ID   CYLD_BOVIN              Reviewed;         953 AA.
AC   Q1RMU2;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase CYLD;
DE            EC=3.1.2.15;
DE   AltName: Full=Ubiquitin thioesterase CYLD;
DE   AltName: Full=Ubiquitin-specific-processing protease CYLD;
DE   AltName: Full=Deubiquitinating enzyme CYLD;
GN   Name=CYLD; Synonyms=CYLD1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Negative regulator of TRAF2 and NF-kappa-B signaling
CC       pathway. Has deubiquitinating activity that is directed towards
CC       non-'Lys-48'-linked polyubiquitin chains. The inhibition of NF-
CC       kappa-B activation is mediated at least in part, by the
CC       deubiquitination and inactivation of TRAF2 and, to a lesser
CC       extent, TRAF6 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Ubiquitin C-terminal thioester + H(2)O =
CC       ubiquitin + a thiol.
CC   -!- SUBUNIT: Interacts with NEMO, TRAF2 and TRIP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C67 family.
CC   -!- SIMILARITY: Contains 2 CAP-Gly domains.
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DR   EMBL; BC114710; AAI14711.1; -; mRNA.
DR   IPI; IPI00686064; -.
DR   RefSeq; NP_001039882.1; -.
DR   UniGene; Bt.58637; -.
DR   SMR; Q1RMU2; 125-206, 228-306, 454-547.
DR   MEROPS; C67.001; -.
DR   Ensembl; ENSBTAG00000006291; Bos taurus.
DR   GeneID; 536421; -.
DR   KEGG; bta:536421; -.
DR   HOVERGEN; Q1RMU2; -.
DR   OMA; Q1RMU2; GVQLCSF.
DR   BRENDA; 3.1.2.15; 251.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:InterPro.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR000938; Cytoskel-assoc-prot_CAP-Gly.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   InterPro; IPR001593; Ribosomal_S3Ae.
DR   PANTHER; PTHR11830; Ribosomal_S3AE; 1.
DR   Pfam; PF01302; CAP_GLY; 3.
DR   Pfam; PF00443; UCH; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 2.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; FALSE_NEG.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Phosphoprotein; Protease; Repeat;
KW   Thiol protease; Ubl conjugation pathway.
FT   CHAIN         1    953       Probable ubiquitin carboxyl-terminal
FT                                hydrolase CYLD.
FT                                /FTId=PRO_0000326147.
FT   DOMAIN      153    198       CAP-Gly 1.
FT   DOMAIN      489    532       CAP-Gly 2.
FT   REGION      106    590       Interaction with TRIP (By similarity).
FT   REGION      391    466       Interaction with TRAF2 (By similarity).
FT   REGION      467    681       Interaction with NEMO (By similarity).
FT   ACT_SITE    598    598       By similarity.
FT   ACT_SITE    868    868       By similarity.
FT   MOD_RES     396    396       Phosphoserine (By similarity).
SQ   SEQUENCE   953 AA;  106805 MW;  F478EBCB7D52863E CRC64;
     MSSGLWSQEK VTSPYWEERI FYLLLQECSV TDKQTQKLLK VPKGSIGQNI QDRSVGLSRI
     PSAKGKKNQI GLKILEQPHA VLFVDEKDVV EINEKFTELL LAITNCEERF SLFKNRNRLS
     KGLQIDVGCP VKVQLRSGEE KFPGVVRFRG PLLAERTVSG IFFGVELLEE GRGQGFTDGV
     YQGKQLFQCD EDCGVFVALD KLELIEDDDT GLESDYAGPV DTMQVELPPL EINSRVSLKL
     GETIESGTVI FCDVLPGKES LGYFVGVDMD NPIGNWDGRF DGVQLCSFAS VESTILLHIN
     DIIPESVTQE RRPPKLAFMS RGVGDKGSFS HNKPKATGST SDPGTRNRSE LFYTLNGSSV
     DSQPQSKSKN SWYIDEVAED PAKSLTEIPP DFGHASPPLQ PPSMNSLSSE NRFHSLPFSL
     TKMPNTNGSI SHSPLSLSVQ SVMGELNNAP VQESPPLAVS SGNSHGLEVG SLAEVKENPP
     FYGVIRWIGQ PPGLNEVLAG LELEDECAGC TDGTFRGTRY FTCALKKALF VKLKSCRPDS
     RFASLQPVSN QIERCNSLAF GGYLSEVVEE NTPPKMEKEG FEIMIGKKKG IQGHYNSCYL
     DSTLFCLFAF SSVLDTVLLR PKEKNDVEYY SETQELLRTE IVNPLRIYGY VCATKIMKLR
     KILEKVEAAS GFTSEEKDPE EFLNILFHHI LRVEPLLKIR SAGQKVQDCY FYQIFMEKNE
     KVGVPTIQQL LECSFINSNL KFAEAPSCLI IQMPRFGKDF KLFKKIFPSL ELNITDLLED
     TPRQCRICGG LAMYECRECY DDPDISAGKI KQFCKTCNAQ VHLHPKRLNH KYNPVSLPKD
     LPDWDWRHGC IPCQKMELFA VLCIETSHYV AFVKYGKDDS AWLFFDSMAD RDGGQNGFNI
     PQVTPCPEVG EYLKMSLDDL HSLDSRRIQG CARRLLCDAY MCMYQSPTMS LYK
//