ID   UBP15_MOUSE             Reviewed;         981 AA.
AC   Q8R5H1; Q3TGF5; Q3TTB2; Q3UL25; Q3UZH0; Q80TY6; Q80UK9;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 174.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 15;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q9Y4E8};
DE   AltName: Full=Deubiquitinating enzyme 15;
DE   AltName: Full=Ubiquitin thioesterase 15;
DE   AltName: Full=Ubiquitin-specific-processing protease 15;
GN   Name=Usp15; Synonyms=Kiaa0529;
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:0000312|EMBL:AAL77418.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=12532266; DOI=10.1007/s00335-002-3035-0;
RA   Angelats C., Wang X.-W., Jermiin L.S., Copeland N.G., Jenkins N.A.,
RA   Baker R.T.;
RT   "Isolation and characterization of the mouse ubiquitin-specific protease
RT   Usp15.";
RL   Mamm. Genome 14:31-46(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Amnion, Corpora quadrigemina, Testis, and Thymus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Trophoblast stem cell;
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229; THR-602; SER-961 AND
RP   SER-965, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
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   [8]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=24852371; DOI=10.1093/hmg/ddu244;
RA   Cornelissen T., Haddad D., Wauters F., Van Humbeeck C., Mandemakers W.,
RA   Koentjoro B., Sue C., Gevaert K., De Strooper B., Verstreken P.,
RA   Vandenberghe W.;
RT   "The deubiquitinase USP15 antagonizes Parkin-mediated mitochondrial
RT   ubiquitination and mitophagy.";
RL   Hum. Mol. Genet. 23:5227-5242(2014).
CC   -!- FUNCTION: Hydrolase that removes conjugated ubiquitin from target
CC       proteins and regulates various pathways such as the TGF-beta receptor
CC       signaling, NF-kappa-B and RNF41/NRDP1-PRKN pathways. Acts as a key
CC       regulator of TGF-beta receptor signaling pathway, but the precise
CC       mechanism is still unclear: according to a report, acts by promoting
CC       deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or
CC       SMAD3), thereby alleviating inhibition of R-SMADs and promoting
CC       activation of TGF-beta target genes. According to another reports,
CC       regulates the TGF-beta receptor signaling pathway by mediating
CC       deubiquitination and stabilization of TGFBR1, leading to an enhanced
CC       TGF-beta signal. Able to mediate deubiquitination of monoubiquitinated
CC       substrates, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitin
CC       chains. May also regulate gene expression and/or DNA repair through the
CC       deubiquitination of histone H2B. Acts as an inhibitor of mitophagy by
CC       counteracting the action of parkin (PRKN): hydrolyzes cleavage of 'Lys-
CC       48'- and 'Lys-63'-linked polyubiquitin chains attached by parkin on
CC       target proteins such as MFN2, thereby reducing parkin's ability to
CC       drive mitophagy. Acts as an associated component of COP9 signalosome
CC       complex (CSN) and regulates different pathways via this association:
CC       regulates NF-kappa-B by mediating deubiquitination of NFKBIA and
CC       deubiquitinates substrates bound to VCP. Involved in endosome
CC       organization by mediating deubiquitination of SQSTM1: ubiquitinated
CC       SQSTM1 forms a molecular bridge that restrains cognate vesicles in the
CC       perinuclear region and its deubiquitination releases target vesicles
CC       for fast transport into the cell periphery. Acts as a negative
CC       regulator of antifungal immunity by mediating 'Lys-27'-linked
CC       deubiquitination of CARD9, thereby inactivating CARD9.
CC       {ECO:0000250|UniProtKB:Q9Y4E8}.
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:0000250|UniProtKB:Q9Y4E8};
CC   -!- SUBUNIT: A homodimer structure has been reported; however it is unclear
CC       whether the protein form a homodimer in vivo. Identified in a complex
CC       with the COP9 signalosome complex (CSN). Interacts with SMAD1, SMAD2
CC       and SMAD3; the interaction is direct. Forms a complex with SMURF2 and
CC       SMAD7. Interacts with TGFBR1. Interacts with SART3; the interaction is
CC       direct. May interact with RNF20 and RNF40. May interact with PRKN.
CC       Interacts with INCA1. {ECO:0000250|UniProtKB:Q9Y4E8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24852371}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9Y4E8}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q9Y4E8}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Experimental confirmation may be lacking for some isoforms.;
CC       Name=1;
CC         IsoId=Q8R5H1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R5H1-2; Sequence=VSP_005262, VSP_005263;
CC       Name=3;
CC         IsoId=Q8R5H1-3; Sequence=VSP_005264;
CC       Name=4;
CC         IsoId=Q8R5H1-4; Sequence=VSP_005265, VSP_005266;
CC       Name=5;
CC         IsoId=Q8R5H1-5; Sequence=VSP_005263;
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in the brain
CC       and spleen, and lowest levels in the muscles (at protein level)
CC       (PubMed:24852371). In the midbrain, strong expression in neurons
CC       including the dopaminergic neurons (at protein level)
CC       (PubMed:24852371). Widely expressed with highest levels in testis,
CC       heart and liver (PubMed:12532266). {ECO:0000269|PubMed:12532266,
CC       ECO:0000269|PubMed:24852371}.
