ID   A0A3Q0RN04_AMPCI        Unreviewed;       935 AA.
AC   A0A3Q0RN04;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000011971.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000011971.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC       perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085}.
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DR   AlphaFoldDB; A0A3Q0RN04; -.
DR   STRING; 61819.ENSACIP00000011971; -.
DR   Ensembl; ENSACIT00000012308.1; ENSACIP00000011971.1; ENSACIG00000009313.1.
DR   GeneTree; ENSGT00390000018123; -.
DR   OMA; YGHLLPI; -.
DR   Proteomes; UP000261340; Unplaced.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
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; IPR028889; USP_dom.
DR   PANTHER; PTHR11830; 40S RIBOSOMAL PROTEIN S3A; 1.
DR   PANTHER; PTHR11830:SF45; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE CYLD-LIKE; 1.
DR   Pfam; PF01302; CAP_GLY; 3.
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; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          453..496
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   DOMAIN          553..897
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          189..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..392
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   935 AA;  103117 MW;  91C3325A835D2287 CRC64;
     MSGAHEQIRK RRPPKTFLIS TDVNLRDQLE GTIPLQRGFI CQEQDPGRRG DNPWVKVLDN
     DFMVKIDRRL LVDVPSDLTG LLEAVSDPEA RLKLLSKKQM LEIFTQLASL PSDSPLWVKI
     GQQDDLAEAE LKYIGPLTRG SSAVYFGVQL KGSAVGKGQS NGTYKGQRLF TCPDACALFV
     PASHIRPRQW SSNSDGHERA RERDSSQLSP FSVLSRTAES APITAHNQVQ GQRVCCHQND
     RVSTGEVAYF GPLPGRGPSG MYVGVILDTP DGNWDGNYNG EKLCHVPSNL YGALLSANKV
     SLETSNFFPS ASSEPKSHHQ NLTHKISKAV LKPALPPVTK SVPISPPASA PKIALMPPIK
     PALKSPPLPP PKPTQKSVLP APLPPPKPQT TPTVATQPQH TNGTHGPASP LRVTDHGDNA
     AENGEAGPGS NLEVGSMVEV NDPPLFGVIR WIGWIKGISE PVAGIELDQE LSAGTDGSYL
     GERHFRCPAN KGLFVKLRNC RRDSRFPAPE MPVNQVERCN SIAFAEWGSE RVEDHTPPIE
     GDEARELYQG WKKGIQGHLN SCYLDATLFS LFSCCSSADC VLFWPTDPET DQSSSQAQDL
     LRCDIVNPLR RYGYVCASKT MALRRLLEAA NSDTGFTNQE KDPEEFLNKL FQLLRVEPLL
     KIRSMSQQPQ ECHLYQLFPP PLPTSPTSPQ SLSPVNSPIP LSSASSMRVA SVQTLLESSF
     LHSGLKFVEA PSCLLLLMPR FGKDFKMFDA ILPTLSLDIT DLLDDTLRQC SICQAVAEWE
     CLQCYDDPDI TPGHLKQYCQ TCNIQVHSHR KRASHSPVQI GVPGGQWTGP LHCTRQRMSL
     FAVTCIETSH YVSFVKHGPL NTDWLFFDSM ADREGGENGF NIPQVKACPE VGRYLSLSEE
     ELSRVDPASL REATRRLLCD SYMCLYHSPE LSLYK
//