SENP1_PONAB
ID SENP1_PONAB Reviewed; 645 AA.
AC Q5RBB1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Sentrin-specific protease 1;
DE EC=3.4.22.-;
DE AltName: Full=Sentrin/SUMO-specific protease SENP1;
GN Name=SENP1;
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. Deconjugates SUMO1 from
CC HIPK2. Deconjugates SUMO1 from HDAC1 and BHLHE40/DEC1, which decreases
CC its transcriptional repression activity. Deconjugates SUMO1 from CLOCK,
CC which decreases its transcriptional activation activity. Deconjugates
CC SUMO2 from MTA1. Deconjugates SUMO2 from MTA1 (By similarity).
CC Deconjugates SUMO1 from METTL3. Desumoylates CCAR2 which decreases its
CC interaction with SIRT1. Deconjugates SUMO1 from GPS2.
CC {ECO:0000250|UniProtKB:Q9P0U3}.
CC -!- SUBUNIT: Interacts with MTA1. Interacts with CCAR2 (via N-terminus).
CC {ECO:0000250|UniProtKB:Q9P0U3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9P0U3}. Cytoplasm
CC {ECO:0000250}. Note=Shuttles between cytoplasm and nucleus.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR EMBL; CR858740; CAH90949.1; -; mRNA.
DR RefSeq; NP_001129011.1; NM_001135539.1.
DR RefSeq; XP_009245938.1; XM_009247663.1.
DR AlphaFoldDB; Q5RBB1; -.
DR BMRB; Q5RBB1; -.
DR SMR; Q5RBB1; -.
DR STRING; 9601.ENSPPYP00000005082; -.
DR MEROPS; C48.002; -.
DR Ensembl; ENSPPYT00000005282; ENSPPYP00000005082; ENSPPYG00000004452.
DR GeneID; 100190851; -.
DR KEGG; pon:100190851; -.
DR CTD; 29843; -.
DR eggNOG; KOG0778; Eukaryota.
DR GeneTree; ENSGT00940000155489; -.
DR InParanoid; Q5RBB1; -.
DR OrthoDB; 1480705at2759; -.
DR Proteomes; UP000001595; Chromosome 12.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016929; F:deSUMOylase activity; ISS:UniProtKB.
DR GO; GO:0016926; P:protein desumoylation; ISS:UniProtKB.
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; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..645
FT /note="Sentrin-specific protease 1"
FT /id="PRO_0000267605"
FT REGION 1..200
FT /note="Interaction with CCAR2"
FT /evidence="ECO:0000250|UniProtKB:Q9P0U3"
FT REGION 92..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..615
FT /note="Protease"
FT /evidence="ECO:0000250"
FT MOTIF 171..177
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 575..578
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 629..635
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 636..645
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT ACT_SITE 534
FT /evidence="ECO:0000250"
FT ACT_SITE 551
FT /evidence="ECO:0000250"
FT ACT_SITE 604
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0U3"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0U3"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0U3"
SQ SEQUENCE 645 AA; 73604 MW; C0FC170E881D1932 CRC64;
MDDIADRMRM DAGEVTLVNH NSVFKTHLLP QTGFPEDQLS LSDQQILSSR QGYLDRSFTC
STRSAAYNPS YYSDNPSSDS FLGSGDLRTF GQSANGQWRN STPSSSSSLQ KSRNSRSLYL
ETRKTSSGLS NIFAGKSNHH CHVSAYEKSF PIKPVPSPSW SGSCRRSLLS PKKTQRRHVS
TAEETVQEEE REIYRQLLQM VTGKQFTIAK PTTHFPLHLS RCLSSSKNTL KDSLFKNGNS
CASQIIGSDT SSSGSASILT NQEQLSHSVY SLSSYTPDVV AFGSKDSGTL HHPHHHHSVP
HQPDNLAASN TQSEGSDSVI LLKVKDSQTP TPSSTFFQAE LWIKELTSVY DSRARERLRQ
IEEQKALALQ LQNQRLQERE HSVHDSVELH LRVPLEKEIP VTVAQETQKK GHKLTDSEDE
FPEITEEMEK EIKNVFRNGN QDEVLSEAFR LTITRKDIQT LNHLNWLNDE IINFYMNMLM
ERSKEKGLPS VHAFNTFFFT KLKTAGYQAV KRWTKKVDVF SVDILLVPIH LGVHWCLAVV
DFRKKNITYY DSMGGINNEA CRILLQYLKQ ESIDKKRKEF DTNGWQLFSK KSQEIPQQMN
GSDCGMFACK YADCITKDRP INFTQQHMPY FRKRMVWEIL HRKLL
