ID   UBP7_ARATH              Reviewed;         477 AA.
AC   Q84WC6; F4IXI8; Q9FPT3; Q9LU31;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 124.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 7;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 7;
DE            Short=AtUBP7;
DE   AltName: Full=Ubiquitin thioesterase 7;
DE   AltName: Full=Ubiquitin-specific-processing protease 7;
GN   Name=UBP7; OrderedLocusNames=At3g21280; ORFNames=MXL8.15;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=11115897; DOI=10.1104/pp.124.4.1828;
RA   Yan N., Doelling J.H., Falbel T.G., Durski A.M., Vierstra R.D.;
RT   "The ubiquitin-specific protease family from Arabidopsis. AtUBP1 and 2 are
RT   required for the resistance to the amino acid analog canavanine.";
RL   Plant Physiol. 124:1828-1843(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   INTERACTION WITH CALMODULIN.
RX   PubMed=15987637; DOI=10.1016/j.febslet.2005.05.080;
RA   Moon B.C., Choi M.S., Kang Y.H., Kim M.C., Cheong M.S., Park C.Y.,
RA   Yoo J.H., Koo S.C., Lee S.M., Lim C.O., Cho M.J., Chung W.S.;
RT   "Arabidopsis ubiquitin-specific protease 6 (AtUBP6) interacts with
RT   calmodulin.";
RL   FEBS Lett. 579:3885-3890(2005).
CC   -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal
CC       Gly of ubiquitin. Involved in the processing of poly-ubiquitin
CC       precursors as well as that of ubiquitinated proteins (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12;
CC   -!- SUBUNIT: Interacts with calmodulin (CaM).
CC       {ECO:0000269|PubMed:15987637}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AEE76487.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB01721.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF302661; AAG42752.1; -; mRNA.
DR   EMBL; AB023045; BAB01721.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE76487.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BT003992; AAO42031.1; -; mRNA.
DR   RefSeq; NP_566680.2; NM_113023.4.
DR   AlphaFoldDB; Q84WC6; -.
DR   SMR; Q84WC6; -.
DR   BioGRID; 7014; 6.
DR   STRING; 3702.Q84WC6; -.
DR   MEROPS; C19.A05; -.
DR   PaxDb; 3702-AT3G21280-1; -.
DR   ProteomicsDB; 245288; -.
DR   GeneID; 821682; -.
DR   KEGG; ath:AT3G21280; -.
DR   Araport; AT3G21280; -.
DR   TAIR; AT3G21280; UBP7.
DR   eggNOG; KOG1872; Eukaryota.
DR   HOGENOM; CLU_017549_2_1_1; -.
DR   InParanoid; Q84WC6; -.
DR   OrthoDB; 160664at2759; -.
DR   PhylomeDB; Q84WC6; -.
DR   PRO; PR:Q84WC6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q84WC6; baseline and differential.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IBA:GO_Central.
DR   CDD; cd02657; Peptidase_C19A; 1.
DR   CDD; cd16104; Ubl_USP14_like; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR044635; UBP14-like.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR43982:SF1; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   Genevisible; Q84WC6; AT.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Hydrolase; Protease; Reference proteome;
KW   Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..477
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 7"
FT                   /id="PRO_0000313034"
FT   DOMAIN          2..77
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          104..473
FT                   /note="USP"
FT   REGION          171..190
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          364..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        113
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        425
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   CONFLICT        209
FT                   /note="S -> F (in Ref. 1; AAG42752)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        217
FT                   /note="P -> A (in Ref. 1; AAG42752)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   477 AA;  53516 MW;  82B469EE366B5E13 CRC64;
     MLTVSVKWQK KVFESIEIDT SQPPFVFKAQ LYDLSGVPPE RQKIMVKGGL LKDDADWSTL
     GLKNGQKLMM MGTADEIVKA PEKGPVFMED LPEEQQAANL GYSAGLVNLG NTCYMNSTMQ
     CLISVPELKS ELSNYQSART KDVDQTSHML TVATRELFSE LDKSVKAVAP MPFWMVLQKK
     YPQFAQLHNG NHMQQDAEEC WTQMLYTLSQ SLKLPSPSED PDAVKALFGL NLLNRLHCQE
     SSEESSETES VFSLKCHISH EVNHLHEGLK HGLKGELEKT SPSLGRTAVY VKESLIDSLP
     RYLTVQFVRF FWKRESNQKA KILRKVDYPL ELDIYDLCSE DLRKKLEAPR QKLRDIEGQK
     LGLQASAKSS SKGDDVKMTD AEGSSNQSGE SSTGDQQEGA SPHMTGIYDL VSVLTHKGRS
     ADSGHYVAWV KQESGKWVQY DDANTSLQRG EDIIKLSGGG DWHMAYIVMY KARLISM
//