ID A0A3B1JJT3_ASTMX Unreviewed; 953 AA.
AC A0A3B1JJT3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:ENSAMXP00000042598.1};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000042598.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000042598.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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}.
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DR STRING; 7994.ENSAMXP00000033073; -.
DR Ensembl; ENSAMXT00000052765.1; ENSAMXP00000033073.1; ENSAMXG00000018616.2.
DR Ensembl; ENSAMXT00000053301.1; ENSAMXP00000042598.1; ENSAMXG00000018616.2.
DR GeneTree; ENSGT00390000018123; -.
DR OrthoDB; 5397179at2759; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000018616; Expressed in brain and 14 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: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:Ensembl.
DR GO; GO:0021551; P:central nervous system morphogenesis; IEA:Ensembl.
DR GO; GO:1904888; P:cranial skeletal system development; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT DOMAIN 156..194
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 499..532
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 589..947
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 307..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 106791 MW; B07ED8A96EBBC674 CRC64;
MSSALWSQEK PAGGFRDDWR FYIVVKECVV EKPPQKTLRI PRGSLGQACQ ERNSLGRPLP
PSKGKRSLRI LDQTNVVVSV DERDVLELDE KLAELLFPIT NCEERYGLLC NKPRLDRARE
IDCGSKVRVQ LRSGDEPLPG VVRFKGALLP DRALSGIWFG VELLEEGRGQ GFTEGSYQGQ
QLFRCEDECG VFVALDKLEL WEDEELEVDH VTLVDNDPEV EGEFPPLEVN SRVLVQTREG
PERGTVIFCD LLPGNETLGY YVGVDMDNPI GDWDGVIDGK LLCNFASLEH TRLVPICDVM
PEYSMQDPRL SKPSFTSRGS CEKPGGQGKP KNKGVGLQAA SRSKSEFYYT LNGSSVDHPA
QSKSKSTWYI DEVGEDPAKS LTETPPDFNQ ASPPPRAPPT AVSLSSDNKF HSLPFSLNRK
SGPNGSMSHG PLSLSVQSVM GEQQEIPPPV TAPSPRPSSP PKGQPGLEVG SLVEVKENPP
LCGVIRWVGL PPGLLEPLAG LELEEECVGC TDGTFKGTRY FTCPPKKALF VKLKCCRPDS
RFPSQHHSPN PIERCNSIAF GGYLSEVVNE NTPPRTENDG LEVMVGKKKG IQGHYNSCYL
DSTLFCLFSF SSVLDTVLLR PKSKTDVEYY LETQELLRTE IVNPLRIHGY VCATKIMKLR
RILEKVEAAS GFTSEEKDPE EFLNILFHHI LRVDPLLKLR SAGQKVQDCY FYQIFMDKKD
KVLVPTSQQL LEWSFINSDL KFAEAPSCLI IQMPRFGKDF KMFNKIFPSL ELDITDLLED
TPRECRICGG LALYECRECY EDADITAGKI KQFCEKCNTQ VHLHPRRKTH RYGKLSVPKE
LQEGVWRQGS FPHQQMELFA VLCIETSHYV AFVKYGAADS AWLFFDSMAD RDGGQNGFNI
PQVSPCPEVG AYLKMTPEEL HALDPKNIQG YARRLLCDAY MCMYQSPTMS LYK
//
