ID A0A5F9CB59_RABIT Unreviewed; 910 AA. AC A0A5F9CB59; DT 11-DEC-2019, integrated into UniProtKB/TrEMBL. DT 11-DEC-2019, sequence version 1. DT 29-MAY-2024, entry version 19. 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:ENSOCUP00000031143.1}; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000031143.1, ECO:0000313|Proteomes:UP000001811}; RN [1] {ECO:0000313|Ensembl:ENSOCUP00000031143.1, ECO:0000313|Proteomes:UP000001811} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S., RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B., RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J., RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M., RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M., RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D., RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J., RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S., RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A., RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R., RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R., RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C., RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E., RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N., RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSOCUP00000031143.1} RP IDENTIFICATION. RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000031143.1}; RG Ensembl; RL Submitted (FEB-2024) 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; A0A5F9CB59; -. DR Ensembl; ENSOCUT00000055744.1; ENSOCUP00000031143.1; ENSOCUG00000012853.4. DR GeneTree; ENSGT00390000018123; -. DR Proteomes; UP000001811; Unplaced. DR Bgee; ENSOCUG00000012853; Expressed in blood and 17 other cell types or tissues. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:0061578; F:K63-linked deubiquitinase activity; IEA:TreeGrafter. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0070266; P:necroptotic process; IEA:TreeGrafter. DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:TreeGrafter. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:2001242; P:regulation of intrinsic apoptotic signaling pathway; IEA:TreeGrafter. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IEA:TreeGrafter. 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801}; 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:UP000001811}; 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 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..910 FT /note="USP" FT /evidence="ECO:0000259|PROSITE:PS50235" FT REGION 310..350 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 385..410 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" FT COMPBIAS 389..410 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 910 AA; 101782 MW; 8FBC94B89D771A65 CRC64; MSSGLWSQEK VTSPYWEERI FYLLLQECSV TDKQTQKLLK VPKGSIGQYI QDRSVGHARM PSAKGKKNQI GLKILEQPHA VLFVDEKDVV EINEKFTELL LAITNCEERF SLFKNRSRLS KGLQITVGCP VKVQLRSGEE KFPGVVRFRG PLLAERTVSG IFFGVELLEE GRGQGFTDGL YQGKQLFQCD EDCGVFVALD KLEIIEDDDN GLESDYAGPV DNMQVELPPL EINSRVSLKV GETIESGTVI FCDVLPGKES LGYFVGVDMD NPIGNWDGRF DGVQLCSFAS VESTILLHIN DIIPDSVTQE RRPPKLAFMS RGVGDKGSSS HSKPKATGST SDPGNRNRSE LFYTLNGSSV DSQPQSKSKN TWYIDEVAED PAKSLTELSP DYGHSSPPLQ PPSVNSLSSE NRFHSLPFSL TKMPNTNGSI GHSPLSLSVQ SVMGELNNAP VQESPPLPMS SSNSHGLEVG 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 IPCQKMELFA VLCIETSHYV AFVKYGKDDS AWLFFDSMAD RDATSSVPAS RVFCSGPLST //