ID A0A2K5CZF0_AOTNA Unreviewed; 953 AA.
AC A0A2K5CZF0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase CYLD {ECO:0000256|ARBA:ARBA00018699};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Deubiquitinating enzyme CYLD {ECO:0000256|ARBA:ARBA00030882};
DE AltName: Full=Ubiquitin thioesterase CYLD {ECO:0000256|ARBA:ARBA00031094};
DE AltName: Full=Ubiquitin-specific-processing protease CYLD {ECO:0000256|ARBA:ARBA00032487};
GN Name=CYLD {ECO:0000313|Ensembl:ENSANAP00000014077.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000014077.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000014077.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000256|ARBA:ARBA00004186}. Cytoplasm, perinuclear region
CC {ECO:0000256|ARBA:ARBA00004556}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR AlphaFoldDB; A0A2K5CZF0; -.
DR Ensembl; ENSANAT00000031908.1; ENSANAP00000014077.1; ENSANAG00000024887.1.
DR GeneTree; ENSGT00390000018123; -.
DR OrthoDB; 5397179at2759; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd02670; Peptidase_C19N; 1.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 3.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
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; PTHR11830; 40S RIBOSOMAL PROTEIN S3A; 1.
DR PANTHER; PTHR11830:SF15; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE CYLD; 1.
DR Pfam; PF01302; CAP_GLY; 2.
DR Pfam; PF16607; CYLD_phos_site; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM01052; CAP_GLY; 3.
DR SUPFAM; SSF74924; Cap-Gly domain; 3.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT DOMAIN 153..198
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 489..532
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 589..947
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 313..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 106982 MW; 7C6ADC65615E02B5 CRC64;
MSSGLWSQEK VTSPYWEERM FYLLLQECSV TDKQTQKLLK VPKGSIGQYV QDRSVGHSRI
PSAKGKKNQI GLKILEQPHA VLFVDEKDVV EINEKFTELL LAITNCEERV SLFRTKNRLS
KGVQIDVGCP VKVQLRSGEE KFPGVVRFRG PLLAERTVSG IFFGVELLEE GRGQGFTDGV
YQGKQLFQCD EDCGVFVALD KLELIEDDDP ALESDYAGPV DTMQVELPPL EINSRVSLKV
GKTIESGTVI FCDVLPGKES LGYFVGVDMD NPIGNWDGRF DGVQLCSFAC VESTILLHIN
DIIPESVTQE RRPPKLAFMS RGVGDKGSSS HNKPKATGST SDPGNRNRSE LFYTLNGSSV
DSQPQSKSKN TWYIDEVAED PAKSLTEVST DFDRSSPPLQ PPPVNTLSTE NRFHSLPFSL
TKMPNSNGSI GHSPLSLSAQ SVMEELNTAP VQESPPLAMP PGNSHGLEVG SLAEVKENPP
FYGVIRWIGQ PPGLNEVLAG LELEDECAGC TDGTFRGTRY FTCALKKALF VKLKSCRPDS
RFASLQPVSN QIERCNSLAF GGYLSEVVEE NTPPKMEKEG LEIMIGKKKG IQGHYNSCYL
DSTLFCLFAF SSVLDTVLLR PKEKNDVEYY SETQELLRTE IVNPLRIYGY VCATKIMKLR
KILEKVEAAS GFTSEEKDPE EFLNILFHHI LRVEPLLKIR SAGQKVQDCY FYQIFMEKNE
KVGVPTIQQL LEWSFINSNL KFAEAPSCLI IQMPRFGKDF KLFKKIFPSL ELNITDLLED
TPRQCRICGG LAMYECRECY DDPDISAGKI KQFCKTCNTQ VHLHPKRLNH KYNPVSLPKD
LPDWDWRHGC IPCQNMELFA VLCIETSHYV AFVKYGKDDS AWLFFDSMAD RDGGQNGFNI
PQVTPCPEVG EYLKMSLEDL HSLDSRRIQG CARRLLCDAY MCMYQSPTMS LYK
//
