UBP37_DANRE
ID UBP37_DANRE Reviewed; 937 AA.
AC E7F6T8; A1L1F9; E7FBK6; F1QUQ3; Q08BR8;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 37;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 37;
DE AltName: Full=Ubiquitin thioesterase 37;
DE AltName: Full=Ubiquitin-specific-processing protease 37;
GN Name=usp37; ORFNames=zgc:152882, zgc:153999;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deubiquitinase that antagonizes the anaphase-promoting
CC complex (APC/C) during G1/S transition by mediating deubiquitination of
CC APC/C target proteins, thereby promoting S phase entry. Specifically
CC mediates deubiquitination of 'Lys-11'-linked polyubiquitin chains, a
CC specific ubiquitin-linkage type mediated by the APC/C complex (By
CC similarity). {ECO:0000250}.
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;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; CT583711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC124596; AAI24597.1; -; mRNA.
DR EMBL; BC129040; AAI29041.1; -; mRNA.
DR RefSeq; NP_001070811.1; NM_001077343.1.
DR AlphaFoldDB; E7F6T8; -.
DR SMR; E7F6T8; -.
DR STRING; 7955.ENSDARP00000108006; -.
DR MEROPS; C19.046; -.
DR PaxDb; E7F6T8; -.
DR PeptideAtlas; E7F6T8; -.
DR GeneID; 768201; -.
DR KEGG; dre:768201; -.
DR CTD; 57695; -.
DR ZFIN; ZDB-GENE-061013-802; usp37.
DR eggNOG; KOG1868; Eukaryota.
DR InParanoid; E7F6T8; -.
DR OrthoDB; 129045at2759; -.
DR PhylomeDB; E7F6T8; -.
DR Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR PRO; PR:E7F6T8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0021551; P:central nervous system morphogenesis; IMP:ZFIN.
DR GO; GO:1904888; P:cranial skeletal system development; IMP:ZFIN.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0035871; P:protein K11-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd13312; PH_USP37_like; 1.
DR Gene3D; 2.30.29.180; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR032069; USP37-like_PH.
DR InterPro; IPR038093; USP37-like_PH_sf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF16674; UCH_N; 1.
DR Pfam; PF02809; UIM; 3.
DR SMART; SM00726; UIM; 3.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50330; UIM; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Hydrolase; Mitosis; Protease;
KW Reference proteome; Repeat; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..937
FT /note="Ubiquitin carboxyl-terminal hydrolase 37"
FT /id="PRO_0000412648"
FT DOMAIN 322..911
FT /note="USP"
FT DOMAIN 672..691
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 766..785
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 788..807
FT /note="UIM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 132..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 38..40
FT /note="KEN box 1"
FT /evidence="ECO:0000250"
FT MOTIF 76..84
FT /note="D-box 1"
FT /evidence="ECO:0000250"
FT MOTIF 101..110
FT /note="D-box 2"
FT /evidence="ECO:0000250"
FT MOTIF 162..170
FT /note="D-box 3"
FT /evidence="ECO:0000250"
FT MOTIF 204..206
FT /note="KEN box 2"
FT /evidence="ECO:0000250"
FT MOTIF 742..744
FT /note="KEN box 3"
FT /evidence="ECO:0000250"
FT COMPBIAS 132..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 331
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 866
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT CONFLICT 79
FT /note="L -> Q (in Ref. 2; AAI24597)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="T -> N (in Ref. 2; AAI24597/AAI29041)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="S -> N (in Ref. 2; AAI24597/AAI29041)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="L -> F (in Ref. 2; AAI24597/AAI29041)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="T -> M (in Ref. 2; AAI24597/AAI29041)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="A -> V (in Ref. 2; AAI24597/AAI29041)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="R -> K (in Ref. 2; AAI24597/AAI29041)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="E -> V (in Ref. 2; AAI24597)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="E -> EQ (in Ref. 2; AAI24597)"
FT /evidence="ECO:0000305"
FT CONFLICT 654..656
FT /note="LQQ -> HHH (in Ref. 2; AAI29041/AAI24597)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="L -> P (in Ref. 2; AAI24597)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 937 AA; 105264 MW; 6B483279C5C4EB83 CRC64;
MAAAVPRLTS GGAVRIRIRC GELGTTKWRE GVIEIQERDN KINLLVKFNS GGAPRVFQLS
HNVKSVSWFQ THGPNRMTLT LKDSCIVMMD KLNMLVAKKM KEYLETVKLG KPAVFKTNQG
SASFGLVLGN RTAQNDSGLS PSDKQSAPRR SSLDSREDST PRKPLGSPSR VTSTPARGSL
SEIRSEKRKR LMNSDGDLTE DYPKENDSSS NNKAITDSSR KFLLSCKDKL KQSEENRASA
PHTPAPLQPT SFYGSRTGAK DYTQTHSFLD RPSSTGSCPS AKRSLVLPNH STPFKKVRPT
LDYGGWNKPR PSVLAQPQPP LQGFSNLGNT CYMNAILQSL FSLPSFSNDL LKQGIPWKRV
PINALLRRFA HLLAKKDISP PEVKKDLLRR VKNAISSTAE RFSGYMQNDA HEFLSQCLDQ
LKEDVEKINK SWKNEPSAWD EPQSTRLADE VDTSRIYTCP VTVNMEFEVQ HTITCKSCGE
VVLKREQFND LSIDLPRRRK TLPMRSIQDS LDLFFRMEEI EYSCEKCSGK AATVSHKFSR
LPRVLILHLK RYSYNTQLSL NSKLGQQVLI PKYLTLLSHC TDATRSPLSL GWSAQNALSR
TLKISQSVNS STLRRASQRP ESSGSVLCDS DSDEELVRKV ARKHHPDDDR ADELQQHHPH
AAVEQSEFNG INDEEMLAAV LEMSRHDTSL CAGPDEEPSS SPDTGFGDAD AHDLTQHLEL
LDAEKQPTDA LESLDLTMDE NKENQTPDGL QGELDWVQQY SLEQEREEQE LQQALAQSLQ
EQEAREMRED DDLKRATELS LQEFNNSLPE LLCSDEDSGN EDGLDMEYSE AEAEELKKNA
ETGELPNSFR LISVVSHIGS SSSSGHYISD VYDMKKQSWL TYNDLDVSRT QESTVQRDRD
RSGYIFFYMH KDVFEELSEL EKAGVNTDGG RTVLQPL
