ID G3SV11_LOXAF Unreviewed; 1222 AA.
AC G3SV11;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:ENSLAFP00000004040.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000004040.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000004040.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000004040.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000004040.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000004040.3};
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; G3SV11; -.
DR STRING; 9785.ENSLAFP00000004040; -.
DR Ensembl; ENSLAFT00000004824.3; ENSLAFP00000004040.3; ENSLAFG00000004826.3.
DR eggNOG; KOG4345; Eukaryota.
DR GeneTree; ENSGT00390000002854; -.
DR HOGENOM; CLU_009674_0_0_1; -.
DR InParanoid; G3SV11; -.
DR OMA; DNRLHRC; -.
DR TreeFam; TF329469; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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; IEA:UniProtKB-EC.
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:UP000007646}.
FT DOMAIN 208..361
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1222 AA; 134323 MW; 4D26F8BAF519F858 CRC64;
FSPSFPVLSS PPKAPPPEAP QTPPPLAAAA AAPGGLSKRR DRRILSGSCP DPKCQARLFF
PASGSVSIEC TECGQRHEQQ QLLGVEEVTD PDVVLHNLLR NALLGVTGAP KKNTELVKVM
GLSNYHCKLL SPILARYGMD KQTGRAKLLR DMNQGELFDC ALLGDRAFLI EPEHVNTVGY
GKDRSGSLLY LHDTLEDIKR ANKSQECLIP VHVDGDGHCL VHAVSRALVG RELFWHALRE
NLKQHFQQHL AQYQALFHDF IDAAEWEDII NECDPLFVPP EGVPLGLRNI HIFGLANVLH
RPIILLDSLS GMRSSGDYSA TFLPGLIPAE KCTGKDGHLN KPICIAWSSS GRNHYIPLVG
IKGAALPKLP MNLLPKAWGV PQDLIKKYIK LEDDGGCVIG GDRSLQDKYL LRLVAAMEEV
FMDKHGIHPS LVADVHQYFY RRTGVIGVQP EEVTAAAKKA VMDNRLHKCL LCGALSELHV
PPEWLAPGGK LYNLAKSTHG QLRPDKNYSF PLNNLVCSYD SVKDVLVPDY GLSNLTACNW
CHGTSVRRVR GDGSIVYLDG DRTNSRSTGG KCGCGFKHFW DGKEYDNLPE AFPITLEWGG
RVVRETVYWF QYESDSSLNS NVYDVAMKLV TKHFPGEFGS EILVQKVVNT ILHQTAKKNP
DDYTPVNIDG AHAQRVGDVQ GQESEPQLPT KIILTGQKTK TLHKEELNMS KTERTIQQNI
TEQASVMQKR KTEKLKQEQK GQPRTVSPSA IRDGPSSAPA TPTKAPYSPT TSKEKKIRIT
TNDGRQSMVT LKSSTTYFEL QESIAREFNI PPYLQCIRYG FPPKELMPPQ AGMEKEPVPL
QHGDRITIEI LKSKAEGGQS TAAHSAHAVK QEEIAVTSKL SSRELQEQAD KEMYSLCLLA
TLMGEDVWSY AKGLPHMFQQ GGVFYNIMKK TMGMADGKHC TFPHLPGKTF VYNASEDRLE
LCVDAAGHFP IGPDVEDLVK EAVSQVRAEA TTRSRESSPS HGLLKLGSGG VVKKKSEQLH
NVAAFQGKGH SLGTASSNPH LDPRARETPV VRKHSTGKDF SNSSTKTEPS VFTAAPSNSE
LIRIAPGVVT MRDSRQLDPD LVEAQRKKLQ EMVSSIQASM DKHLRDQSTE QSLSDLPQRK
VEVVSSAAKS GTLQTGLPES FSLTGDTENL NTETTDSSVA DALGAAFATR SKAQKGNSVE
EPEEMDSQDA EMTNTAEPMD HS
//
