ID G5C252_HETGA Unreviewed; 934 AA.
AC G5C252;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
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};
DE Flags: Fragment;
GN ORFNames=GW7_02648 {ECO:0000313|EMBL:EHB15613.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB15613.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB15613.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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 EMBL; JH172953; EHB15613.1; -; Genomic_DNA.
DR AlphaFoldDB; G5C252; -.
DR STRING; 10181.G5C252; -.
DR MEROPS; C67.001; -.
DR eggNOG; KOG3556; Eukaryota.
DR InParanoid; G5C252; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
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:0006508; P:proteolysis; 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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EHB15613.1};
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 Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT DOMAIN 134..179
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 470..513
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 570..928
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 299..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHB15613.1"
SQ SEQUENCE 934 AA; 104605 MW; CE13C4A4085B5A96 CRC64;
IFYLLLQECS VTDKQTQKLL KVPKGSIGQY IQDRSVGHSR IPSAKGKKNQ IGLKILEQPH
AVLFVDEKDV VEINEKFTEL LLAITNCEER LSLFKNRSRL SKGLQVDVGC PVKVQLRSGE
EKFPGVVRFR GPLLAERTVS GIFFGVELLE EGRGQGFTDG VYQGKQLFQC DEDCGVFVAL
DKLEIIEDDD NGLESDYAGP VDTMQVELPP LEINSRVSLK VGETIESGTV IFCDVLPGKE
SLGYFVGVDM DNPIGNWDGK FDGVQLCSFA SVESTILLHI NDIIPDSMTQ ERRPPKLAFM
SRGVGDKGSS SHNKPKATGS TSDPGNRNRS ELFYTLNGSS VDSQPQSKSK NTWYIDEVAE
DPAKSLTDLS PEFGHSSPPL QPPSMNSLSS ENRFHSLPFS LTKMPNTNSS MAHSPLSLSV
QSVMGELNSA PVQESPPLPV SSGNSHGLEV GSLAEVKENP PFYGVIRWIG QPPGLNEILA
GLELEDECAG CTDGTFRGTR YFTCALKKAL FVKLKSCRPD SRFASLQPVS NQIERCNSLA
FGGYLSEVVE ENTPPKMEKE GLEIMIGKKK GIQGHYNSCY LDSTLFCLFA FSSVLDTVLL
RPKEKNDVEY YSETQELLRT EIVNPLRIYG YVCATKIMKL RKILEKVEAA SGFTSEEKDP
EEFLNILFHH ILRVEPLLKI RSAGQKVQDC YFYQIFMEKN EKVGVPTIQQ LLEWSFINSN
LKFAEAPSCL IIQMPRFGKD FKLFKKIFPS LELNITDLLE DTPRQCRICG GLAMYECREC
YDDPDISAGK IKQFCKTCNT QVHLHPKRLN HKYNPVSLPK DLPDWDWRHG CIPCQKMELF
AVLCIETSHY VAFVKYGKDD SAWLFFDSMA DRDGGQNGFN IPQVTPCPEV GEYLKMSPED
LHSLDSRRIQ GCARRLLCDA YMCMYQSPTM SLYK
//
