UBP37_CHICK
ID UBP37_CHICK Reviewed; 986 AA.
AC E1C213; E1BU11;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 51.
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;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
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; AADN02016788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02016789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1C213; -.
DR SMR; E1C213; -.
DR STRING; 9031.ENSGALP00000037410; -.
DR PaxDb; E1C213; -.
DR VEuPathDB; HostDB:geneid_424216; -.
DR eggNOG; KOG1868; Eukaryota.
DR InParanoid; E1C213; -.
DR OrthoDB; 129045at2759; -.
DR PhylomeDB; E1C213; -.
DR Proteomes; UP000000539; Unplaced.
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: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: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; 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; Protease;
KW Reference proteome; Repeat; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..986
FT /note="Ubiquitin carboxyl-terminal hydrolase 37"
FT /id="PRO_0000412647"
FT DOMAIN 344..958
FT /note="USP"
FT DOMAIN 712..731
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 813..832
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 835..854
FT /note="UIM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 134..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..840
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 224..226
FT /note="KEN box 2"
FT /evidence="ECO:0000250"
FT MOTIF 789..791
FT /note="KEN box 3"
FT /evidence="ECO:0000250"
FT COMPBIAS 168..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 353
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 913
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 986 AA; 110863 MW; A1780CFB799F5970 CRC64;
MAPLKVHGPV RMRSMQTGIT KWKEGSFEIV EKDNKVSLVV HYNVGGIPKT FQLSHNIKSV
TLRPNGRKLC CLMLTLKDTS FLTIDKVPLK DANEMRMYLD AVHQDRVHTA GKPSQGSGSF
GGVLGSRTTQ KEANRQFSYI ENQAPPKRVT VESKDETPFR KVLGTPARAS VKNSSGTGAP
SNRVNVAASP TSSVPHRTGL LESRSEKRKR AQPPSSEMSE DYPKENDSST NNTAMSDPAW
KYLNSSREKQ LKLKQEEENR TSGVLPLQSS SYYGSRSSSK EYSTSSSTLD RSSVSSQTTS
AKRSLGFLSQ PAPLSVKKMR SNQDYTGWNK PRVPLSTHPQ QQLQGFSNLG NTCYMNAILQ
SLFSIQSFAN DLLKQGIPWK KIPLNALIRR FAHLLAKKDV SSPEVKKELL KKVKSAISAT
AERFSGYMQN DAHEFLSQCL DQLKEDMEKL NKTWKSEPVP NDDSSPGRAS DDLSATKVYT
CPVISNLEFE VQHSIICKTC GETVTKREQF NDLSIDLPRR KKLFPSRSIQ DSLDLFFRAE
EIEYSCEKCN GKSAVVTHKF NRLPRVLILH LKRYSFNVAL SLNHKVGQQV VIPRYLTLLS
HCTESTRLPL TLGWSAHSAI SRPLKASQMV NSCTISTSTP CRKGRFLRKE GLSELRSSTG
RKNLNRVHVF KEDVQDINSS LQVQRGIRKS SKRSKMEGDK PELGNAGFDG MSEDELLAAV
LEISKREASL SLSHDEDKPT SSPDTGFGDD EIQELPENLE TMETEKPKAP LESGPANFTE
ITKDFDENKE NKTPEGSQGE VDWLQQYDME REREEQELQQ ALAQSLQEQE AREQKEDDDL
KRATELSLQE FNSSLLDSVG SDEDSGNEDV LDMEYSEAEA EELKRNAETG ELPHSYRLIS
IVSHIGSTSS SGHYISDVYD IKKQSWFTYN DLEVSRTLET TVQCDRDRSG YIFFYMHKDI
FDELLETEKN AQPLSMEVGR SIRQPL
