UBPA_DICDI
ID UBPA_DICDI Reviewed; 837 AA.
AC P54201; Q54EP2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase A;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme A;
DE AltName: Full=Ubiquitin thioesterase A;
DE AltName: Full=Ubiquitin-specific-processing protease A;
GN Name=ubpA; Synonyms=usp5; ORFNames=DDB_G0291239;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=9786928; DOI=10.1074/jbc.273.44.29178;
RA Lindsey D.F., Amerik A., Deery W.J., Bishop J.D., Hochstrasser M.,
RA Gomer R.H.;
RT "A deubiquitinating enzyme that disassembles free polyubiquitin chains is
RT required for development but not growth in Dictyostelium.";
RL J. Biol. Chem. 273:29178-29187(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Required for development but not growth.
CC {ECO:0000269|PubMed:9786928}.
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 -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL61603.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U48271; AAC71068.1; -; mRNA.
DR EMBL; AAFI02000177; EAL61603.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_635198.2; XM_630106.2.
DR AlphaFoldDB; P54201; -.
DR SMR; P54201; -.
DR STRING; 44689.DDB0231492; -.
DR MEROPS; C19.104; -.
DR PaxDb; P54201; -.
DR EnsemblProtists; EAL61603; EAL61603; DDB_G0291239.
DR GeneID; 8628143; -.
DR KEGG; ddi:DDB_G0291239; -.
DR dictyBase; DDB_G0291239; ubpA.
DR eggNOG; KOG0944; Eukaryota.
DR InParanoid; P54201; -.
DR PhylomeDB; P54201; -.
DR Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR Reactome; R-DDI-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-DDI-8948751; Regulation of PTEN stability and activity.
DR PRO; PR:P54201; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; TAS:dictyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:dictyBase.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0140676; P:oscillatory cAMP signaling; IMP:dictyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR GO; GO:0016579; P:protein deubiquitination; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR InterPro; IPR041432; UBP13_Znf-UBP_var.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR Pfam; PF00627; UBA; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR Pfam; PF17807; zf-UBP_var; 1.
DR PIRSF; PIRSF016308; UBP; 1.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Protease; Reference proteome; Repeat;
KW Thiol protease; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..837
FT /note="Ubiquitin carboxyl-terminal hydrolase A"
FT /id="PRO_0000080686"
FT DOMAIN 319..835
FT /note="USP"
FT DOMAIN 628..669
FT /note="UBA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 700..740
FT /note="UBA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT ZN_FING 166..277
FT /note="UBP-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 676..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 328
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 797
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT CONFLICT 180
FT /note="T -> N (in Ref. 1; AAC71068)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="N -> I (in Ref. 1; AAC71068)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 837 AA; 94966 MW; 5E50A4E2CFE68BB4 CRC64;
MELFPELKNI KVPTEKSRLW KDECCYCFDT PENGEGLFID LIGLLAFSKK YVQLNHQKTH
HHLYLNFKKV AIVNEKVKSP TIENGGEEKP PKKLAIGVEG GFNVEDEEIK YEEHYKLYIF
PDDKFLELSD PIIPENVRVC CEKIKTLNSQ SRKEEIVSWN AESVFPSAFA ESIIQLDNNT
KKIDPKGPWR CDIEGCDKVE NLWLNLTDGF IGCGRKYADG TGGNGHAQEH FNQTQYPISV
KLGTITKDHA DVYSYPEDDM VSDPLLFQHL THWGLNPNVM VKTEKSMAEL ELDQNLNFEF
GKIQEKGKLL ENVFGPGLTG IENLGNSCYM SSVIQMIFAI DSFQTRYLKD REASFKDITQ
DPTQSFEIQM SKLAHGLLSG DYSIPLSKPS KNANEESEAA TQIGIAPKMF KSLIGASHAE
FSTMKQQDAH EYLQYLLEYI ERAEHSRPSW IQQANPTRLF QFHNEDRIEC GSSGQVKYTR
RLENILSVPV NLDDATNKQE VAQYEETLKQ QNGVRQKDQE EIRPIIPLVS CINGFVEPYR
VEDFLSPATG VKTFSLNSSR MATFPEVLII HLKKYTYNAD YTPKKLNVFM DVPDIIDIDS
LRGRGIKEGE VPLKEGTINT TTKVPEPSFN QEVLDTLLSM DFPLVRCKKA LLATGGKDAE
LAMNWIFEHT EDPDIDIEQT PVNNNNNNNN SSNSNDKLFV FNSQDVDNII GMGFTDSQAK
LALKNTKGNL ERAADWLFSH IDNLDELVAK DNASTSSINP SLIPQSTTSL QPVSDGVGKY
ELLGFISHLG NNVTCGHYVC HIKKNNRWIK FNDRHVQLSE QPPKELGYIY FYKRQLN
