ID A0A5F9CB59_RABIT Unreviewed; 910 AA. AC A0A5F9CB59; DT 11-DEC-2019, integrated into UniProtKB/TrEMBL. DT 11-DEC-2019, sequence version 1. DT 25-MAY-2022, entry version 9. DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase CYLD {ECO:0000256|ARBA:ARBA00018699}; 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}; 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, ECO:0000313|Proteomes:UP000001811}; RN [1] {ECO:0000313|Ensembl:ENSOCUP00000031143, 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} RP IDENTIFICATION. RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000031143}; RG Ensembl; RL Submitted (OCT-2019) to UniProtKB. 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 --------------------------------------------------------------------------- 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 Ensembl; ENSOCUT00000055744; ENSOCUP00000031143; ENSOCUG00000012853. DR GeneTree; ENSGT00390000018123; -. DR Proteomes; UP000001811; Unplaced. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell. 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:thiol-dependent deubiquitinase; IEA:InterPro. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 2.30.30.190; -; 3. 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 Pfam; PF01302; CAP_GLY; 2. DR Pfam; PF00443; UCH; 1. DR SMART; SM01052; CAP_GLY; 3. DR SUPFAM; SSF54001; SSF54001; 1. DR SUPFAM; SSF74924; SSF74924; 3. 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 4: Predicted; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Cell projection {ECO:0000256|ARBA:ARBA00023273}; 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 Protease {ECO:0000256|ARBA:ARBA00022670}; KW Reference proteome {ECO:0000313|Proteomes:UP000001811}; 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 //