UCH37_PLAF7
ID UCH37_PLAF7 Reviewed; 465 AA.
AC Q8IIJ6;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase UCH54 {ECO:0000303|PubMed:16925553};
DE EC=3.4.19.12 {ECO:0000269|PubMed:16925553, ECO:0000269|PubMed:31658303};
DE AltName: Full=PfUCH37 {ECO:0000303|PubMed:31658303};
DE AltName: Full=PfUCH54 {ECO:0000303|PubMed:16925553};
GN Name=UCH54 {ECO:0000303|PubMed:16925553};
GN Synonyms=UCH37 {ECO:0000303|PubMed:31658303};
GN ORFNames=PF3D7_1117100 {ECO:0000312|EMBL:CZT98832.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000312|Proteomes:UP000001450};
RN [1] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND MUTAGENESIS OF CYS-145.
RX PubMed=16925553; DOI=10.1111/j.1365-2958.2006.05307.x;
RA Artavanis-Tsakonas K., Misaghi S., Comeaux C.A., Catic A., Spooner E.,
RA Duraisingh M.T., Ploegh H.L.;
RT "Identification by functional proteomics of a
RT deubiquitinating/deNeddylating enzyme in Plasmodium falciparum.";
RL Mol. Microbiol. 61:1187-1195(2006).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, IDENTIFICATION BY MASS
RP SPECTROMETRY, DOMAIN, AND MUTAGENESIS OF ASN-18; ASP-38 AND
RP 251-LYS--MET-295.
RX PubMed=31658303; DOI=10.1371/journal.ppat.1008086;
RA Karpiyevich M., Adjalley S., Mol M., Ascher D.B., Mason B.,
RA van der Heden van Noort G.J., Laman H., Ovaa H., Lee M.C.S.,
RA Artavanis-Tsakonas K.;
RT "Nedd8 hydrolysis by UCH proteases in Plasmodium parasites.";
RL PLoS Pathog. 15:e1008086-e1008086(2019).
CC -!- FUNCTION: Thiol protease that recognizes and hydrolyzes a peptide bond
CC at the C-terminal glycine of either ubiquitin or NEDD8.
CC {ECO:0000269|PubMed:16925553, ECO:0000269|PubMed:31658303}.
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; Evidence={ECO:0000269|PubMed:16925553,
CC ECO:0000269|PubMed:31658303};
CC -!- DEVELOPMENTAL STAGE: Expressed during the parasite blood stage, in
CC schizonts (at protein level). {ECO:0000269|PubMed:16925553,
CC ECO:0000269|PubMed:31658303}.
CC -!- DOMAIN: The Asn-rich domain is dispensable for deubiquitinating and
CC deneddylating activities. {ECO:0000269|PubMed:31658303}.
CC -!- SIMILARITY: Belongs to the peptidase C12 family. {ECO:0000305}.
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DR EMBL; LN999945; CZT98832.1; -; Genomic_DNA.
DR RefSeq; XP_001347848.1; XM_001347812.1.
DR AlphaFoldDB; Q8IIJ6; -.
DR SMR; Q8IIJ6; -.
DR STRING; 5833.PF11_0177; -.
DR MEROPS; C12.A12; -.
DR PRIDE; Q8IIJ6; -.
DR EnsemblProtists; CZT98832; CZT98832; PF3D7_1117100.
DR GeneID; 810724; -.
DR KEGG; pfa:PF3D7_1117100; -.
DR VEuPathDB; PlasmoDB:PF3D7_1117100; -.
DR HOGENOM; CLU_018316_0_1_1; -.
DR InParanoid; Q8IIJ6; -.
DR OMA; GVGDIGW; -.
DR PhylomeDB; Q8IIJ6; -.
DR Reactome; R-PFA-5689603; UCH proteinases.
DR Proteomes; UP000001450; Chromosome 11.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0019784; F:deNEDDylase activity; IDA:UniProtKB.
DR GO; GO:0000338; P:protein deneddylation; IDA:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:GeneDB.
DR Gene3D; 3.40.532.10; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR PANTHER; PTHR10589; PTHR10589; 1.
DR Pfam; PF01088; Peptidase_C12; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..465
FT /note="Ubiquitin carboxyl-terminal hydrolase UCH54"
FT /id="PRO_0000451573"
FT REGION 244..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8IKM8"
FT ACT_SITE 220
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT SITE 235
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT MUTAGEN 18
FT /note="N->D: No effect on deubiquitinating and
FT deneddylating activities; when associated with 251-K--M-295
FT DEL."
FT /evidence="ECO:0000269|PubMed:31658303"
FT MUTAGEN 38
FT /note="D->E: No defect in parasite growth in host
FT erythrocytes. Severe loss of deneddylating activity with no
FT effect on deubiquitinating activity; when associated with
FT 251-K--M-295 DEL."
FT /evidence="ECO:0000269|PubMed:31658303"
FT MUTAGEN 145
FT /note="C->S: Complete loss of deubiquitinating and
FT deneddylating activities."
FT /evidence="ECO:0000269|PubMed:16925553"
FT MUTAGEN 251..295
FT /note="Missing: No effect on deubiquitinating activity.
FT Slight increase in deneddylating activity. Severe loss of
FT deneddylating activity with no effect on deubiquitinating
FT activity; when associated with E-38. No effect on
FT deubiquitinating and deneddylating activities; when
FT associated with D-18."
FT /evidence="ECO:0000269|PubMed:31658303"
SQ SEQUENCE 465 AA; 54460 MW; 138A55EB774F99DD CRC64;
MARDNENILE EWCLIESNPC IFYDMLKRMG ATEISVEDVY SLSYFDDYIN NKEIINMNHI
LGVDTYLGEN NKTLDKENNV VDVIELYKNN ICMEDKYNKL LKHHSYIYGI IFLFNIGKHY
KNNKYIEHNV PDNLFFAKQV IPNACATQAI LSIVLNKDIE LNDEIKNIKT FSLNFDSSMK
GLTLSNCTFL RNIHNSYKPP IYLDKEDVHH DKKKSEDSFH FVSYISFQDK VYLLDGLQSG
PVLINADEQN KPNPNNNNNN KDNDNDNNNN NNNNNNNNNN NNNNNNNNNN NNIGMNGKDW
IEISREHIKK EIDEICNSQT NNDVRFNIIA VMKDKEYIIQ EYINIHRIVK QRVNIKLINL
GENIELSDEI NEDEFPLLND IPSIENLPNN VDTLYNIVNK STLEINYLQS LLHEQKEIKK
LWNKELTFKF FNFYPFIMSS LNLMAKHKLL KDAYQKEKLK NATKS
