|Proteomes:UP000006729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729};
RX PubMed=16973872; DOI=10.1126/science.1128691;
RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA Rokhsar D.;
RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL Science 313:1596-1604(2006).
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; CM009293; PNT39725.1; -; Genomic_DNA.
DR RefSeq; XP_006384060.1; XM_006383998.1.
DR AlphaFoldDB; U5GKD1; -.
DR STRING; 3694.U5GKD1; -.
DR MEROPS; C01.104; -.
DR EnsemblPlants; Potri.004G055900.1.v4.1; Potri.004G055900.1.v4.1; Potri.004G055900.v4.1.
DR GeneID; 18097499; -.
DR Gramene; Potri.004G055900.1.v4.1; Potri.004G055900.1.v4.1; Potri.004G055900.v4.1.
DR KEGG; pop:18097499; -.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_0_1; -.
DR InParanoid; U5GKD1; -.
DR OMA; PKTHFRY; -.
DR OrthoDB; 5472443at2759; -.
DR Proteomes; UP000006729; Chromosome 4.
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; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR PANTHER; PTHR12411:SF705; SENESCENCE-SPECIFIC CYSTEINE PROTEASE SAG12; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006729};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..339
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018541761"
FT DOMAIN 37..94
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 121..338
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 339 AA; 37403 MW; EF2A370E3228DF64 CRC64;
MAAKKCSIHI FLPFLLILAT KIVCRPLDEQ EYMLKRHEEW MAQHGRVYGD MKEKEKRYLI
FKENIERIEA FNNGSDRGYK LGVNKFADLT NEEFRAMHHG YKRQSSKLMS SSFRHENLSA
IPTSMDWRKA GAVTPVKDQG TCGCCWAFSA VAAIEGIIKL KTGKLISLSE QQLVDCDVKG
VDQGCGGGLM DNAFQFILRN GGLTSEATYP YQGVDGTCKS KKTASIEAKI TGYEDVPVNN
ENALLQAVAK QPVSVAVEGG GYDFQFYKSG VFKGDCGTYL DHAVTAIGYG TNSDGTNYWL
VKNSWGTSWG ESGYMRMQRG IGAREGLCGV AMDASYPTA
//