SENP2_PONAB
ID SENP2_PONAB Reviewed; 589 AA.
AC Q5R7K7; Q5RDS3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Sentrin-specific protease 2 {ECO:0000305};
DE EC=3.4.22.- {ECO:0000250|UniProtKB:Q9HC62};
DE AltName: Full=Sentrin/SUMO-specific protease SENP2;
GN Name=SENP2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protease that catalyzes two essential functions in the SUMO
CC pathway. The first is the hydrolysis of an alpha-linked peptide bond at
CC the C-terminal end of the small ubiquitin-like modifier (SUMO)
CC propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the
CC proteins. The second is the deconjugation of SUMO1, SUMO2 and SUMO3
CC from targeted proteins, by cleaving an epsilon-linked peptide bond
CC between the C-terminal glycine of the mature SUMO and the lysine
CC epsilon-amino group of the target protein (By similarity). May down-
CC regulate CTNNB1 levels and thereby modulate the Wnt pathway (By
CC similarity). Deconjugates SUMO2 from MTA1. Plays a dynamic role in
CC adipogenesis by desumoylating and promoting the stabilization of CEBPB
CC (By similarity). Acts as a regulator of the cGAS-STING pathway by
CC catalyzing desumoylation of CGAS and STING1 during the late phase of
CC viral infection (By similarity). {ECO:0000250|UniProtKB:Q91ZX6,
CC ECO:0000250|UniProtKB:Q9HC62}.
CC -!- SUBUNIT: Binds to SUMO2 and SUMO3. Interacts with the C-terminal domain
CC of NUP153 via its N-terminus. Interacts with MTA1.
CC {ECO:0000250|UniProtKB:Q9HC62}.
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 -!- DOMAIN: The N-terminus is necessary and sufficient for nuclear envelope
CC targeting. {ECO:0000250|UniProtKB:Q9HC62}.
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; CR857828; CAH90084.1; -; mRNA.
DR EMBL; CR860108; CAH92253.1; -; mRNA.
DR RefSeq; NP_001124998.1; NM_001131526.1.
DR AlphaFoldDB; Q5R7K7; -.
DR SMR; Q5R7K7; -.
DR MEROPS; C48.007; -.
DR PRIDE; Q5R7K7; -.
DR GeneID; 100171874; -.
DR KEGG; pon:100171874; -.
DR CTD; 59343; -.
DR eggNOG; KOG0778; Eukaryota.
DR InParanoid; Q5R7K7; -.
DR OrthoDB; 1480705at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0016929; F:deSUMOylase activity; ISS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0016926; P:protein desumoylation; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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..589
FT /note="Sentrin-specific protease 2"
FT /id="PRO_0000267606"
FT REGION 71..382
FT /note="Axin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT REGION 148..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..559
FT /note="Protease"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT MOTIF 28..31
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 46..51
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 317..332
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT COMPBIAS 192..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 478
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT ACT_SITE 495
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT ACT_SITE 548
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 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT CONFLICT 417
FT /note="N -> NF (in Ref. 1; CAH90084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 68057 MW; 8B03391F2121C7C8 CRC64;
MYRWLVRILG TIFRFCDRSV PPARALLKRR RSDSTLFSTV DTDEIPAKRP RLDCFIHQVK
NSLYNAASLF GFPFQLTTKP MVTSACNGTR NVAPSGEVFS NPSSCELTGS GSWNNMLKLG
NKSPNGISDY PKIRVTVTRD QPRRVLPSFG FTLNSEGYNR RPGGRRHSKG NPESSLMWKP
QEQAVTEMIS EESGKGLRRP HRTVEEGVQK EEREKYRKLL ERLKESGHGN SVCPVTSNYH
SSQRSQMDTL KTKGWGEEQN HGVKTTQFVP KQYRLVETRG PLCSLRSEKR CSKGKITDTE
KMVGIRFENE SRRGYQLEPD LSEEVSARLR LGSGSNGLLR RKVSIIETKE KNCSGKERDR
RTDDLLELTE DMEKEISNAL GHGPQDEILS SAFKLRITRG DIQTLKNYHW LNDEVINFYM
NLLVERNKKQ GYPALHVFST FFYPKLKSGG YQAVKRWTKG VNLFEQEIIL VPIHRKVHWS
LVVIDLRKKC LKYLDSMGQK GHRICEILLQ YLQDESKTKR NIDLNLLEWT HYSMKPHEIP
QQLNGSDCGM FTCKYADYIS RDKPITFTQH QMPLFRKKMV WEILHQQLL
