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Database: UniProt
Entry: D4A251_RAT
LinkDB: D4A251_RAT
Original site: D4A251_RAT 
ID   D4A251_RAT              Unreviewed;       714 AA.
AC   D4A251;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 2.
DT   05-JUN-2019, entry version 85.
DE   RecName: Full=Ubiquitinyl hydrolase 1 {ECO:0000256|SAAS:SAAS01044305};
DE            EC=3.4.19.12 {ECO:0000256|SAAS:SAAS01044305};
GN   Name=Usp44 {ECO:0000313|Ensembl:ENSRNOP00000007465};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000007465, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000007465, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000007465,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000007465}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000007465};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide,
CC         peptide and isopeptide bonds formed by the C-terminal Gly of
CC         ubiquitin (a 76-residue protein attached to proteins as an
CC         intracellular targeting signal).; EC=3.4.19.12;
CC         Evidence={ECO:0000256|SAAS:SAAS01117307};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|SAAS:SAAS01045498}.
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DR   EMBL; AABR07056654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 10116.ENSRNOP00000007465; -.
DR   MEROPS; C19.057; -.
DR   PaxDb; D4A251; -.
DR   PRIDE; D4A251; -.
DR   Ensembl; ENSRNOT00000007465; ENSRNOP00000007465; ENSRNOG00000005637.
DR   UCSC; RGD:1308216; rat.
DR   RGD; 1308216; Usp44.
DR   eggNOG; KOG1867; Eukaryota.
DR   eggNOG; ENOG410XQQ0; LUCA.
DR   GeneTree; ENSGT00940000160526; -.
DR   OMA; KIGVHVG; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000005637; Expressed in 6 organ(s), highest expression level in testis.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007059; P:chromosome segregation; IEA:Ensembl.
DR   GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:Ensembl.
DR   GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; IEA:Ensembl.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002494};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01044238};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01044152};
KW   Protease {ECO:0000256|SAAS:SAAS01044292};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Thiol protease {ECO:0000256|SAAS:SAAS01044269};
KW   Ubl conjugation pathway {ECO:0000256|SAAS:SAAS01044331};
KW   Zinc {ECO:0000256|SAAS:SAAS01044373};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS01044352}.
FT   DOMAIN       24     85       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      271    679       USP. {ECO:0000259|PROSITE:PS50235}.
FT   ZN_FING      24     85       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
FT   REGION      225    250       Disordered. {ECO:0000256|MobiDB-lite:
FT                                D4A251}.
FT   REGION      345    364       Disordered. {ECO:0000256|MobiDB-lite:
FT                                D4A251}.
FT   REGION      687    714       Disordered. {ECO:0000256|MobiDB-lite:
FT                                D4A251}.
FT   COILED      172    203       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    225    239       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                D4A251}.
SQ   SEQUENCE   714 AA;  80440 MW;  B1A01676EF16BB91 CRC64;
     MDRCKHIEQL QLAQGHSILN PQKWFCMVCN TTESIWACLS CSHVACGQYI QEHALKHFEE
     SSHPVAFEVN DMYVFCYLCN DYVLNDNTAG DLKSLRSTLS AIKGKSYPCV VQSDSVLQPV
     NAQADSYSLH DSTQSLPGSE DPMCTALWHR RRALMGKTFR TWFEQSPIGR KRQEQTQEKT
     VAKREVKRRQ QELEQQMKAE LECTPPRKSL RLQGLSEAAT VEILPVQAPP PPPASPAKEK
     ALALPPSEDG KLKRVSDSLI KRRPAVTPGV TGLRNLGNTC YMNSVLQVLS HLLIFRQCFL
     KLDLNQWLAV AASDKARSYK HSAVTDAATA AAHQLNEGQE KEKGFACSRH PGLSSGLSGG
     ASKGRNMELI QPREPSSPYS SLCHELHTLF QVMWSGEWAL VSPFAMLHSV WKLIPAFRGY
     AQQDAQEFLC ELLDKIQREL ETTGTKLPAL IPTSQRRLIE QVLNVVNNIF HGQLLSQVTC
     LACNNKSNTI EPFWDLSLEF PERYQCSGKD AASQPCLVTD MLGKFTETEA LEGKIYVCDH
     CNSKRRKFSS KPVVLTEAQK QLMICHLPQV LRLHLKRFRW SGRNNREKIG VHVVFEETLN
     MEPYCCSETL NALRPECFIY NLSAVVIHHG KGFGSGHYTA YCYNSEGGFW VHCNDSKLSM
     CTMEEVLRAQ AYILFYTQRV TENGHSRLLP PELLSNSQQH PSEETDTSSN EVLS
//
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