CC   -!- PTM: Phosphorylated. Phosphorylation protects against ubiquitination
CC       and subsequent degradation by the proteasome.
CC       {ECO:0000250|UniProtKB:Q9Y4E8}.
CC   -!- PTM: Ubiquitinated, leading to degradation by the proteasome.
CC       {ECO:0000250|UniProtKB:Q9Y4E8}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65583.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=EDL24441.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF468037; AAL77418.1; -; mRNA.
DR   EMBL; AK046332; BAC32683.1; -; mRNA.
DR   EMBL; AK083303; BAC38854.1; -; mRNA.
DR   EMBL; AK133852; BAE21887.1; -; mRNA.
DR   EMBL; AK145749; BAE26626.1; -; mRNA.
DR   EMBL; AK161469; BAE36413.1; -; mRNA.
DR   EMBL; AK168755; BAE40593.1; -; mRNA.
DR   EMBL; AK122301; BAC65583.1; ALT_INIT; mRNA.
DR   EMBL; CH466578; EDL24441.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BC050042; AAH50042.1; -; mRNA.
DR   CCDS; CCDS24217.1; -. [Q8R5H1-1]
DR   CCDS; CCDS88095.1; -. [Q8R5H1-5]
DR   RefSeq; NP_001288557.1; NM_001301628.1. [Q8R5H1-5]
DR   RefSeq; NP_081880.2; NM_027604.4. [Q8R5H1-1]
DR   AlphaFoldDB; Q8R5H1; -.
DR   BMRB; Q8R5H1; -.
DR   SMR; Q8R5H1; -.
DR   BioGRID; 199854; 98.
DR   IntAct; Q8R5H1; 3.
DR   MINT; Q8R5H1; -.
DR   STRING; 10090.ENSMUSP00000151244; -.
DR   MEROPS; C19.022; -.
DR   GlyGen; Q8R5H1; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8R5H1; -.
DR   PhosphoSitePlus; Q8R5H1; -.
DR   SwissPalm; Q8R5H1; -.
DR   EPD; Q8R5H1; -.
DR   jPOST; Q8R5H1; -.
DR   MaxQB; Q8R5H1; -.
DR   PaxDb; 10090-ENSMUSP00000020334; -.
DR   PeptideAtlas; Q8R5H1; -.
DR   ProteomicsDB; 298091; -. [Q8R5H1-1]
DR   ProteomicsDB; 298092; -. [Q8R5H1-2]
DR   ProteomicsDB; 298093; -. [Q8R5H1-3]
DR   ProteomicsDB; 298094; -. [Q8R5H1-4]
DR   ProteomicsDB; 298095; -. [Q8R5H1-5]
DR   Pumba; Q8R5H1; -.
DR   Antibodypedia; 1729; 385 antibodies from 38 providers.
DR   DNASU; 14479; -.
DR   Ensembl; ENSMUST00000020334.9; ENSMUSP00000020334.9; ENSMUSG00000020124.11. [Q8R5H1-5]
DR   Ensembl; ENSMUST00000220377.2; ENSMUSP00000151244.2; ENSMUSG00000020124.11. [Q8R5H1-1]
DR   GeneID; 14479; -.
DR   KEGG; mmu:14479; -.
DR   UCSC; uc007hgn.2; mouse. [Q8R5H1-1]
DR   UCSC; uc007hgo.2; mouse. [Q8R5H1-5]
DR   UCSC; uc007hgt.2; mouse. [Q8R5H1-3]
DR   UCSC; uc011xpf.2; mouse. [Q8R5H1-4]
DR   AGR; MGI:101857; -.
DR   CTD; 9958; -.
DR   MGI; MGI:101857; Usp15.
DR   VEuPathDB; HostDB:ENSMUSG00000020124; -.
DR   eggNOG; KOG1870; Eukaryota.
DR   GeneTree; ENSGT00940000154932; -.
DR   HOGENOM; CLU_001060_7_1_1; -.
DR   InParanoid; Q8R5H1; -.
DR   OMA; PCHAQQS; -.
DR   OrthoDB; 5474185at2759; -.
DR   PhylomeDB; Q8R5H1; -.
DR   TreeFam; TF106276; -.
DR   Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR   BioGRID-ORCS; 14479; 7 hits in 78 CRISPR screens.
DR   ChiTaRS; Usp15; mouse.
DR   PRO; PR:Q8R5H1; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q8R5H1; Protein.
DR   Bgee; ENSMUSG00000020124; Expressed in spermatid and 275 other cell types or tissues.
DR   ExpressionAtlas; Q8R5H1; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:MGI.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0101005; F:deubiquitinase activity; IMP:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:1990380; F:K48-linked deubiquitinase activity; ISO:MGI.
DR   GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR   GO; GO:0005160; F:transforming growth factor beta receptor binding; ISO:MGI.
DR   GO; GO:0061649; F:ubiquitin modification-dependent histone binding; ISO:MGI.
DR   GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0035520; P:monoubiquitinated protein deubiquitination; ISS:UniProtKB.
