SENP7_MOUSE
ID SENP7_MOUSE Reviewed; 1037 AA.
AC Q8BUH8; Q6P398; Q80TA3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Sentrin-specific protease 7 {ECO:0000305};
DE EC=3.4.22.- {ECO:0000269|PubMed:28095500};
DE AltName: Full=SUMO-1-specific protease 2;
DE AltName: Full=Sentrin/SUMO-specific protease SENP7;
GN Name=Senp7 {ECO:0000303|PubMed:28095500, ECO:0000312|MGI:MGI:1913565};
GN Synonyms=Kiaa1707 {ECO:0000303|PubMed:12693553}, Susp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-434 AND SER-435, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACTIVE SITE, AND
RP MUTAGENESIS OF CYS-979.
RX PubMed=28095500; DOI=10.1371/journal.ppat.1006156;
RA Cui Y., Yu H., Zheng X., Peng R., Wang Q., Zhou Y., Wang R., Wang J.,
RA Qu B., Shen N., Guo Q., Liu X., Wang C.;
RT "SENP7 potentiates cGAS activation by relieving SUMO-mediated inhibition of
RT cytosolic DNA sensing.";
RL PLoS Pathog. 13:e1006156-e1006156(2017).
CC -!- FUNCTION: Protease that acts as a positive regulator of the cGAS-STING
CC pathway by catalyzing desumoylation of CGAS (PubMed:28095500).
CC Desumoylation of CGAS promotes DNA-binding activity of CGAS, subsequent
CC oligomerization and activation (PubMed:28095500). Deconjugates SUMO2
CC and SUMO3 from targeted proteins, but not SUMO1 (By similarity).
CC Catalyzes the deconjugation of poly-SUMO2 and poly-SUMO3 chains (By
CC similarity). Has very low efficiency in processing full-length SUMO
CC proteins to their mature forms (By similarity).
CC {ECO:0000250|UniProtKB:Q9BQF6, ECO:0000269|PubMed:28095500}.
CC -!- INTERACTION:
CC Q8BUH8; Q61686: Cbx5; NbExp=4; IntAct=EBI-15972382, EBI-307973;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28095500}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65824.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK122542; BAC65824.1; ALT_INIT; mRNA.
DR EMBL; AK085060; BAC39352.1; -; mRNA.
DR EMBL; BC058593; AAH58593.1; -; mRNA.
DR CCDS; CCDS28222.1; -.
DR RefSeq; NP_079759.2; NM_025483.4.
DR RefSeq; XP_011244296.1; XM_011245994.2.
DR AlphaFoldDB; Q8BUH8; -.
DR SMR; Q8BUH8; -.
DR BioGRID; 211378; 9.
DR DIP; DIP-60609N; -.
DR IntAct; Q8BUH8; 3.
DR STRING; 10090.ENSMUSP00000086779; -.
DR MEROPS; C48.009; -.
DR iPTMnet; Q8BUH8; -.
DR PhosphoSitePlus; Q8BUH8; -.
DR EPD; Q8BUH8; -.
DR jPOST; Q8BUH8; -.
DR MaxQB; Q8BUH8; -.
DR PaxDb; Q8BUH8; -.
DR PeptideAtlas; Q8BUH8; -.
DR PRIDE; Q8BUH8; -.
DR ProteomicsDB; 256547; -.
DR Antibodypedia; 15887; 247 antibodies from 29 providers.
DR DNASU; 66315; -.
DR Ensembl; ENSMUST00000089362; ENSMUSP00000086779; ENSMUSG00000052917.
DR GeneID; 66315; -.
DR KEGG; mmu:66315; -.
DR UCSC; uc007zmi.2; mouse.
DR CTD; 57337; -.
DR MGI; MGI:1913565; Senp7.
DR VEuPathDB; HostDB:ENSMUSG00000052917; -.
DR eggNOG; KOG0779; Eukaryota.
