UBP42_BOVIN
ID UBP42_BOVIN Reviewed; 1333 AA.
AC E1B9W9;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 60.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
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; AAFC03050082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1B9W9; -.
DR SMR; E1B9W9; -.
DR STRING; 9913.ENSBTAP00000000967; -.
DR PaxDb; E1B9W9; -.
DR PRIDE; E1B9W9; -.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_005541_1_0_1; -.
DR InParanoid; E1B9W9; -.
DR TreeFam; TF315281; -.
DR Proteomes; UP000009136; Unplaced.
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; IBA:GO_Central.
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 3: Inferred from homology;
KW Differentiation; Hydrolase; Phosphoprotein; Protease; Reference proteome;
KW Spermatogenesis; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1333
FT /note="Ubiquitin carboxyl-terminal hydrolase 42"
FT /id="PRO_0000404198"
FT DOMAIN 111..412
FT /note="USP"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..935
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..981
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1041
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1218
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1254
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 120
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 371
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9J4"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9J4"
FT MOD_RES 863
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:0000250|UniProtKB:B2RQC2"
FT MOD_RES 1231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RQC2"
FT MOD_RES 1235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9J4"
FT MOD_RES 1256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9J4"
SQ SEQUENCE 1333 AA; 146748 MW; 8E638010675EA919 CRC64;
MTIVDKASES SDPSTYQNQP GSSEAVSPGD MDAGSASWGA VSSLNDVSNH TLSLGPVPGA
VVYSSSSVPE KSKPSPQKDQ ALGDGIAPPQ KVLFPSEKIC LKWQQTHRVG AGLQNLGNTC
FANAALQCLT YTPPLANYML SHEHSKTCHA EGFCMMCTMQ AHITQALSNP GDVIKPMFVI
NEMRRIARHF RFGNQEDAHE FLQYTVDAMQ KACLNGSNKL DRHTQATTLV CQIFGGYLRS
RVKCLNCKGV SDTFDPYLDI TLEIKAAQSV NKALEQFVKP EQLDGENSYK CSKCKKMVPA
SKRFTIHRSS NVLTLSLKRF ANFTGGKIAK DVKYPEYLDI RPYMSQPNGE PIIYVLYAVL
VHTGFNCHAG HYFCYIKASN GLWYQMNDSI VSTSDIRSVL SQQAYVLFYI RSHDVKNGGE
LTHSAHSPGQ SSPRPVISQR VVNSKQAASG FIGPQLPSHM MKNPPHLNGT GPLKETPSSP
MSGPSGNSSV SRTGPVSASP SVQNWSVNRP SVIPEHPKKQ KITISIHNKL PVRQGQSQSN
LHSNSLEHPN KPAPSSTITT SSAIQSTSSA PTPPASSKVP KQMAPREACS RPMMNGRPRL
SAGVLVPYGA ESSEESDEEA KGLGQENGRG LTESACSPAL DAEDGDASPH ELQEPVALNG
ATGLDSDPTE NGLPSDGAPC PGQPALHSEH PFPKANGLPG KLMPAPLPPL PEDKILETFK
LGSKAKGSAE ETRTPGSEER PLEHPEAELE AGRSPPGDAR DNLESVSNLS SKFKKASPPS
DPSIKPTKEE VSERVSAEPE EAVPSASTFC NPDKDALGDD QLLAPCDPGN LTDDQSKPSP
DVGGTLPERP QDPVAAEAAG RLSPGPSVPS EGDHEPEPLG HSGRDRGSDA EGPSKSMGVS
TDEAPSAQLD TITENRPEGP PERSSSERGE DSKAGQKAPE PCLVQEKVSS LRKVDRGHYR
SRRDRSSSGE HARESRSRTE VQHRRKRPHR EHERPRPERP RPEPCALAPQ PPCPSSLARS
GHHHSRSRGA PDQEWGRYHH AEGDHAWTRE KYYPDRLRWE RCRYHHDRSP LYPSREPRDW
RPFHAEREYE RAGPYGGRPY KDHYRGRKGY ELVAKERDRH RFSSPRAGMA HAPPPHPAAK
YTHDRLSFGA EDGSCDLAAR FHEHDNIKSR KRRYDSLENE SHVEKKAWRS LQKDPVEEPK
VKKHKKSKKK KKSKDKHRDR DSRHQQDSDL SVAHSDADLH RHKKKKKKKK RHSRKSEDFG
RDSEPRLPKA ASCETVDHFR KAEGAFPLAD GLPLEGAAPF CEKTKHFRME SREVRCRLSQ
CDQGKGARWE SGS
