SENP2_RAT
ID SENP2_RAT Reviewed; 588 AA.
AC Q9EQE1;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Sentrin-specific protease 2 {ECO:0000305};
DE EC=3.4.22.- {ECO:0000250|UniProtKB:Q9HC62};
DE AltName: Full=Axin-associating molecule {ECO:0000303|PubMed:10944533};
DE Short=Axam {ECO:0000303|PubMed:10944533};
DE AltName: Full=Sentrin/SUMO-specific protease SENP2;
GN Name=Senp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10944533; DOI=10.1074/jbc.m005984200;
RA Kadoya T., Kishida S., Fukui A., Hinoi T., Michiue T., Asashima M.,
RA Kikuchi A.;
RT "Inhibition of Wnt signaling pathway by a novel Axin-binding protein.";
RL J. Biol. Chem. 275:37030-37037(2000).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF CYS-547.
RX PubMed=11997515; DOI=10.1128/mcb.22.11.3803-3819.2002;
RA Kadoya T., Yamamoto H., Suzuki T., Yukita A., Fukui A., Michiue T.,
RA Asahara T., Tanaka K., Asashima M., Kikuchi A.;
RT "Desumoylation activity of Axam, a novel Axin-binding protein, is involved
RT in downregulation of beta-catenin.";
RL Mol. Cell. Biol. 22:3803-3819(2002).
CC -!- FUNCTION: Protease that catalyzes two essential functions in the SUMO
CC pathway (By similarity). The first is the hydrolysis of an alpha-linked
CC peptide bond at the C-terminal end of the small ubiquitin-like modifier
CC (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form
CC of the proteins (By similarity). The second is the deconjugation of
CC SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-
CC linked peptide bond between the C-terminal glycine of the mature SUMO
CC and the lysine epsilon-amino group of the target protein (By
CC similarity). May down-regulate CTNNB1 levels and thereby modulate the
CC Wnt pathway (PubMed:10944533, PubMed:11997515). Deconjugates SUMO2 from
CC MTA1 (By similarity). Plays a dynamic role in adipogenesis by
CC desumoylating and promoting the stabilization of CEBPB (By similarity).
CC Acts as a regulator of the cGAS-STING pathway by catalyzing
CC desumoylation of CGAS and STING1 during the late phase of viral
CC infection (By similarity). {ECO:0000250|UniProtKB:Q91ZX6,
CC ECO:0000250|UniProtKB:Q9HC62, ECO:0000269|PubMed:10944533,
CC ECO:0000269|PubMed:11997515}.
CC -!- SUBUNIT: Binds to SUMO2 and SUMO3 (By similarity). Interacts with the
CC C-terminal domain of NUP153 via its N-terminus (By similarity).
CC Interacts with MTA1 (By similarity). Binds to AXIN1 (PubMed:10944533).
CC {ECO:0000250|UniProtKB:Q9HC62, ECO:0000269|PubMed:10944533}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:Q9HC62}. Nucleus membrane
CC {ECO:0000250|UniProtKB:Q9HC62}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9HC62}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:Q9HC62}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9HC62}. Note=Shuttles between cytoplasm and
CC nucleus. {ECO:0000250|UniProtKB:Q9HC62}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain, lung and
CC testis. {ECO:0000269|PubMed:10944533}.
CC -!- PTM: Polyubiquitinated; which leads to proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q9HC62}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR EMBL; AF260129; AAG34653.1; -; mRNA.
DR RefSeq; NP_076479.1; NM_023989.1.
DR AlphaFoldDB; Q9EQE1; -.
DR SMR; Q9EQE1; -.
DR BioGRID; 249380; 2.
DR STRING; 10116.ENSRNOP00000002425; -.
DR MEROPS; C48.007; -.
DR iPTMnet; Q9EQE1; -.
DR PhosphoSitePlus; Q9EQE1; -.
DR PaxDb; Q9EQE1; -.