DR   GO; GO:1905035; P:negative regulation of antifungal innate immune response; ISS:UniProtKB.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; ISO:MGI.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR   GO; GO:1990167; P:protein K27-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:1902238; P:regulation of intrinsic apoptotic signaling pathway in response to osmotic stress by p53 class mediator; IMP:MGI.
DR   GO; GO:0140673; P:transcription elongation-coupled chromatin remodeling; ISS:UniProtKB.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
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; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   InterPro; IPR028135; Ub_USP-typ.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR029346; USP_C.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF28; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 15; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF14836; Ubiquitin_3; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF14533; USP7_C2; 1.
DR   SMART; SM00695; DUSP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   SUPFAM; SSF55205; EPT/RTPC-like; 1.
DR   SUPFAM; SSF54236; Ubiquitin-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.
DR   Genevisible; Q8R5H1; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Hydrolase; Mitochondrion;
KW   Nucleus; Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation; Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E8"
FT   CHAIN           2..981
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 15"
FT                   /id="PRO_0000080642"
FT   DOMAIN          7..118
FT                   /note="DUSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT   DOMAIN          289..933
FT                   /note="USP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT   REGION          2..223
FT                   /note="Mediates interaction with SART3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E8"
FT   REGION          216..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          633..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          952..981
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        655..670
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..694
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        298
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        891
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E8"
FT   MOD_RES         226
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E8"
FT   MOD_RES         229
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         242
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4E8"
FT   MOD_RES         602
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         961
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         965
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         18..25
FT                   /note="TLLKTSLR -> DAWLKPRSG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12532266"
FT                   /id="VSP_005262"
FT   VAR_SEQ         209..227
FT                   /note="LVIEQKNEDGTWPRGPSTP -> PRCIQFFNFTKDLSFISIK (in
FT                   isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_005265"
FT   VAR_SEQ         228..981
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_005266"
FT   VAR_SEQ         228..256
FT                   /note="Missing (in isoform 2 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:12532266,
FT                   ECO:0000303|PubMed:12693553, ECO:0000303|PubMed:16141072"
FT                   /id="VSP_005263"
FT   VAR_SEQ         229..981
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_005264"
FT   CONFLICT        130
FT                   /note="E -> G (in Ref. 3; BAE40593)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        158
FT                   /note="I -> M (in Ref. 3; BAE36413)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        184
FT                   /note="M -> V (in Ref. 5; AAH50042)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        662
FT                   /note="D -> G (in Ref. 5; AAH50042)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        800
FT                   /note="K -> E (in Ref. 5; AAH50042)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   981 AA;  112325 MW;  6D5377C3FEA6E40A CRC64;
     MAEGGAADLD TQRSDIATLL KTSLRKGDTW YLVDSRWFKQ WKKYVGFDSW DKYQMGDQNV
     YPGPIDNSGL LKDGDAQSLK EHLIDELDYI LLPTEGWNKL VSWYTLMEGQ EPIARKVVEQ
     GMFVKHCKVE VYLTELKLCE NGNMNNVVTR RFSKADTIDT IEKEIRKIFN IPDEKEARLW
     NKYMSNTFEP LNKPDSTIQD AGLYQGQVLV IEQKNEDGTW PRGPSTPKSP GASNFSTLPK
     ISPSSLSNNY NNINNRNVKN SNYCLPSYTA YKNYDYSEPG RNNEQPGLCG LSNLGNTCFM
     NSAIQCLSNT PPLTEYFLND KYQEELNFDN PLGMRGEIAK SYAELIKQMW SGKFSYVTPR
     AFKTQVGRFA PQFSGYQQQD CQELLAFLLD GLHEDLNRIR KKPYIQLKDA DGRPDKVVAE
     EAWENHLKRN DSIIVDIFHG LFKSTLVCPE CAKISVTFDP FCYLTLPLPM KKERSLEVYL
     VRMDPLAKPM QYKVIVPKIG NILDLCTALS ALSGVPADKM IVTDIYNHRF HRIFAVDENL
     SSIMERDDIY VFEININRAE DTEHVVIPVC LREKFRHSSY THHTGSSLFG QPFLMAIPRN
     NTEDKLYNLL LLRMCRYVKM STETEETDGH LRCCEDQNIN GNGPNGLHEE GSPSEMETDE
     PDDESSQDQE LPSENENSQS EDSVGGDNDS ENGLCTEETC KGQLTGHKKR LFTFQFNNLG
     NNDINYIKDD TSHIRFDDRQ LRLDERSFLA LDWDPDLKKR YFDENAAEDF EKHESVEYKP
     PKRPFVKLKD CIELFTTKEK LGAEDPWYCP NCKEHQQATK KLDLWSLPPV LVVHLKRFSY
     SRYMRDKLDT LVDFPISDLD MSEFLINPNA GPCRYNLIAV SNHYGGMGGG HYTAFAKNKD
     DGKWYYFDDS SVSTASEDQI VSKAAYVLFY QRQDTFSGTG FFPLDRETKG ASAATGIPLE
     SDEDSNDNDN DLENENCMHT N
//