ID Q6NXV6_MOUSE Unreviewed; 961 AA.
AC Q6NXV6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 122.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
DE Flags: Fragment;
GN Name=Usp4 {ECO:0000313|EMBL:AAH66865.1, ECO:0000313|MGI:MGI:98905};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH66865.1};
RN [1] {ECO:0000313|EMBL:AAH66865.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:AAH66865.1};
RC TISSUE=Blastocyst {ECO:0000313|EMBL:AAH66180.1}, and Embryo
RC {ECO:0000313|EMBL:AAH66865.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC from specific proteins to regulate different cellular processes.
CC {ECO:0000256|RuleBase:RU366025}.
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 ECO:0000256|RuleBase:RU366025};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP4 subfamily.
CC {ECO:0000256|ARBA:ARBA00037971}.
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DR EMBL; BC066180; AAH66180.1; -; mRNA.
DR EMBL; BC066865; AAH66865.1; -; mRNA.
DR AlphaFoldDB; Q6NXV6; -.
DR MEROPS; C19.010; -.
DR PeptideAtlas; Q6NXV6; -.
DR AGR; MGI:98905; -.
DR MGI; MGI:98905; Usp4.
DR ChiTaRS; Usp4; mouse.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028135; Ub_USP-typ.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF45; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 4; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 1.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 10..121
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 301..921
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 219..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAH66865.1"
SQ SEQUENCE 961 AA; 108171 MW; 39FD7C6C4775BEBC CRC64;
AEGRGSRERP DVETQKTELG ALMGTTLQRG AQWYLIDSRW FKQWKKYVGF DSWDMYNVGE
HNLFPGPIDN SGLFSDPESQ TLKEHLIDEL DYVLVPAEAW NKLLNWYGCV EGQQPIVRKV
VEHGLFVKHC KVEVYLLELK LCENSDPTNV LSCHFSKADT IATIEKEMRR LFNIPTERET
RLWNKYMSNT YEQLSKLDNT IQDAGLYQGQ VLVIEPQNED GTWPRQSLQS KSSTAPSRNF
TTSSKPSASP YCSVSASLIA NGDSTNSSGM HSSGVSRGGS GFSASYNCQE PPSPHIQPGL
CGLGNLGNTC FMNSALQCLS NTAPLTEYFL KDEYEAEINR DNPLGMKGEI AEAYAELIKQ
MWSGRDTHVA PRMFKTQVGR FAPQFSGYQQ QDSQELLAFI LDGLHEDLNR VKKKPYLEPK
DANGRPDAVV AKEAWENHRL RNDSVIVDTF HGLFKSTLVC PECAKVSVTF DPFCYLTLPL
PLKKDRIMEV FLVPADPQCR PIQYRVTVPL MGAISDLCEA LSKLSGIAAE NMVVTDVYNH
RFHKIFQMDE GLSHITPRDD IFVYEVCNTS MDGSECITLP VYFREKKSRP SSASSGAVLY
GQPLLVSVPK HKLTLESLYQ AVCDRISRYI KQPLPDEFLS SPLEPGACNG SRSSYEGDEE
EEMDHQEEGK EQLSEVEGSG EDDQGDDHSE SAQKVKGQPR HKRLFTFSLV NSCGTADINS
LATDGKLLKL NSRSTLAIDW DSETRSLYFD EQESEACEKH LSMSQPQKKK KAAVALRECI
ELFTTMETLG EHDPWYCPTC KKHQQATKKF DLWSLPKILV VHLKRFSYNR YWRDKLDTVV
EFPVGALNMS EFVCDRSARP YVYDLIAVSN HYGAMGVGHY TAYAKNRLNG KWYYFDDSSV
SLASEDQIVT KAAYVLFYQR RDDECSSTSS LGSFPGSDGG VKLSSSHQGM GDEEAYNMDT
N
//