SENP6_MOUSE
ID SENP6_MOUSE Reviewed; 1132 AA.
AC Q6P7W0; E9QN09; Q6ZQ43; Q8BK94; Q8BUL4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Sentrin-specific protease 6;
DE EC=3.4.22.-;
DE AltName: Full=SUMO-1-specific protease 1;
DE AltName: Full=Sentrin/SUMO-specific protease SENP6;
GN Name=Senp6; Synonyms=Kiaa0797, Susp1;
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 MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Limb;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-231 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-356, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, 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).
CC -!- FUNCTION: Protease that deconjugates SUMO1, SUMO2 and SUMO3 from
CC targeted proteins. Processes preferentially poly-SUMO2 and poly-SUMO3
CC chains, but does not efficiently process SUMO1, SUMO2 and SUMO3
CC precursors. Deconjugates SUMO1 from RXRA, leading to transcriptional
CC activation. Involved in chromosome alignment and spindle assembly, by
CC regulating the kinetochore CENPH-CENPI-CENPK complex. Desumoylates PML
CC and CENPI, protecting them from degradation by the ubiquitin ligase
CC RNF4, which targets polysumoylated proteins for proteasomal
CC degradation. Desumoylates also RPA1, thus preventing recruitment of
CC RAD51 to the DNA damage foci to initiate DNA repair through homologous
CC recombination.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts with RXRA. Forms a complex with KAT5-TIP60 and UBE2I
CC in response to UV irradiation. Interacts with RPA1 to maintain it in
CC hyposumoylated state during S phase preventing DNA repair initiation
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P7W0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P7W0-2; Sequence=VSP_021943;
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH61480.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC35583.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAC98029.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129219; BAC98029.1; ALT_INIT; mRNA.
DR EMBL; AC142111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC061480; AAH61480.1; ALT_FRAME; mRNA.
DR EMBL; AK053904; BAC35583.1; ALT_SEQ; mRNA.
DR EMBL; AK083377; BAC38892.2; -; mRNA.
DR CCDS; CCDS40705.1; -. [Q6P7W0-1]
DR RefSeq; NP_001298039.1; NM_001311110.1.
DR RefSeq; NP_666115.2; NM_146003.2. [Q6P7W0-1]
DR AlphaFoldDB; Q6P7W0; -.
DR SMR; Q6P7W0; -.
DR BioGRID; 229616; 7.
DR IntAct; Q6P7W0; 2.
DR MINT; Q6P7W0; -.
DR STRING; 10090.ENSMUSP00000047220; -.
DR MEROPS; C48.004; -.
DR iPTMnet; Q6P7W0; -.
DR PhosphoSitePlus; Q6P7W0; -.
DR EPD; Q6P7W0; -.
DR jPOST; Q6P7W0; -.
DR MaxQB; Q6P7W0; -.
DR PaxDb; Q6P7W0; -.
DR PeptideAtlas; Q6P7W0; -.
DR PRIDE; Q6P7W0; -.
DR ProteomicsDB; 256545; -. [Q6P7W0-1]
DR ProteomicsDB; 256546; -. [Q6P7W0-2]
DR Antibodypedia; 7742; 420 antibodies from 32 providers.
DR DNASU; 215351; -.
DR Ensembl; ENSMUST00000037484; ENSMUSP00000047220; ENSMUSG00000034252. [Q6P7W0-1]
DR Ensembl; ENSMUST00000164859; ENSMUSP00000128918; ENSMUSG00000034252. [Q6P7W0-2]
DR GeneID; 215351; -.
DR KEGG; mmu:215351; -.
DR UCSC; uc009qvb.1; mouse. [Q6P7W0-1]
DR CTD; 26054; -.
DR MGI; MGI:1922075; Senp6.
DR VEuPathDB; HostDB:ENSMUSG00000034252; -.
DR eggNOG; KOG0779; Eukaryota.
DR GeneTree; ENSGT00940000155724; -.
DR InParanoid; Q6P7W0; -.
DR OMA; RKEYPAH; -.
DR OrthoDB; 1241636at2759; -.
DR TreeFam; TF350136; -.
DR BRENDA; 3.4.22.B74; 3474.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 215351; 10 hits in 72 CRISPR screens.
DR ChiTaRS; Senp6; mouse.
DR PRO; PR:Q6P7W0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6P7W0; protein.
DR Bgee; ENSMUSG00000034252; Expressed in undifferentiated genital tubercle and 258 other tissues.
