UBP37_CANLF
ID UBP37_CANLF Reviewed; 981 AA.
AC E2RK09; F1PGV7;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 37;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q86T82};
DE AltName: Full=Deubiquitinating enzyme 37;
DE AltName: Full=Ubiquitin thioesterase 37;
DE AltName: Full=Ubiquitin-specific-processing protease 37;
GN Name=USP37;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
CC -!- FUNCTION: Deubiquitinase that antagonizes the anaphase-promoting
CC complex (APC/C) during G1/S transition by mediating deubiquitination of
CC cyclin-A (CCNA1 and CCNA2), thereby promoting S phase entry.
CC Specifically mediates deubiquitination of 'Lys-11'-linked polyubiquitin
CC chains, a specific ubiquitin-linkage type mediated by the APC/C
CC complex. Also mediates deubiquitination of 'Lys-48'-linked
CC polyubiquitin chains in vitro. Phosphorylation at Ser-628 during G1/S
CC phase maximizes the deubiquitinase activity, leading to prevent
CC degradation of cyclin-A (CCNA1 and CCNA2). Plays an important role in
CC the regulation of DNA replication by stabilizing the licensing factor
CC CDT1. {ECO:0000250|UniProtKB:Q86T82}.
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:0000250|UniProtKB:Q86T82};
CC -!- SUBUNIT: Interacts with FZR1/CDH1. Interacts with CDT1.
CC {ECO:0000250|UniProtKB:Q86T82}.
CC -!- DOMAIN: The KEN box 3 is required for interaction with FZR1/CDH1 and is
CC essential for APC(CDH1)-mediated ubiquitination.
CC {ECO:0000250|UniProtKB:Q86T82}.
CC -!- PTM: Polyubiquitinated via 'Lys-11'-linked ubiquitin by the APC(CDH1)
CC complex during late mitosis, leading to its degradation. Able to
CC mediate auto-deubiquitination. {ECO:0000250|UniProtKB:Q86T82}.
CC -!- PTM: Phosphorylated at Ser-630 by CDK2 during G1/S phase but not during
CC mitosis; phosphorylation at Ser-630 is required for deubiquitinase
CC activity. Also polyubiquitinated during early G1 phase, without leading
CC to degradation. {ECO:0000250|UniProtKB:Q86T82}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR RefSeq; NP_001300791.1; NM_001313862.1.
DR RefSeq; XP_013966369.1; XM_014110894.1.
DR RefSeq; XP_013966370.1; XM_014110895.1.
DR RefSeq; XP_013966371.1; XM_014110896.1.
DR RefSeq; XP_545643.2; XM_545643.5.
DR AlphaFoldDB; E2RK09; -.
DR SMR; E2RK09; -.
DR STRING; 9615.ENSCAFP00000021817; -.
DR MEROPS; C19.053; -.
DR PaxDb; E2RK09; -.
DR Ensembl; ENSCAFT00030042622; ENSCAFP00030037185; ENSCAFG00030023150.
DR Ensembl; ENSCAFT00040043401; ENSCAFP00040037861; ENSCAFG00040023347.
DR Ensembl; ENSCAFT00845048558; ENSCAFP00845038091; ENSCAFG00845027522.
DR GeneID; 488523; -.
DR KEGG; cfa:488523; -.
DR CTD; 57695; -.
DR VEuPathDB; HostDB:ENSCAFG00845027522; -.
DR eggNOG; KOG1868; Eukaryota.
DR GeneTree; ENSGT00940000158091; -.
DR HOGENOM; CLU_012557_0_0_1; -.
DR InParanoid; E2RK09; -.
DR OMA; NRVNISA; -.
DR OrthoDB; 129045at2759; -.
DR Reactome; R-CFA-5689880; Ub-specific processing proteases.
DR Proteomes; UP000002254; Chromosome 37.
DR Bgee; ENSCAFG00000014781; Expressed in jejunum and 49 other tissues.
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:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; 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:0006275; P:regulation of DNA replication; 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; 4.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50330; UIM; 3.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Hydrolase; Mitosis; Phosphoprotein; Protease;
KW Reference proteome; Repeat; Thiol protease; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..981
FT /note="Ubiquitin carboxyl-terminal hydrolase 37"
FT /id="PRO_0000412645"
FT DOMAIN 343..953
FT /note="USP"
FT DOMAIN 706..725
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 808..827
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 830..849
FT /note="UIM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 111..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 32..34
FT /note="KEN box 1"
FT /evidence="ECO:0000250"
FT MOTIF 71..79
FT /note="D-box 1"
FT /evidence="ECO:0000250"
FT MOTIF 96..105
FT /note="D-box 2"
FT /evidence="ECO:0000250"
FT MOTIF 160..168
FT /note="D-box 3"
FT /evidence="ECO:0000250"
FT MOTIF 223..225
FT /note="KEN box 2"
FT /evidence="ECO:0000250"
FT MOTIF 784..786
FT /note="KEN box 3"
FT /evidence="ECO:0000250"
FT COMPBIAS 119..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 352
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q86T82,
FT ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-
FT ProRule:PRU10093"
FT ACT_SITE 908
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86T82"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86T82"
FT MOD_RES 630
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000250|UniProtKB:Q86T82"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86T82"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86T82"
FT MOD_RES 772
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86T82"
SQ SEQUENCE 981 AA; 110453 MW; EBF79BF01F784AE5 CRC64;
MSPLKIHGPI RIRSMQTGIT KWKEGSFEIV EKENKVSLVV HYNTGGIPRI FQLSHNIKNV
VLRPSGAKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD AVHQNRLHAA MKPSQGSGSF
GAILGSRTSQ KETNRQLSYS DNQASSKRGS LETKDDIPFR KVLGNPGRGS IKTATGSGIT
VTRTIPSLTS ASTPLRSGLL ENRTEKRKRM LSSGSELNED YPKENDSSSN NKAMTDPSRK
YLTSSREKQL SLKQSEENRT SGLLPLQSSS FYGSRTGSKD YSSGSTNLDR TNVSGQTPSA
KRSLGFLPQP APLSVKKLRC NQDYTGWNKP RVPLSSHQQQ QLQGFSNLGN TCYMNAILQS
LFSLQSFAND LLKQGIPWKK IPLNALIRRF AHLLVKKDIC NSETKKDLLK KVKNAISATA
ERFSGYMQND AHEFLSQCLD QLKEDMEKLN KTWKTEPVPG EENSPDISAT RVYTCPVITN
LEFEVQHSII CKACGEIIPK REQFNDLSID LPRRKKPLPP RSIQDSLDLF FRAEELEYSC
EKCGGKCALV RHKFNRLPRI LILHLKRYSF NVTLSLNNKI GQQVIIPRYL TLSSHCTENT
KPPFTLGWSA HMAISRPLKA SQMVNSCITS PSTPSKNFTF KSKSSLALCL DSDSEDELKR
SVALSQRLCE MSGCEQQQDD LEKDSKPCRI EPDKSELENS GFDGMSEEEL LAAVLEMSKR
EASPTLSHED DDKPTSSPDT GFAEDDIQEM PENQDPVETE KPKTVTEPDP ASFTEITKDC
DENKENKTPE GSQGEVDWLQ QYDMEREREE QELQQALAQS LQEQEAWEQK EDDDLKRATE
LSLQEFNNSF LDSLGSDEDS GNEDVLDMEY TEAEAEELKR NAETGNLPHS YRLISVVSHI
GSTSSSGHYI SDVYDIKKQA WFTYNDLEVS KIQEASVQSD RDRSGYIFFY MHKEIFDELL
ETEKNSQALS MEVGKTTRQA L
