ID H0ZB11_TAEGU Unreviewed; 953 AA.
AC H0ZB11;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 75.
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:ENSTGUP00000007768.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000007768.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000007768.2}
RP IDENTIFICATION.
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};
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; H0ZB11; -.
DR STRING; 59729.ENSTGUP00000007768; -.
DR Ensembl; ENSTGUT00000007850.2; ENSTGUP00000007768.2; ENSTGUG00000007517.2.
DR GeneTree; ENSGT00390000018123; -.
DR HOGENOM; CLU_003910_0_0_1; -.
DR InParanoid; H0ZB11; -.
DR OMA; SPWYIDE; -.
DR OrthoDB; 5397179at2759; -.
DR TreeFam; TF318734; -.
DR Proteomes; UP000007754; Unplaced.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0097542; C:ciliary tip; IEA:Ensembl.
DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:Ensembl.
DR GO; GO:1990380; F:K48-linked deubiquitinase activity; IEA:Ensembl.
DR GO; GO:0061578; F:K63-linked deubiquitinase activity; IEA:Ensembl.
DR GO; GO:0070064; F:proline-rich region binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0043369; P:CD4-positive or CD8-positive, alpha-beta T cell lineage commitment; IEA:Ensembl.
DR GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:2000493; P:negative regulation of interleukin-18-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:1901223; P:negative regulation of non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; IEA:Ensembl.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:1903829; P:positive regulation of protein localization; IEA:Ensembl.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IEA:Ensembl.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045577; P:regulation of B cell differentiation; IEA:Ensembl.
DR GO; GO:1902017; P:regulation of cilium assembly; IEA:Ensembl.
DR GO; GO:2001242; P:regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0060544; P:regulation of necroptotic process; IEA:Ensembl.
DR GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:1901026; P:ripoptosome assembly involved in necroptotic process; IEA:Ensembl.
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; 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:UP000007754};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT DOMAIN 161..199
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 309..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 106989 MW; C2D03B5F77044230 CRC64;
MNSGLWSQEK ASSSYWEERI FYLLLQECSV IDKQTQKLLK VPKGSIGQFF QDRSSVAHSR
NIPCKGKKLQ IGLKILEQPH AVLFVDEKDV IEINEKLAEL LLAITNCEER YSLFKSKSRL
AKGVQIDIGS PVRVQLRSGD EKYPGVVRFR GPLMQERSLT GIYFGVELLE EGRGQGFTDG
QYQGKQLFRC DEDCGVFVAL DKLELVEDDD NELESDYAAP VDAMQVELPP LEINSRVSLK
IGESIEYGTV IFCDVLPGNE SLGYVVGVDM DNPIGNWDGR YNGIQLCSFA SVESTLLLHI
NDVIPETVSQ DRRPPKLAYT SRSGDKGLFN HSKPKAIGST SEPGNRSRSE VFYTLNGSSV
DSQPQTKTKS PWYIDEAAED PSKSLTDSSP GFGHSSPPLQ PPLTNSVSTE NRFHSLPFSL
TKTTSTNGTI GHSPLSLSVQ SVMGDVNTTA TQESPSTASP IGNSHGLEAG SLAEVKENPP
FYGVIRWIGQ PPGVNEVLAG LELEDECAGC TDGTFKGTRY FTCAPKKALF VKLKSCRPDS
RFASLQPVSN QIERCNSLAF GGYLSEVVEE NTPPKMEKEG LETMIGKKKG IQGHYNSCYL
DSTLFCLFSF SSVLDTVLLR PKEMNDVEYY SETQELLRTE IVNPLRIYGY VCATKIMKLR
KILEKVEAAS GFTSEEKDPE EFLNILFHHI LRVEPLLKIR SAGQKVQDCY FYQIFMDKNE
KVGVPTIQQL LEWSFINSNL KFAEAPSCLI IQMPRFGKDF KMFNKIFPSL ELNITDLLED
TPRQCRICRG LAMYECRECY EDTDISAGKI KQFCKTCNTQ VHLHPKRQSH KFNPLSLPKD
LPDWDWRHGC IPSQKMELFA VLCIETSHYV AFVKYGRDDS AWLFFDSMAD RDGGQNGFNI
PQVTPCPEVG EYLKMSLEEL HSLDSRKIQG CARRLLCDAY MCMYQSPTMS LYK
//
