ID   UBP43_MOUSE             Reviewed;        1132 AA.
AC   Q8BUM9; Q8VDP5;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   24-JAN-2024, entry version 145.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 43;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 43;
DE   AltName: Full=Ubiquitin thioesterase 43;
DE   AltName: Full=Ubiquitin-specific-processing protease 43;
GN   Name=Usp43;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-1132 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 207-1132 (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
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).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-970, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-746, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: May recognize and hydrolyze the peptide bond at the C-
CC       terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin
CC       precursors as well as that of ubiquitinated proteins (By similarity).
CC       {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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BUM9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BUM9-2; Sequence=VSP_020469, VSP_020470;
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH21474.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC38837.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL732570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK083271; BAC38837.1; ALT_INIT; mRNA.
DR   EMBL; BC021474; AAH21474.1; ALT_INIT; mRNA.
DR   CCDS; CCDS24861.2; -. [Q8BUM9-1]
DR   RefSeq; NP_001277978.1; NM_001291049.1.
DR   RefSeq; NP_776115.2; NM_173754.4. [Q8BUM9-1]
DR   AlphaFoldDB; Q8BUM9; -.
DR   STRING; 10090.ENSMUSP00000021288; -.
DR   MEROPS; C19.979; -.
DR   GlyGen; Q8BUM9; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q8BUM9; -.
DR   PhosphoSitePlus; Q8BUM9; -.
DR   MaxQB; Q8BUM9; -.
DR   PaxDb; 10090-ENSMUSP00000021288; -.
DR   ProteomicsDB; 297705; -. [Q8BUM9-1]
DR   ProteomicsDB; 297706; -. [Q8BUM9-2]
DR   Antibodypedia; 6274; 162 antibodies from 25 providers.
DR   DNASU; 216835; -.
DR   Ensembl; ENSMUST00000021288.10; ENSMUSP00000021288.4; ENSMUSG00000020905.12. [Q8BUM9-1]
DR   GeneID; 216835; -.
DR   KEGG; mmu:216835; -.
DR   UCSC; uc007jne.1; mouse. [Q8BUM9-1]
DR   AGR; MGI:2444541; -.
DR   CTD; 124739; -.
DR   MGI; MGI:2444541; Usp43.
DR   VEuPathDB; HostDB:ENSMUSG00000020905; -.
DR   eggNOG; KOG1868; Eukaryota.
DR   eggNOG; KOG1870; Eukaryota.
DR   GeneTree; ENSGT00940000158772; -.
DR   HOGENOM; CLU_001060_6_0_1; -.
DR   InParanoid; Q8BUM9; -.
DR   OMA; LAVEWDC; -.
DR   OrthoDB; 5474185at2759; -.
DR   PhylomeDB; Q8BUM9; -.
DR   TreeFam; TF106278; -.
DR   Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
DR   BioGRID-ORCS; 216835; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Usp43; mouse.
DR   PRO; PR:Q8BUM9; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q8BUM9; Protein.
DR   Bgee; ENSMUSG00000020905; Expressed in animal zygote and 118 other cell types or tissues.
DR   ExpressionAtlas; Q8BUM9; baseline and differential.
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   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF20; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 43; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   Genevisible; Q8BUM9; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Methylation; Phosphoprotein; Protease;
KW   Reference proteome; Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..1132
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 43"
FT                   /id="PRO_0000249522"
FT   DOMAIN          101..710
FT                   /note="USP"
FT   REGION          1..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          935..1008
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1024..1044
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1057..1106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        954..979
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1062..1077
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1090..1106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        110
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        668
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   MOD_RES         746
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         970
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1047
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_020469"
FT   VAR_SEQ         1052
FT                   /note="Q -> QARGSSP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_020470"
FT   CONFLICT        760
FT                   /note="M -> V (in Ref. 3; AAH21474)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        982
FT                   /note="S -> N (in Ref. 3; AAH21474)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1002
FT                   /note="D -> G (in Ref. 3; AAH21474)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1132 AA;  123874 MW;  3E9E9E46B75E67FA CRC64;
     MDPGVGNALG EGPPAPRPRR RRSLRRLLNR FLLALGSRSR SGDSPPRPPA QPSPYDGDGE
     GGFACAPGPA PASAGSPGPD RPPGSQPQIS SGDGARPPGA QGLKNHGNTC FMNAVVQCLS
     NTDLLAEFLA LGRYRAAPGR AEVTEQLAAL VRALWTREYT PQLSAEFKNA VSKYGSQFQG
     NSQHDALEFL LWLLDRVHED LEGSAHGLVS EQLPPEVSKI SEDLRPSAAP TSLGPSFVQS
     HFQAQYRSSL TCPHCLKQSN TFDPFLCVSL PIPLRQTRFL SVTLVFPSKS QRFLRVGLAV
     PILSTVAALR KMVAEEGGVP AEEVILVELY PNGFQRSFFD EEDLNTIAEG DNVYAFQVPP
     SPGLGTLSAH PSGLSVSPRL PVRDSQRFSG PLHSENRVVF LFCNLVGSGQ QASRFGPPFL
     IREDRTISWA QLQQCILSKV RCLMRSEVSA QDLGTLFSIR VVGLSLACSY LSPKDNRPLC
     HWAVDRALHL RRPGGPPHVK LAVEWDSSVT ERLFGSLQEE RVQDADSVWR QQQAHQQPSC
     TLDECFQSYT KEEQLAQDDA WKCPHCQVLQ QGVVKLSLWT LPDILIIHLK RFCQVGERRN
     KLSTLVKFPL SGLNMAPHVA RRSTNSKAGP GPWSSWKQPI CLPTTYPLDF LYDLYAVCNH
     HGSLQGGHYT AYCRNSLDGQ WYSYDDSTVE ALREDEVNTR GAYILFYQKR NSIPPWSASS
     SMRGSTSSSL SDHWLMRLGS LNNSTRGSLL SWSSAPCPSM ARVPDSPVFT NGVCHQDKGG
     VETRPLVRGV GGRSISMKAS PASRSRHGPF KTMPLRWSFG HREKRPGASV ELVEYLESRR
     RPRSTSQSIV PLLTRAAGGE ETSASPRSDG TLPAKSEDSG RAIGQGTTGV PLSSCHLNHH
     PALGSLDDSL HTARTRTGNV SQDIRLPKKF DLPLTVMPSV GDEKPARPEG QKMTPWKGSS
     QVGSQSSPPS PSTGLLRNFK DSGPGTLPKM KSKAAMEERA PDKDRGQGTF TLLKSVFWKK
     EHKRTVRTES SPPAPPISLG SDRLSPAAMN EQALRIRESP AKGLGNHMER DIRSAPSSLH
     LPRKASRPPR ASTAGTSQRT IPGEQISYGT LQRVKYHTLS LGRKKSLPES SF
//