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   27-MAR-2024, entry version 68.
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.ENSDARP00000110966; -.
DR   MEROPS; C19.046; -.
DR   PaxDb; 7955-ENSDARP00000108006; -.
DR   PeptideAtlas; E7F6T8; -.
DR   GeneID; 768201; -.
DR   KEGG; dre:768201; -.
DR   AGR; ZFIN:ZDB-GENE-061013-802; -.
DR   CTD; 57695; -.
DR   ZFIN; ZDB-GENE-061013-802; usp37.
DR   eggNOG; KOG1868; Eukaryota.
DR   InParanoid; E7F6T8; -.
DR   OrthoDB; 227085at2759; -.
DR   PhylomeDB; E7F6T8; -.
DR   Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR   PRO; PR:E7F6T8; -.
DR   Proteomes; UP000000437; Chromosome 9.
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:0035871; P:protein K11-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02257; Peptidase_C19; 1.
DR   CDD; cd13312; PH_USP37_like; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 2.30.29.180; Ubiquitin carboxyl-terminal hydrolase 26/29/37, pleckstrin homology-like domain; 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   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF733; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE-RELATED; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF16674; UCH_N; 1.
DR   Pfam; PF02809; UIM; 3.
DR   SMART; SM00726; UIM; 3.
DR   SUPFAM; SSF54001; Cysteine proteinases; 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
//