ID G7Q141_MACFA Unreviewed; 957 AA.
AC G7Q141;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 ORFNames=EGM_11727 {ECO:0000313|EMBL:EHH60379.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000313|EMBL:EHH60379.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH60379.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(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; CM001295; EHH60379.1; -; Genomic_DNA.
DR AlphaFoldDB; G7Q141; -.
DR MEROPS; C67.001; -.
DR eggNOG; KOG3556; Eukaryota.
DR Proteomes; UP000009130; Chromosome 20.
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 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 492..535
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 592..951
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 321..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 107338 MW; 59097EA317B8E436 CRC64;
MSSGLWSQEK VTSPYWEERI FYLLLQECSV TDKQTQKLLK VPKGSIGQYI QDRSVGHSRI
PSAKGKKNQI GLKILEQPHA VLFVDEKDVA EINEKFTELL LAITNCEERF SLFKNRNRLS
KGLQIDVGCP VKVQLRSGEE KFPGVVRFRG PLLAERTVSG IFFGVELLEE GRGQGFTDGV
YQGKQLFQCD EDCGVFVALD KLELIEDDDT ALESDYAGPV DTMQVELPPL EINSRVSLKV
GETIESGTVI FCDVLPGKES LGYFVGVDMD NPIGNWDGRF DGVQLCSFAC VESTILLHIN
DIIPGMFSSV SQERRPPKLA FMSRGVGDKG SSSHNKPKAT GSTSDPGNRN RSELFYTLNG
SSVDSQPQSK SKNTWYIDEV AEDPAKSLTE ISTDFDRSSP PLQPPPVNSL STENRFHSLP
FSLTKMPNTN GSIGHSPLSL SAQSVMEELN TAPVQESPPL AMPPGNSHGL EVGSLAEVKE
NPPFYGVIRW IGQPPGLNEV LAGLELEDEC AGCTDGTFRG TRYFTCALKK ALFVKLKSCR
PDSRFASLQP VSNQIERCNS LAFGGYLSEV VEENTPPKME KEGLEIMIGK KKGIQGHYNS
CYLDSTLFCL FAFSSVLDTV LLRPKEKNDV EYYSETQELL RTEIVNPLRI YGYVCATKIM
KLRKILEKVE AASGFTSEEK DPEEFLNILF HHILRVEPLL KIRNCAEKVN KCHFTQAYYP
NISKCSVSFP PSLRDKMSIN SFIFAKEQAP SCLIIQMPRF GKDFKLFKKI FPSLELNITD
LLEDTPRQCR ICGGLAMYEC RECYDDPDIS AGKIKQFCKT CNTQVHLHPK RLNHKYNPVS
LPKDLPDWDW RHGCIPCQKM ELFAVLCIET SHYVAFVKYG KDDSAWLFFD SMADRDGGQN
GFNIPQVTPC PEVGEYLKMS LEDLHSLDSR RIQGCARRLL CDAYMCMYQS PTMSLYK
//
