LOCUS       NP_001001516            1357 aa            linear   ROD 05-JUN-2024
DEFINITION  ubiquitin carboxyl-terminal hydrolase 19 [Rattus norvegicus].
ACCESSION   NP_001001516 XP_341472 XP_341473
VERSION     NP_001001516.1
DBSOURCE    REFSEQ: accession NM_001001516.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1357)
  AUTHORS   Miao,R., Lu,Y., He,X., Liu,X., Chen,Z. and Wang,J.
  TITLE     Ubiquitin-specific protease 19 blunts pathological cardiac
            hypertrophy via inhibition of the TAK1-dependent pathway
  JOURNAL   J Cell Mol Med 24 (18), 10946-10957 (2020)
   PUBMED   32798288
  REMARK    GeneRIF: Ubiquitin-specific protease 19 blunts pathological cardiac
            hypertrophy via inhibition of the TAK1-dependent pathway.
REFERENCE   2  (residues 1 to 1357)
  AUTHORS   Zhang,X., Jiang,Y., Han,W., Liu,A., Xie,X., Han,C., Fan,C.,
            Wang,H., Zhang,H., Ding,S., Shan,Z. and Teng,W.
  TITLE     Effect of Prolonged Iodine Overdose on Type 2 Iodothyronine
            Deiodinase Ubiquitination-Related Enzymes in the Rat Pituitary
  JOURNAL   Biol Trace Elem Res 174 (2), 377-386 (2016)
   PUBMED   27156111
  REMARK    GeneRIF: High iodine intake had no discernible effects on USP20.
            Temporary increases in USP33 and USP19 mRNA levels were observed.
            The enzymes related to D2 ubiquitination change with prolonged high
            iodine intake. Increased D2 ubiquitination suppresses the activity
            of D2, causing a decrease in negative feedback of the
            hypothalamic-pituitary-thyroid axis.
REFERENCE   3  (residues 1 to 1357)
  AUTHORS   Wiles,B., Miao,M., Coyne,E., Larose,L., Cybulsky,A.V. and Wing,S.S.
  TITLE     USP19 deubiquitinating enzyme inhibits muscle cell differentiation
            by suppressing unfolded-protein response signaling
  JOURNAL   Mol Biol Cell 26 (5), 913-923 (2015)
   PUBMED   25568336
  REMARK    GeneRIF: Deubiquitination by USP19 does modulate muscle cell
            differentiation and that this function requires the ER-localized
            isoform and appears to act through regulation of the
            unfolded-protein response (UPR) signaling.
REFERENCE   4  (residues 1 to 1357)
  AUTHORS   Nakamura,N., Harada,K., Kato,M. and Hirose,S.
  TITLE     Ubiquitin-specific protease 19 regulates the stability of the E3
            ubiquitin ligase MARCH6
  JOURNAL   Exp Cell Res 328 (1), 207-216 (2014)
   PUBMED   25088257
REFERENCE   5  (residues 1 to 1357)
  AUTHORS   Lee,J.G., Kim,W., Gygi,S. and Ye,Y.
  TITLE     Characterization of the deubiquitinating activity of USP19 and its
            role in endoplasmic reticulum-associated degradation
  JOURNAL   J Biol Chem 289 (6), 3510-3517 (2014)
   PUBMED   24356957
REFERENCE   6  (residues 1 to 1357)
  AUTHORS   Ogawa,M., Yamaji,R., Higashimura,Y., Harada,N., Ashida,H.,
            Nakano,Y. and Inui,H.
  TITLE     17beta-estradiol represses myogenic differentiation by increasing
            ubiquitin-specific peptidase 19 through estrogen receptor alpha
  JOURNAL   J Biol Chem 286 (48), 41455-41465 (2011)
   PUBMED   21971047
REFERENCE   7  (residues 1 to 1357)
  AUTHORS   Sundaram,P., Pang,Z., Miao,M., Yu,L. and Wing,S.S.
  TITLE     USP19-deubiquitinating enzyme regulates levels of major
            myofibrillar proteins in L6 muscle cells
  JOURNAL   Am J Physiol Endocrinol Metab 297 (6), E1283-E1290 (2009)
   PUBMED   19773579
  REMARK    GeneRIF: USP19 modulates transcription of major myofibrillar
            proteins.
REFERENCE   8  (residues 1 to 1357)
  AUTHORS   Hassink,G.C., Zhao,B., Sompallae,R., Altun,M., Gastaldello,S.,
            Zinin,N.V., Masucci,M.G. and Lindsten,K.
  TITLE     The ER-resident ubiquitin-specific protease 19 participates in the
            UPR and rescues ERAD substrates
  JOURNAL   EMBO Rep 10 (7), 755-761 (2009)
   PUBMED   19465887
REFERENCE   9  (residues 1 to 1357)
  AUTHORS   Lu,Y., Adegoke,O.A., Nepveu,A., Nakayama,K.I., Bedard,N., Cheng,D.,
            Peng,J. and Wing,S.S.
  TITLE     USP19 deubiquitinating enzyme supports cell proliferation by
            stabilizing KPC1, a ubiquitin ligase for p27Kip1
  JOURNAL   Mol Cell Biol 29 (2), 547-558 (2009)
   PUBMED   19015242
  REMARK    GeneRIF: study reports that the USP19 deubiquitinating enzyme
            interacts with and stabilizes KPC1, thereby modulating p27(Kip1)
            levels and cell proliferation
            Erratum:[Mol Cell Biol. 2009 Jun;29(11):3241]
REFERENCE   10 (residues 1 to 1357)
  AUTHORS   Combaret,L., Adegoke,O.A., Bedard,N., Baracos,V., Attaix,D. and
            Wing,S.S.