DR PRIDE; Q9EQE1; -.
DR GeneID; 78973; -.
DR KEGG; rno:78973; -.
DR UCSC; RGD:708378; rat.
DR CTD; 59343; -.
DR RGD; 708378; Senp2.
DR VEuPathDB; HostDB:ENSRNOG00000001773; -.
DR eggNOG; KOG0778; Eukaryota.
DR HOGENOM; CLU_024324_4_0_1; -.
DR InParanoid; Q9EQE1; -.
DR OMA; PGMYRWL; -.
DR OrthoDB; 1480705at2759; -.
DR PhylomeDB; Q9EQE1; -.
DR TreeFam; TF316289; -.
DR Reactome; R-RNO-3065679; SUMO is proteolytically processed.
DR PRO; PR:Q9EQE1; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001773; Expressed in brain and 19 other tissues.
DR ExpressionAtlas; Q9EQE1; baseline and differential.
DR Genevisible; Q9EQE1; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; IEA:Ensembl.
DR GO; GO:0016929; F:deSUMOylase activity; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0070139; F:SUMO-specific endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IDA:RGD.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0060711; P:labyrinthine layer development; ISO:RGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0035562; P:negative regulation of chromatin binding; ISO:RGD.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:RGD.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:RGD.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0031648; P:protein destabilization; ISO:RGD.
DR GO; GO:0016926; P:protein desumoylation; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032875; P:regulation of DNA endoreduplication; ISO:RGD.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0051246; P:regulation of protein metabolic process; IDA:RGD.
DR GO; GO:0060712; P:spongiotrophoblast layer development; ISO:RGD.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; ISO:RGD.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR Pfam; PF02902; Peptidase_C48; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Phosphoprotein; Protease; Protein transport; Reference proteome;
KW Thiol protease; Translocation; Transport; Ubl conjugation;
KW Ubl conjugation pathway; Wnt signaling pathway.
FT CHAIN 1..588
FT /note="Sentrin-specific protease 2"
FT /id="PRO_0000101720"
FT REGION 72..381
FT /note="Axin-binding"
FT /evidence="ECO:0000269|PubMed:10944533"
FT REGION 157..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..558
FT /note="Protease"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT MOTIF 28..31
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 47..52
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 316..331
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT ACT_SITE 477
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT ACT_SITE 494
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT ACT_SITE 547
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT MUTAGEN 547
FT /note="C->S: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:11997515"
SQ SEQUENCE 588 AA; 67252 MW; BEC186367D8284C4 CRC64;
MYRWLTKVLG TILRLCERPA PGARALLKRR RSSSSLFSTA VDTDEIPAKR PRLDCFIHQV
KNSLYNAASL FGFPFQLTTK PMVSSACNGT RNVAPSGEVF SNSPSCELTT SGSCSSMLKL
GNKSPNGISD YPKIRVTVAR DQPRRVLPSF GFTLKSEGYN RRPSGRRHSK SNPESSLPWK
PQEQGVTEMI SEEGGKGARR PHCTVEEGVQ KDEREKYLKL LERLKEGAHG STFPPAVSHH
SSQRTQMDTL KTKGWMEEQN HGVRTTHLVP KQYRVVETRG PLCSVRSEKR YSKGKADTEK
VVGLRFEKDG TRGHQLEPDL SEEVSARLRL GSGSNGLLRR KISVLEAKEK NFPSKEKDRR
TEDLFELTED MEKEISNALG HGPPDEILSS AFKLRITRGD IQTLKNYHWL NDEVINFYMN
LLVERSKKQG YPALHALSTF FYPKLKSGGY QAVKRWTKGV NLFDQELVLV PIHRKVHWSL
VVMDLRKKCL KYLDSMGQKG HRICEILLQY LQDESKTKRN TDLNLLEWTH YSMKPHEIPQ
QLNGSDCGMF TCKYADYISR DKPITFTQHQ MPLFRKKMVW EILHQQLL
