ID H2ZX11_LATCH Unreviewed; 969 AA.
AC H2ZX11;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=USP35 {ECO:0000313|Ensembl:ENSLACP00000001932.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000001932.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000001932.1}
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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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 EMBL; AFYH01022435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01022436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01022437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01022438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01022439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01022440; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01022441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01022442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01022443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2ZX11; -.
DR STRING; 7897.ENSLACP00000001932; -.
DR Ensembl; ENSLACT00000001946.1; ENSLACP00000001932.1; ENSLACG00000001725.1.
DR eggNOG; KOG1864; Eukaryota.
DR GeneTree; ENSGT00940000160942; -.
DR HOGENOM; CLU_010910_0_0_1; -.
DR InParanoid; H2ZX11; -.
DR OMA; RCKKLCD; -.
DR TreeFam; TF324529; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd02664; Peptidase_C19H; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR033840; USP38.
DR InterPro; IPR049407; Usp38-like_N.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF660; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 35; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF21246; Usp38-like_N; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 443..872
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 619..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 969 AA; 109000 MW; 9C2088F9BC3A5209 CRC64;
MDKILEAVLV SPYSNAVKHG LIRRVLEAAK EPLDRQQCWS MLEVATKLFL LGDTKLKRDT
GKEVFEAYAH HHPKEFEEFF SVRFILNLLQ EGYGTLGTKS LKIIEYLHLG LQYLLQGSSA
DEVFSLLQTE VLRMVCERPG PKFCAGLAKL LSQNPQCIPT GKQLTLFCQQ LVRSIGQFQC
LSEAEDDIME FLDHVIKVSG LLQKIWRAQT SSILPSLKEL FTIISTTGQE TPSNALASVV
QFVPVELMDG VIKNLTNDDS ISDAQMMTAI NRFSSQVSWL KNYIAGLLHT VLRKLIKVLR
LSVSAEIKLT LCLQVFSKLY YPIVREGTLS VLKYMLLSFQ HSPDAFHMLL PHIPKMVAAL
CKEDPKSGRS CLEQLAELIH CMIFRFSGFP DLYEPLMEAI KDLPVPNEER VKQLLGQNAW
TSQKNELAPF YPRLAAKSNT GRIGLVNLGN TCYMNSVLQA LFMASDFRQA VMYLKESDSQ
PLMMKLQRLF AFLEHSQRPA ISPDNFLAAS WPPWFSPGAQ QDCSEYLKYL LDRLHEEEKT
GRRINLKLRR SNSGPYIEEY QDFGKTLIEK MFGGKLMTNT CCLCCHNISL REEAFTDLSL
AFPPPQKAAV RYGGSTSPAL PIEEIGPKST HSPLKSQNRM CRSPKRQRSP LKSEQPYVHI
VPIEILGSHG KVETERPTFS RQYTEELEDH DGIEDAKNSA IASGEQTHAA DGSRSVPDLI
NFFLSPEMLT GDNKYYCEMC ASLQDAEKVV EVSEAPCYLI LTLLRFSFDL KVMKRRKIID
NVYVPLVLKL PVRVSVYDLC SVVVHSGISS ESGHYYCYAR EGLGTNESQA DSGSQWYLFN
DTRVSFSSFE SVSNVTSYLP KDTAYVLFYR QRTSQRGTAG PQHTSGAVKQ YGEPPLSKEI
MEAISKDNIQ YLQEQEREAR NRATYIPALS RSPMWWRGFG DDDDNEGSSG SCGPAAGGGG
SGSFSRLVF
//
