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Database: UniProt
Entry: A0A0J7KWP2_LASNI
LinkDB: A0A0J7KWP2_LASNI
Original site: A0A0J7KWP2_LASNI 
ID   A0A0J7KWP2_LASNI        Unreviewed;       828 AA.
AC   A0A0J7KWP2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=RF55_4871 {ECO:0000313|EMBL:KMQ94947.1};
OS   Lasius niger (Black garden ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Lasius; Lasius.
OX   NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ94947.1, ECO:0000313|Proteomes:UP000036403};
RN   [1] {ECO:0000313|EMBL:KMQ94947.1, ECO:0000313|Proteomes:UP000036403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole {ECO:0000313|EMBL:KMQ94947.1};
RA   Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT   "Lasius niger genome sequencing.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMQ94947.1}.
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DR   EMBL; LBMM01002347; KMQ94947.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J7KWP2; -.
DR   STRING; 67767.A0A0J7KWP2; -.
DR   PaxDb; 67767-A0A0J7KWP2; -.
DR   OrthoDB; 5397179at2759; -.
DR   Proteomes; UP000036403; Unassembled WGS sequence.
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; 2.
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:SF3; CYLINDROMATOSIS, ISOFORM D; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM01052; CAP_GLY; 2.
DR   SUPFAM; SSF74924; Cap-Gly domain; 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 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   Hydrolase {ECO:0000313|EMBL:KMQ94947.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036403};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          467..822
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
SQ   SEQUENCE   828 AA;  94636 MW;  B8D44F411D8B7BC2 CRC64;
     MEDRDGSKEH RVLQHYIAKQ DTVLIRIYGA CVVNVNELRV GMLVEALEDL KESVLKVRVI
     DTIGGSKIWC GTEWRCHKYD LIPVSPKIWQ YLLTVQSPQE RIRIANDEAL CERIRNISVN
     DRVLYCSDSS NRRAKEIALV RYIGSVKQLG LGHYFGLELL ESQEVSKTSV LAKEYFISTH
     SNANVTFATV NNIYPYKAES DTISGNIEKT FLKSNTGTDY TNDKKRSVHL LDSTPAVLLE
     QFTLFDDNKN NNQESVNILK ERHQAAKSNL ENNVNNYTKS NDHSLFKCAE LQNIPIFVLE
     HKWSSDIESN VYSDVEDARS IDLLDYSNAL EKNEIEKFKV ENKGDLMVGS TVKVLLDSDI
     HYGVIRWIGT PSGISPGKLM AAVELDDGHP LGTDGTYKDV KYFHCRPYRA IFTDIEHCSH
     YENTKLNEQP ALTNNDNFGN MESSVIAGLV RPISVKGDLE SICGKYRGIQ GHHNSCYLDA
     TLFSMFTFTS VFDNLLFRPP NEKDCPQYEE VQRVLREEIV NPLRKNMFVR ADRVMKLRTL
     LEKLSSVSGL TSEEKDPEEF LTSLVAQILN AEPFLKLSSG QDAYHYQLFV EKDDHLNLPT
     VQQLLEQSFL TSNIRLKEVP SCLIIQMPRF GKSFKMYQKI QPTLLLDVTD IIEDSPRQCT
     VCGKLAEFEC KECYGQCGVG LESIAFCLQC LEKVHRHERR FNHEPKKLIV PMEFAILQEH
     CPVPRLYLEL SAVVCIETSH YVSFVKCGPG SEAPWCFFDS MADRKGEQNG YNIPEMVPCP
     DFPYWLSEEG GNYLIELTDD RHLPEHAKRL LCDAYMCMYQ SPDVMMYK
//
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