UBP42_RAT
ID UBP42_RAT Reviewed; 1325 AA.
AC D3ZU96;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 42;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 42;
DE AltName: Full=Ubiquitin thioesterase 42;
DE AltName: Full=Ubiquitin-specific-processing protease 42;
GN Name=Usp42;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1228; SER-1231 AND SER-1235,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Deubiquitinating enzyme which may play an important role
CC during spermatogenesis. {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 -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; CH474012; EDL89655.1; -; Genomic_DNA.
DR RefSeq; NP_001099379.1; NM_001105909.1.
DR RefSeq; XP_017453778.1; XM_017598289.1.
DR AlphaFoldDB; D3ZU96; -.
DR SMR; D3ZU96; -.
DR STRING; 10116.ENSRNOP00000001404; -.
DR iPTMnet; D3ZU96; -.
DR PhosphoSitePlus; D3ZU96; -.
DR PaxDb; D3ZU96; -.
DR PeptideAtlas; D3ZU96; -.
DR PRIDE; D3ZU96; -.
DR Ensembl; ENSRNOT00000095083; ENSRNOP00000093270; ENSRNOG00000001059.
DR GeneID; 288482; -.
DR KEGG; rno:288482; -.
DR CTD; 84132; -.
DR RGD; 1305231; Usp42.
DR eggNOG; KOG1865; Eukaryota.
DR GeneTree; ENSGT00940000154596; -.
DR HOGENOM; CLU_005541_1_0_1; -.
DR InParanoid; D3ZU96; -.
DR OMA; HVEKKAW; -.
DR OrthoDB; 929408at2759; -.
DR PhylomeDB; D3ZU96; -.
DR TreeFam; TF315281; -.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR PRO; PR:D3ZU96; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Proteomes; UP000234681; Chromosome 12.
DR Bgee; ENSRNOG00000001059; Expressed in testis and 19 other tissues.
DR Genevisible; D3ZU96; RN.
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; ISO:RGD.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Differentiation; Hydrolase; Phosphoprotein; Protease; Reference proteome;
KW Spermatogenesis; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1325
FT /note="Ubiquitin carboxyl-terminal hydrolase 42"
FT /id="PRO_0000404200"
FT DOMAIN 110..411
FT /note="USP"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1219
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1254
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 370
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9J4"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9J4"
FT MOD_RES 858
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9J4"
FT MOD_RES 1190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9J4"
FT MOD_RES 1228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9J4"
SQ SEQUENCE 1325 AA; 146357 MW; EAC3721C860F59EB CRC64;
MTIVDKTEPS DPSTCQNQPG SSEAVSPEDM DTGSASWGAV SSISDVSNHT LSLGPVPGAV
VYNNSSVPEK SKPSPPKDQV LGDGIAPPQK VLFPSEKICL KWQQSHRVGA GLQNLGNTCF
ANAALQCLTY TPPLANYMLS HEHSKTCHAE GFCMMCTMQT HITQALSNPG DVIKPMFVIN
EMRRIARHFR FGNQEDAHEF LQYTVDAMQK ACLNGSNKLD RHTQATTLVC QIFGGYLRSR
VKCLNCKGVS DTFDPYLDIT LEIKAAQSVT KALEQFVKPE QLDGENSYKC SKCKKMVPAS
KRFTIHRSSN VLTISLKRFA NFTGGKIAKD VKYPEYLDIR PYMSQPNGEP IIYVLYAVLV
HTGFNCHAGH YFCYIKASNG LWYQMNDSIV STSDIRSVLN QQAYVLFYIR SHDVKNGGET
THPAHSPGQS SPRPGISQRV VNSKQAAPGF IGPQLPPHVM KNTPHLNGTT PVKDTPSSSV
SSPNGNTSVN RASPATASTS VQNWSVNRPS VIPEHPKKQK ITISIHNKLP VRQGQAQLNN
NLHGPCLEAP SKAAPSSTIT NPSAIQSTSN APTTSVSPSE SCPKPMVNGK AKVGSSVLVP
YGAESSEESD EESKGLAKEN GVDMMTSTQS SRPETADEDG EASPHELQES VMLNGANSAD
SDSRESSLAF DSASCQVQPD LHTENLFNKL NGLPGKVTPA PLQSVPEDKI LETFKLTNQA
KGPAVEESWT TTGGSSPRAS VSQPEPITDE TSPLEIPEAV TNGSMKTPST TSPLEPTISC
TKEDSSVVVV SAEPMEVLPS VPALCNSTGT TLGDAPVPES CDPGDLTANP SQPSQAVKGD
PAENSENSTL AEVVERLSPA PSVLTGDGCE QKLFLYLSTE GSEEAEDSSR SSAVSADTVP
PQPDRTTSSC AGAAEQAAGD RGDGGSVGPK AQEPSPAKEK MNSLRKVDRG HYRSRRDRSS
SGEHVRDSRA RPEDHHHKKR RCYSRERPKQ ERHPANTYCN GGQHLGHGDR ASPERRSLSR
YSHHHSRVRS GLEQDWSRYH HSENEPAWAR ERFYPDKMRW DKCRYYHDRY TTTLYTAREA
AREWRPLHGR EHERLVQSGR PHKDSYWGRK GWDLQSRGKE RPHFHSPREA PGLAVPLERH
LQEKAALSVQ DSSHSLPERF HEHESVKLRK RRYETLDNND DHPEKKVHKS LEKDALEEPR
AKKHKKSKKK KKSKDKHRAR DSRHQQESDF SGAYSDADLH RHRKKKKKKK RHSRKSEDFI
KDVEMHLPKL SSYEAVGHFR RTEGTFLLAD GLPVEDSGPF REKTKHLRME SRPDRCHLSE
YGQGN