DR GeneTree; ENSGT00940000157308; -.
DR InParanoid; Q8BUH8; -.
DR OMA; PLQWKRS; -.
DR OrthoDB; 1241636at2759; -.
DR PhylomeDB; Q8BUH8; -.
DR TreeFam; TF350136; -.
DR BRENDA; 3.4.22.B75; 3474.
DR BioGRID-ORCS; 66315; 2 hits in 58 CRISPR screens.
DR ChiTaRS; Senp7; mouse.
DR PRO; PR:Q8BUH8; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BUH8; protein.
DR Bgee; ENSMUSG00000052917; Expressed in rostral migratory stream and 218 other tissues.
DR ExpressionAtlas; Q8BUH8; baseline and differential.
DR Genevisible; Q8BUH8; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0070139; F:SUMO-specific endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0140374; P:antiviral innate immune response; IDA:UniProtKB.
DR GO; GO:0016926; P:protein desumoylation; IDA: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; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1037
FT /note="Sentrin-specific protease 7"
FT /id="PRO_0000267609"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..399
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..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..909
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:0000305|PubMed:28095500"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZF42"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQF6"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 979
FT /note="C->S: Abolished protease activity and ability to
FT desumoylate CGAS."
FT /evidence="ECO:0000269|PubMed:28095500"
SQ SEQUENCE 1037 AA; 116346 MW; 35CAC29F61A293C5 CRC64;
MDRARPGRRR ASSEIVTEGK RKKSSPADLQ KITKLLTVKS EDVLAQSPLS KLRGSECWWT
RSLRNKVICL DHKKPKAARG CPPKGLPKRH LRVMLTNVLW TDLGREFRKT LPRKDANLCA
PSKVQSDSLP STSVDSIETC QRLDPLHQSL NLSERTPRVI LTDIRQTELG RKYLKIPPVT
EASLSDTANL KSEQLSSSSD GSLESCQSVN HHKSFLSESG PKPSRTGDVP AKEAACGGQK
QGDDGGVTPE MAAPHPKDFN TGNKGCDYLE EGTSNKNTSY SYSEMDHTPV SRKRKKRGRS
NFHDSHNSKT SLDKPTEHTK EEENDSSVSR KLEESGEDSH QDPAPPEGLA PESLESEATN
LRSFAAGQEP DASAASGRAS SPNKSLESSA SSEVSENSSV AVKGEALTLK EASPPGGSSE
ESQLLISAEP IVVSSDEEGP VEHKNSVILK LQPPHEIMSE NQGTSDPQLS ELTLGACESV
QVTSELFPYN PDVENISCIK SNSEMDLKLD FIFTCVYIGK IKGTPKGCVT FTKKYIKIPF
QVSTNEISLT VDTARLKRFG LWESKDEDHS KRSHAILFLW LSSDYLQDIQ TQLENPMLSQ
QSKANEFIFL ELNSSISQRE ELKLKDIMME ISTKNGNLHL SCPLPWVQAL PLFQDLSPQE
ISFLHYYYAS ASALPTAAGA DMKKKSVSQP SNSDTIKPTY TFLHKQSSGC YSLSITSSPE
EEWQEVRNTG PVQKLIVYPP PPTKGGLGVT NEDLECLEEG EFLNDVIIDF YLKYLLLEKA
SDELVERSHI FSSFFYKCLT RKENNLTEDN PDLSVAQRRH RRVRTWTRHI NIFNKDYIFV
PVNESSHWYL AVICFPWLEE AVYEDCPQTV SQQFQGQQSQ HDHKMTDNDP HTTSTVSTSA
EDSQSTEVNM SVPKKMCKRP CILILDSLKA ASIQNTVQNL REYLEVEWEV KRKTHREFSK
TNMVDLCPKV PKQDNSSDCG VYLLQYVESF FQDPIVNFEL PIHLEKWFPR HVIKTKREDI
RELILKLHLQ QQKGGSC
