ID A0A3Q1ECA9_9TELE Unreviewed; 2625 AA.
AC A0A3Q1ECA9;
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};
GN Name=USP34 {ECO:0000313|Ensembl:ENSAPOP00000001128.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000001128.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000001128.1}
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 -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR STRING; 80966.ENSAPOP00000001128; -.
DR Ensembl; ENSAPOT00000015693.1; ENSAPOP00000001128.1; ENSAPOG00000002447.1.
DR GeneTree; ENSGT00940000158659; -.
DR InParanoid; A0A3Q1ECA9; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021905; DUF3517.
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; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF948; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 34; 1.
DR Pfam; PF12030; DUF3517; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000257200}.
FT DOMAIN 1271..1615
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 52..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2625 AA; 301550 MW; 0CD510DA918D16B6 CRC64;
MTVCSFRVPV QLKHCSRGGA KPKVLPFSPE TSGVMVTAAS ASLEGRMRML DACSASSSAR
PEGTESQQQP PDISPSQMVQ GPQEPSCLPR PGDFLGDAMG SELFNCRRFI GPQHHHHHHH
HHHHHEGPMV EDMLSADDVS CSSSQVSAKS EKNMADFDGE ESGCEEELVQ INSHAELSSH
LQQHLPNLAS IYHEHLVQGP AVHKHQYSSS HAVTDINLDN VCKKGNTLLW DLVQDEDAIH
LSEGLINEAE KLLCSLVCWF TDRQIRMRFI EGCLDNLAHH RSVVVSLRLL PKLFGTFQQF
GSSYDTHWIT MWAEKELHMM KLFFDNLQHY IQEVREHRHK FALYSHSAEV QVRLQFLTCV
FSTLGSPDHF RLSLEQVDIL WHCLVEDAEC YDDALHWFLN QVRSKDQHAM GMETYKHLFL
EKMPQLKPET ISMTGLNLFQ HLCNLARLAT SALDNASSCE LCGMDQLWGI ALRAQSADIS
RAAIQYINSY YINDYLHFLS SKQEFLKKKP KPFHLTMDFY PSNLEKDSHS SLTSIERGLL
MLKTHLEAFR RRFAYHLRQW QIEGTGISSH LKALSDKQSL PLRIVCQPAG LPDKMTIEMY
PSDQVADLRA EVTHWYENLQ KEQMNQQAQL QEFGQSSRQT GDFPGGLMGP VRMISSGHEL
TTDYDEKTLH ELGFKDMQMV FVSLGAPRRE RKGEGVQLPA SCLPPPQKEH IPMLLLLQEP
HLTTLFDLLE MLACFKPPSP NTEKRCVDDL YTSARCEELH LHAENLSRRV WELLMLLPTC
PKMLQAFQNI SDDANGDGLC WKELLRIKSP HKLLYALEII EALGKPNRRI HRESTGSYSD
LYPDSDDSSE DQIENSKNTW SCKFVSSGGL QLLLEIFNSG ILEPKDQESW TVWLLDCLAC
LLKLICQFAV DPADLDLAYH DVFSWSGLAD SQRKRAWPGK SRKSTVEHGK GLHIPRLTEV
FLSLVQGTNL IQRLINVAYT YDNLAHRVLK AQSDHRSRHE VTHYSMWLLV SWAHCSSTVK
SSLADSDHLH DWLKKLTLLV PEPAVRHEAC NGLYKLSLSG LEGGESINRS FLLLAASTLL
KFLPDAQALK PLRVEDYEEE PLLRTGCKEY FWLLCKLIDN IHVKDASQTT LLDLDALARH
LADCIRSREI LDQQDGTIED DGLTGLLRLA TSVLKHKPPF KFSREGQEFL RDVHNLLFLL
PSLADRAQPK CKSHAARAAA YDLLVETVKG SVENYRLLHN WVMSQHMQAS HAPYKWDYWP
HDDVRAECRF VGLTNLGATC YLASTIQQLY MIPEARQAVF TAKYAEDIKH KTTLLELQKM
FTYLMESERK AYNPRPFCKT YTMDKQPLNT GEQKDMTEFF TDLITKIEEM SQDLKNTVKT
LFGGVITNNV VSLDCDHVSQ TAEEFYTVRC QVADMKNIYE SLDEVTIKDT LEGDNMYTCS
QCGKKVRAEK RACFKKLPRI LSFNTMRYTF NMVTMMKEKV NTHFSFPLRL DMTPYTEDFL
MGKGERKEGF REEGETKITE SYEYDLIGVT VHTGTADGGH YYSFIRDIVN PHAYKNNKWY
LFNDAEVKPF DSAQLASECF GGEMTTKTYD SVTDKFMDFS FEKTHSAYML FYKRVELEEE
NGKDFNFDVS PDLLEWIWHD NMQFLQDKNI FEHTYFGFMW QLCSSIPSTL PDPKAVSLMT
AKLSTSFVLE TFIHSKEKPT MLQWIELLTK QFNNSQAACE WFLDRMADDN WWPMQILIKC
PNQIVRQMFQ RLCIHVIQRL RPVHAHLYLQ PGMEDGSDDM DGPVEDIGSR SCVTRFVKTL
LSIMEHGVKP HSKHLTEYFA FLYEFAKMGE EESQFLLSLQ AISIMVHFYM GTKGPENPQV
EVLSEEEGEE EDEEEDILSL AEEKYRPAAL EKMIALIALL VEQSRSERHL TLSQSDMAAL
TGGKGFPFLF QHIRDGINIR QTCNLIFSLC RYNNRLAEHI VSMLFTSIAK LTPEAANPFF
KLLTMLMEFA GGPPGMPSFA SYILQRIWEV IEYNPSQCLD WLAVQTPRNK LAHSWVLQNM
ENWVERFLLA HNYPRVRTSA AYLLVSLIPS NSFRQMFRST RSLHLPTREL PLSPDTTVVL
HQVYNLLLGL LGRAKLYVDA SVHGTTKLVQ YFSFMTYCLI SKTEKLMFSG YFMDLWNLFQ
PKLSEPAIAT NHNKQALLSF WYNVCVDCPE NVRLVVQNPV VTKNIAFNYI LADHDDQEVV
LFNRGMLPAY YGILRMCCEQ SPAFTRQLAS HQNIQWAFKN LTPHASQYPG AVEELFNLMQ
LFVAQRADMR EEEVEDVKQF KKTTISCYLR CLDGRSCWTT LISAFRVLLE NDEDRLLVVF
NRGLILMTES FNTLHMMYHE ATACHVTGDL VELLSIFLSV LKATRPYLQR KDVKQALIQW
QERIDFAHKL LTLLNSYSPP ELRNACLDVL KELVLLSPHD FLHTLVPFLQ HNHCTYHHSN
IPMSFGPYLP CRENIKLMGA KNNIRPPRPE LNMCLLPSLV ESSKGKDEVY DRMLLDYFLS
YHQFIHLLCR VAINCEKFTD TLVKLSVLIA YEGLPLHLPL FPKLWTELCQ SQSVLAKTCV
KLLCEDPAFS EYIKCILMDE RTFLNNNAAY SFLTCFLHKV QLWEA
//