DR ExpressionAtlas; Q6P7W0; baseline and differential.
DR Genevisible; Q6P7W0; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0070139; F:SUMO-specific endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0016926; P:protein desumoylation; ISS:UniProtKB.
DR GO; GO:0070646; P:protein modification by small protein removal; ISS:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0090234; P:regulation of kinetochore assembly; ISS:UniProtKB.
DR GO; GO:0090169; P:regulation of spindle assembly; ISS:UniProtKB.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR Pfam; PF02902; Peptidase_C48; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Isopeptide bond; Nucleus; Phosphoprotein;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..1132
FT /note="Sentrin-specific protease 6"
FT /id="PRO_0000267608"
FT REGION 23..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..1132
FT /note="Protease"
FT ACT_SITE 785
FT /evidence="ECO:0000250"
FT ACT_SITE 936
FT /evidence="ECO:0000250"
FT ACT_SITE 1049
FT /evidence="ECO:0000250"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR1"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR1"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR1"
FT MOD_RES 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR1"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR1"
FT MOD_RES 1131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR1"
FT CROSSLNK 648
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9GZR1"
FT VAR_SEQ 1..166
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_021943"
FT CONFLICT 121
FT /note="G -> A (in Ref. 3; AAH61480)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="K -> Q (in Ref. 1; BAC98029 and 3; AAH61480)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="E -> D (in Ref. 1; BAC98029 and 3; AAH61480)"
FT /evidence="ECO:0000305"
FT CONFLICT 1075
FT /note="M -> V (in Ref. 1; BAC98029)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1132 AA; 127013 MW; 7D9BE2AE1202ECFF CRC64;
MAAGKSGGSA GALFLKALDR SESKRDGGFK NNWSFDHEEE SEGDADKDGA NLLSVEDEDS
EISKGKKLNR RSEIVATSSG DFILKTYVRR SKTDGFKTLK GNPIGLNMLS NNKKLSESTA
GTALCSGTVV HGRRFHHAHS QTPGIRTAAQ RKEYPPYVHK AENSPVMLSH GQGGDHIMKK
TEESESYVES EIKRKVQQKR HCSTYQLSPL SPASKKCLTH LEVSEQREYC PKCGKEKENQ
TKCQSCGIVF HNDLQRNCRQ AVTLNEPTGP LLRTSIHQNS GGQKSQNTGL TAKKFYGNSV
DKIPIDILVT CDDSRHNYIQ TNGKVILPGG KIPKLTNPKE RKISVSDLND PIILSSDDDD
DDDDRTKRRE STSPKPADSA CSSPVPSTGK VEAALNADAC RAEQEPRSSP AEPELNTIVI
PRKARMKDQL GNSISTPLKR RKVNSHAAFI HPMSLSCQNF ESVILNCRSI RVGTLFRLLV
EPVIFSLESI TIHLDGPESD PVDIILNTSD LTKCEWCNVR KLPVVFLQAI PAVYQKLSMQ
LQMSKEDKVW NDCKGINRIT SLEEQYIILI FQTGLDHQAE VVFESIITDI GIRNNVPNFF
AKILFDEANS RLVACTRSYE ESIKGNCAQK ENKVKTVSFE SKIQLRSKQE LQFFDDDEEA
GESHTIFIGP VEKLIVYPPP PAKGGISVTN EDLHCLSEGE FLNDVIIDFY LKYLVLEKLK
KEDADRIHIF SSFFYKRLNQ RERRNPETTN LSIQQKRHGR VKTWTRHVDI FEKDFIFVPL
NEAAHWFLAV VCFPGLEKPK YEPNPHYHEN AVMQKTPSAE DSCVSSASEM GACSQNSAAK
PVIKKMLNRK HCLAVTDSSA AQEESEPCYR RNAYSVKCSM KKKNHAINEN EEPSNGESTC
QDICDRTQSE NGLRDECFSS VHHPDALSKI RLNYGDQSAD GGKLLEDELI DFSEDQDDPD
DSSDDGLLAD ENYSSEIGQW HLKPTVCKQP CILLMDSLRG PSRSNVVKIL REYLEVEWEV
KKGSKRSFSK DVMKGSNPKV PQQNNFSDCG VYVLQYVESF FENPVLNFEL PMNLMNWFPP
PRMKTKREEI RNIILKLQES QSKDKKLLKD SLAETSLGDG AEQYASASGG SE
