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 24-JAN-2024, entry version 65. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAFC03050082; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; E1B9W9; -. DR SMR; E1B9W9; -. DR STRING; 9913.ENSBTAP00000000967; -. DR PaxDb; 9913-ENSBTAP00000000967; -. 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:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central. DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW. DR CDD; cd02661; Peptidase_C19E; 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; IPR018200; USP_CS. DR InterPro; IPR028889; USP_dom. DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1. DR PANTHER; PTHR24006:SF727; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 42; 1. DR Pfam; PF00443; UCH; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 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 //