ID A0A226NMX1_CALSU Unreviewed; 919 AA.
AC A0A226NMX1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=ASZ78_009589 {ECO:0000313|EMBL:OXB69113.1};
OS Callipepla squamata (Scaled quail).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC Callipepla.
OX NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB69113.1, ECO:0000313|Proteomes:UP000198323};
RN [1] {ECO:0000313|EMBL:OXB69113.1, ECO:0000313|Proteomes:UP000198323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texas {ECO:0000313|EMBL:OXB69113.1,
RC ECO:0000313|Proteomes:UP000198323};
RC TISSUE=Leg muscle {ECO:0000313|EMBL:OXB69113.1};
RA Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA Decker J.E., Seabury C.M.;
RT "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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,
CC ECO:0000256|RuleBase:RU366025};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP20/USP33 subfamily.
CC {ECO:0000256|ARBA:ARBA00008269}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXB69113.1}.
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DR EMBL; MCFN01000004; OXB69113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226NMX1; -.
DR STRING; 9009.A0A226NMX1; -.
DR Proteomes; UP000198323; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF13; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 20; 1.
DR Pfam; PF06337; DUSP; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00695; DUSP; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51283; DUSP; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000198323};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 1..91
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 149..681
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 640..738
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 747..897
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT REGION 258..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 919 AA; 102601 MW; F517EBC987D55082 CRC64;
MGDTRDICPH LDSIGEVTRD DLLLKSKIGC PYVGCGESFA DHSTLHAQAK KHNLTVNLTT
FRVWCYACEK EVFLDQRLAA HAQSPSVKFS EAVGVCPSLA GLNAWQAFPF LVANDSPLPA
HPLKAVPIAV ADEGESESED DDLKPRGLTG MKNLGNSCYM NAALQALSNC PPLTQFFLEC
GGLVRTDKKP ALCKSYQKLV SEVWHKKRPS YVVPSSLSHG IKLVNPMFRG YAQQDTQEFL
RCLMDQLHEE LKEPIVAETR DLDIGDQDDK HEGDRSPSED EFLSCDSSSD RGEGDGQSRT
TGSMAETELL IQDEGGRGIS EKERMKDRKF SCGHRRSNSE QVDEDADVDT TMMPVDGRAS
PEMLPAPCPA SPCRTPAEPD NDAYVRCSSR PCSPVHHEMH SKLSSSPPRS SPARLGPSYV
LKKAQMQASG KKKKELRYRS VISDIFDGSI LSLVQCLTCD RVSTTVETFQ DLSLPIPGKE
DLAKLHSAIY QSVPAKTGAC GDNYASQGWI AFIMEYIRRF VVSCIPSWFW GPVVTLEDCL
AAFFAADELK GDNMYSCERC KKLRNGVKYC KVLRLPEILC IHLKRFRHEV MYSFKINSHV
SFPLEGLDLR PFLAKECVSQ ITTYDLLSVI CHHGTAGSGH YIAYCQNVIN GQWYEFDDHM
KEHSLLQFYI SREWLNKFNT FAEPGPITNH TFLCSHGGIP PNKYHYIDDL VVILPQNVWE
YLYNRFGGGP AVNHLYVCSI CQVEIEALAK RRRIEIDTFI KLNKAFQAEE SPSVIYCISM
QWFREWEAFV KGKDNGKKPE ITGDGPLGGV EIMRISMGSE LNWVGWQRGK HSGSERVCFA
LAEPPGPIDN SKIALTKAGG HVQVKQGADY GQISEETWIY LSTLYGGGPE IAIRQNVAQV
QEMENLHGEQ KIEAETRAV
//