  TITLE     USP19 is a ubiquitin-specific protease regulated in rat skeletal
            muscle during catabolic states
  JOURNAL   Am J Physiol Endocrinol Metab 288 (4), E693-E700 (2005)
   PUBMED   15562254
  REMARK    GeneRIF: USP19 is regulated in rat skeletal muscle during catabolic
            states.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY605065.1.
            
            On or before Aug 30, 2004 this sequence version replaced
            XP_341472.1, XP_341473.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY605065.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1357
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..1357
                     /product="ubiquitin carboxyl-terminal hydrolase 19"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 19; ubiquitin
                     thiolesterase 19; ubiquitin thioesterase 19;
                     deubiquitinating enzyme 19; ubiquitin-specific-processing
                     protease 19"
                     /calculated_mol_wt=150172
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Region          58..140
                     /region_name="p23_like"
                     /note="Proteins containing this p23_like domain include
                     p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1.
                     Both are co-chaperones for the heat shock protein (Hsp)
                     90. p23 binds Hsp90 and participates in the folding of a
                     number of Hsp90 clients, including...; cd06463"
                     /db_xref="CDD:107220"
     Region          162..239
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UJD6; propagated from
                     UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Region          275..296
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Region          327..423
                     /region_name="p23_CS_SGT1_like"
                     /note="p23_like domain similar to the C-terminal
                     CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 allele of
                     Skp1). Sgt1 interacts with multiple protein complexes and
                     has the features of a cochaperone. Human (h) Sgt1
                     interacts with both Hsp70 and Hsp90, and has...; cd06466"
                     /db_xref="CDD:107223"
     Region          414..534
                     /region_name="USP19_linker"
                     /note="Linker region of USP19 deubiquitinase; pfam16602"
                     /db_xref="CDD:465191"
     Region          432..479
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Region          <532..1254
                     /region_name="UBP12"
                     /note="Ubiquitin C-terminal hydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG5560"
                     /db_xref="CDD:227847"
     Region          962..981
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Region          1259..1278
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Region          1292..1320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Site            1331..1351
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     CDS             1..1357
                     /gene="Usp19"
                     /coded_by="NM_001001516.2:1..4074"
                     /db_xref="GeneID:361190"
                     /db_xref="RGD:1303276"
ORIGIN      
        1 msagtsatgp rrgppgleea tskkkqkdra nqeskdgdpr rvsmprkept kdellldwrq
       61 ssdkvvvklr vgtgpiclee vdaaftdtdc vvrlpdgrqw ggvffakiqs sctkvqtrkg
      121 gllqlalpkk vplltwpsll kkplgtqelv pglrcqengq elspialepg seprrakqea
      181 rnqkraqgrg evgsgaspga qagpsakrav hlcrgpegeg smdgpgpqgd apsflsdsat
      241 qveaeeqlhv ppvnpqtsll gseknlallt vektvsprsd svspvmirnr dpekddhfke
      301 emavgadpaa ladepesmvn lafvkndsye kgpdsvvvhv yvkesrrdts rvlfreqdft
      361 lifqtrdgnf lrlhpgcgph tifrwqvklr nliepeqctf cftasridic lrkrqsqrwg
      421 gleapatrvg gakvavptgp tpldstppgg gplpltgqee aravekekpk arsedsgldg
      481 vvartplehv tpkpephlas pkptcmvppm phspvsgdsv eedeeeekkv clpgftglvn
      541 lgntcfmnsv iqslsntrel rdffhdrsfe aeinynnplg tggrlaigfa vllralwkgt
      601 hqafqpsklk aivaskasqf tgyaqhdaqe fmaflldglh edlnriqnkp ytetvdsdgr
      661 pdevvaeeaw qrhkmrndsf ivdlfqgqyk sklvcpvcak vsitfdpfly lpvplpqkqk
      721 vlpiyyfare phskpikflv svskenssas evleslsqsv hvkpeslrla eviknrfhrv
      781 flpshsldav sptdvllcfe llspelaker vvvlevqqrp qvpsipiskc aacqrkqqse
      841 deklkrctrc yrvgycnqfc qkthwpdhkg lcrpenigyp flvsvpasrl tyarlaqlle
      901 gyarysvsvf qppfqpgrma lesqspgctt llstssleag dserepiqps elqlvtpvae
      961 gdtgahrmwp padrgpvpst sgissemlas gpmegcslla gervsrpeaa vpgyqhsres
     1021 vsahtpqffi ykidassreq rledkgdtpl elgddcslal vwrnnerlqe fvlvaskele
     1081 caedpgsage aaraghftld qclnlftrpe vlapeeawyc pqckqhreas kqlllwrlpn
     1141 vlivqlkrfs frsfiwrdki ndlvefpvrn ldlskfcigq keeqlpsydl yavinhyggm
     1201 igghytacar lpsdrssqrs dvgwrlfdds tvttvdesqv vtryayvlfy rrrnspverp
     1261 praahaehhp dlgpaaeaaa sqasriwqel eaeeemvpeg pgplgpwgpq dwvgppprgp
     1321 ttsdegclry fvlgtvaalv alvlnvfypl vsqsrwr
//
