SENP7_RAT
ID SENP7_RAT Reviewed; 1037 AA.
AC D3ZF42;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Sentrin-specific protease 7;
DE EC=3.4.22.- {ECO:0000250|UniProtKB:Q8BUH8};
DE AltName: Full=SUMO-1-specific protease 2;
DE AltName: Full=Sentrin/SUMO-specific protease SENP7;
GN Name=Senp7; Synonyms=Susp2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-13; SER-189; SER-432
RP AND SER-433, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Protease that acts as a positive regulator of the cGAS-STING
CC pathway by catalyzing desumoylation of CGAS. Desumoylation of CGAS
CC promotes DNA-binding activity of CGAS, subsequent oligomerization and
CC activation (By similarity). Deconjugates SUMO2 and SUMO3 from targeted
CC proteins, but not SUMO1. Catalyzes the deconjugation of poly-SUMO2 and
CC poly-SUMO3 chains. Has very low efficiency in processing full-length
CC SUMO proteins to their mature forms (By similarity).
CC {ECO:0000250|UniProtKB:Q8BUH8, ECO:0000250|UniProtKB:Q9BQF6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BUH8}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR EMBL; CH473967; EDM11051.1; -; Genomic_DNA.
DR RefSeq; NP_001099358.1; NM_001105888.1.
DR AlphaFoldDB; D3ZF42; -.
DR SMR; D3ZF42; -.
DR STRING; 10116.ENSRNOP00000043376; -.
DR MEROPS; C48.009; -.
DR iPTMnet; D3ZF42; -.
DR PhosphoSitePlus; D3ZF42; -.
DR PaxDb; D3ZF42; -.
DR PeptideAtlas; D3ZF42; -.
DR PRIDE; D3ZF42; -.
DR GeneID; 288167; -.
DR KEGG; rno:288167; -.
DR UCSC; RGD:1305510; rat.
DR CTD; 57337; -.
DR RGD; 1305510; Senp7.
DR VEuPathDB; HostDB:ENSRNOG00000001616; -.
DR eggNOG; KOG0779; Eukaryota.
DR HOGENOM; CLU_011967_0_0_1; -.
DR InParanoid; D3ZF42; -.
DR OMA; PLQWKRS; -.
DR OrthoDB; 1241636at2759; -.
DR PhylomeDB; D3ZF42; -.
DR TreeFam; TF350136; -.
DR PRO; PR:D3ZF42; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Proteomes; UP000234681; Chromosome 11.
DR Bgee; ENSRNOG00000001616; Expressed in thymus and 19 other tissues.
DR Genevisible; D3ZF42; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0070139; F:SUMO-specific endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0140374; P:antiviral innate immune response; 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 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Immunity; Innate immunity; Phosphoprotein; Protease;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..1037
FT /note="Sentrin-specific protease 7"
FT /id="PRO_0000395502"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..1037
FT /note="Protease"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT REGION 873..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 847
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT ACT_SITE 926
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT ACT_SITE 979
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQF6"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1037 AA; 116872 MW; 945C78977051CA27 CRC64;
MDRARPGRRR ASSEIVTEGK RKKSSPADLQ KITKLLTVKS EDVLAQSPLP KLRGSECWWT
RSLRNKVICL DHKTTKAAHG CPPKALPKRH LKVMLTNVLW TDLGREFRKT LPRNDAKLCD
TSKVQSDSLP STSVDSIETC QRLDPLHQSL NLSERIPRVI LTDIRQTELG RKYLKIPSVT
EASLSDTASP KSEELSSSAD GSLESCQNVN HLKSFLSERG SKPSRTGDIS AKEAANGRQE
QGDDGDIAPE MVTPQSKDFN SGNKGDYHEE GTSNKNTSYS HSETDHTPVS RKRKKRGRSN
FHNSHNPKSS VDKSTEYIKE EENESTVSSK LEESNEDSHQ DPAPPEGLTP DSLETEATNV
CSFVVQEPDV SAASGRACSP NKSSESSVSS EVAENSSAAE KGEASTVKEA PPPGGNSEEN
QLLMSAEPIV VSSDEEGPVE HKNSVILKLQ PSQDYEFMSE NQTTSDPQLS ELMLGACESV
QVSSELCPYN PDMENISCIN PNSEMDLKLD FIFTCVYIGK IKGTSKGCIT FTKKYIKIPF
QVSMNEISLT VDTARLKRFG LWESKDDDHS KRSHAILFLW VSSNYLQDIQ TQLENPMLSQ
QSKANEFIFL ELNSPISQRE ELKLKDIMME IGATNGELQL SCPLPWVQAF PLFQDLSPQE
ISFLHYYCAS ASSFPAVAGA DMKKKPVSQP SNADVVKPTY TFLHKQSSGC YSLSITSSPD
EEWREVRNTG PVQKLIVYPP PPTKGGLGVT NEDLECLEEG EFLNDVIIDF YLKYLLLEKA
SDELVERSHI FSSFFYKCLT RKENNLTEDN PDLSVAQRRH RRVRTWTRHI NIFNKDYIFV
PVNESSHWYL AVICFPWLEE AVYEDFPQTV SQEFQDQQSQ HDNKTIDNDP HTTSTVFTSA
EESQSTETSM SVPKKMCKRP CILILDSLKA ASIQNTVQNL REYLEVEWEV KRKTHREFSK
TNMVDLCPKV PKQDNSSDCG VYLLQYVESF FQDPIVNFEL PIHLEKWFPR HVIKTKREDI
RELILKLHLQ QQKGSSS
