ID E1BCH9_BOVIN Unreviewed; 1223 AA.
AC E1BCH9;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 3.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=VCPIP1 {ECO:0000313|Ensembl:ENSBTAP00000008802.5,
GN ECO:0000313|VGNC:VGNC:53883};
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 {ECO:0000313|Ensembl:ENSBTAP00000008802.5, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000008802.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000008802.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000008802.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000008802.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000707};
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DR AlphaFoldDB; E1BCH9; -.
DR SMR; E1BCH9; -.
DR STRING; 9913.ENSBTAP00000008802; -.
DR PaxDb; 9913-ENSBTAP00000008802; -.
DR Ensembl; ENSBTAT00000008802.5; ENSBTAP00000008802.5; ENSBTAG00000006695.5.
DR VEuPathDB; HostDB:ENSBTAG00000006695; -.
DR VGNC; VGNC:53883; VCPIP1.
DR eggNOG; KOG4345; Eukaryota.
DR GeneTree; ENSGT00390000002854; -.
DR HOGENOM; CLU_009674_0_0_1; -.
DR InParanoid; E1BCH9; -.
DR OMA; DNRLHRC; -.
DR OrthoDB; 5402859at2759; -.
DR TreeFam; TF329469; -.
DR Reactome; R-BTA-5689896; Ovarian tumor domain proteases.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000006695; Expressed in neutrophil and 108 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IBA:GO_Central.
DR GO; GO:0090168; P:Golgi reassembly; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR GO; GO:0106300; P:protein-DNA covalent cross-linking repair; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:1905634; P:regulation of protein localization to chromatin; IEA:Ensembl.
DR CDD; cd22769; OTU_VCIP135; 1.
DR CDD; cd17059; Ubl_OTU1; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR InterPro; IPR048857; OTU1_Ubl.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR039087; VCPIP1.
DR InterPro; IPR045827; VCPIP1_N.
DR PANTHER; PTHR14843; DEUBIQUITINATING PROTEIN VCIP135; 1.
DR PANTHER; PTHR14843:SF2; DEUBIQUITINATING PROTEIN VCPIP1; 1.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF21403; OTU1_UBXL; 1.
DR Pfam; PF19437; VCIP135_N; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50802; OTU; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT DOMAIN 209..362
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1223 AA; 134416 MW; 9AA95CA63F3B8C5C CRC64;
MSQPPPPPPL PPPPPPPEAP QTPPSLAAAA AATPGGLSKR RDRRILSGSC PDPKCQARLF
FPASGSVSIE CTECGQRHEQ QQLLGVEEVT DPDVVLHNLL RNALLGVTGA PKKNTELVKV
MGLSNYHCKL LSPILARYGM DKQTGRAKLL RDMNQGELFD CALLGDRAFL IEPEHVNTVG
YGKDRSGSLL YLHDTLEDIK RANKSQECLI PVHVDGDGHC LVHAVSRALV GRELFWHALR
ENLKQHFQQH LARYQALFHD FIDAAEWEDI INECDPLFVP PEGVPLGLRN IHIFGLANVL
HRPIILLDSL SGMRSSGDYS ATFLPGLIPA EKCTGRDGHL NKPICIAWSS SGRNHYIPLV
GIKGAALPKL PMNLLPKAWG VPQDLIKKYI KLEEDGGCVI GGDRSLQDKY LLRLVAAMEE
VFMDKHGIHP SLVADVHQYF YRRTGVIGVQ PEEVTAAAKK AVMDNRLHKC LLCGALSELH
VPPEWLAPGG KLYNLAKSTH GQLRPDKNYS FPLNNLVCSY DSVRDVLVPD YGLSNLTACN
WCHGTSVRRV RGDGSIVYLD GDRTNSRSTG GKCGCGFKHF WDGKEYDNLP EAFPITLEWG
GRVVRETVYW FQYESDASLN SNVYDVAMKL VTKHFPGEFG SEILVQKVVH TILHQTAKKN
PDDYTPVNID GAHAQRFGDV QGQESESPLP TKIILTGQKA KTLHKEELNM SKTERTIQQN
ITEQASVMQK RKTEKLKQEQ KGQPRTVSPS TVRDGPSSAP ATPTKAPYSP TTSKEKKIRI
TTNDGRQSMV TLKPSTTFFE LQESIAREFN IPPYLQCIRY GFPPKELMPP QAGMEKEPVP
LQHGDRITIE ILKSKAEGGQ SAAAHSAHTM KPEDSAVTGR LSSKELQEQA DKEMYSLCLL
ATLMGEDVWS YAKGLPHMFQ QGGVFYNIMK KTMGMADGKH CTFPHLPGKT FVYNASEDRL
ELCVDAAGHF PIGPDVEDLV KEAVSQVRAE ATTRSRESSP SHGLLKLGSG GVVKKKSEQL
HNVTAFQGKG HSLGTASSTP HLDPRARETP VVRKHTTGTD FSSSSIKTEP SVFTAAPSNS
ELIRIAPGVV TTRDSRQLDP DMVEAQRKKL QEMVSSIQAS MDKHLRDQST EQSPSDPPQR
KVEAVSSSVK SGSLQTGSPE SFSPTGDTEN LNIETADGCV AEALEAAFAE RSEAQKGSSV
EEPEEMDSQD AEMTNTTEPM DHS
//
