SENP7_BOVIN
ID SENP7_BOVIN Reviewed; 1047 AA.
AC A7MBJ2;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; BC151590; AAI51591.1; -; mRNA.
DR RefSeq; NP_001095358.1; NM_001101888.2.
DR RefSeq; XP_005201280.1; XM_005201223.3.
DR AlphaFoldDB; A7MBJ2; -.
DR SMR; A7MBJ2; -.
DR STRING; 9913.ENSBTAP00000022522; -.
DR MEROPS; C48.009; -.
DR PaxDb; A7MBJ2; -.
DR PRIDE; A7MBJ2; -.
DR Ensembl; ENSBTAT00000022522; ENSBTAP00000022522; ENSBTAG00000016932.
DR GeneID; 507820; -.
DR KEGG; bta:507820; -.
DR CTD; 57337; -.
DR VEuPathDB; HostDB:ENSBTAG00000016932; -.
DR VGNC; VGNC:52825; SENP7.
DR eggNOG; KOG0779; Eukaryota.
DR GeneTree; ENSGT00940000157308; -.
DR HOGENOM; CLU_011967_0_0_1; -.
DR InParanoid; A7MBJ2; -.
DR OMA; PLQWKRS; -.
DR OrthoDB; 1241636at2759; -.
DR TreeFam; TF350136; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000016932; Expressed in neutrophil and 109 other tissues.
DR ExpressionAtlas; A7MBJ2; baseline and differential.
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 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Immunity; Innate immunity; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1047
FT /note="Sentrin-specific protease 7"
FT /id="PRO_0000395501"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..1047
FT /note="Protease"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT REGION 883..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 857
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT ACT_SITE 936
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT ACT_SITE 989
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQF6"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BUH8"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQF6"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQF6"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQF6"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQF6"
SQ SEQUENCE 1047 AA; 118889 MW; BD79A921437E86CF CRC64;
MDKGKAGRRR SSAEIVTEGK RKKPSSSELH KITKILNAKP EDVHVQSPLS KLRSSEHWDV
SLQGWKRSLR NKVLSLDHKS KKGVRGHPVT SKISPERQLK VMLTNVLWTD LGRKFRKTLP
RNDANLCDAN KVQSDSLPST SVDSLETCQK LEPLHQSLNL SERIPRVILT NVLGTKLGRK
YIKTSSVTEA NLGDTDNLQS EQLSSSSDGS LESCQNLNPH KNFFLSESSS QSSKTDNYAK
QTSYTKEKRR DDDGISFMSD TQPKDLSSGS RDCDHLEVGS RNKDDTNSVS RMEPTLISRK
RKKRLRSNLP DTHNPASLYK SAEQTKEQEN DPAVFTELEK SSENYHEDPK LFEEVTYESI
ESDFAQLPSD CGQELALSAS PQMTSGCSAM ETFESSISSD TVGNSTLVVK DENELNTIEK
PVLSEHSEGN LSFISAEPIV VSSDEEGPTE QKSSEILKLQ PKQDDAISHE SESTSEPVVS
ELPLITCESV QTSSELCSYN PVMENISCLI PKNEMDLQLD FIFTSVYIGK IKGASKGCVT
FTTKYIKIPF QVSVHEISLL VDTTHLKRFG LWKNKDDDHS KKSHAILFLW VSSNYLQEIQ
TQLENSVFSQ QSKSTEFIFL ELHSSISQRE ELKLKDIMTE ISTTNGELEL SYPLSWVQAL
PLFQNLSSKE SSFIHYYCAS TCSFPAATTE EMKMKSVSQP SNTDTAKPTY TLLQKQSSGC
YSLSITSNPD EEWREVRHTG PVQKLIVYPP PPTKGGLGVT NEDLECLEEG EFLNDVIIDF
YLKYLILEKA SDELVERSHI FSSFFYKCLT RKENNLTEDN PNLSMAQRRH KRVRTWTRHI
NIFNKDYIFV PVNESSHWYL AVICFPWLEE VVYEDFPQTI PQYSQAEESH HDSRTIDNDL
HTSSALSSGT EDSQSPEMNV TVPKKMCKRP CILILDSLKA ASIQNTVQNL REYLEVEWEV
KRKTHREFSK TNMVDLCPKV PKQDNSSDCG VYLLQYVESF FKDPIVNFEL PIHLEKWFPR
HVIKTKREDI RELILKLHLQ QQKGSSS
