SENP1_MOUSE
ID SENP1_MOUSE Reviewed; 640 AA.
AC P59110; Q8BTV5; Q8BZF1;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Sentrin-specific protease 1;
DE EC=3.4.22.- {ECO:0000269|PubMed:29499132};
DE AltName: Full=SUMO-1 protease 2;
DE Short=SuPr-2;
DE AltName: Full=Sentrin/SUMO-specific protease SENP1;
GN Name=Senp1; Synonyms=Supr2;
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 STRAIN=C57BL/6J; TISSUE=Skin;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary cancer;
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 [3]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15923632; DOI=10.1128/mcb.25.12.5171-5182.2005;
RA Yamaguchi T., Sharma P., Athanasiou M., Kumar A., Yamada S., Kuehn M.R.;
RT "Mutation of SENP1/SuPr-2 reveals an essential role for desumoylation in
RT mouse development.";
RL Mol. Cell. Biol. 25:5171-5182(2005).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29499132; DOI=10.1016/j.molcel.2018.01.037;
RA Cardamone M.D., Tanasa B., Cederquist C.T., Huang J., Mahdaviani K., Li W.,
RA Rosenfeld M.G., Liesa M., Perissi V.;
RT "Mitochondrial retrograde signaling in mammals is mediated by the
RT transcriptional cofactor GPS2 via direct mitochondria-to-nucleus
RT translocation.";
RL Mol. Cell 69:757-772(2018).
CC -!- FUNCTION: Protease that catalyzes two essential functions in the SUMO
CC pathway (PubMed:15923632, PubMed:29499132). The first is the hydrolysis
CC of an alpha-linked peptide bond at the C-terminal end of the small
CC ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3
CC leading to the mature form of the proteins. The second is the
CC deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by
CC cleaving an epsilon-linked peptide bond between the C-terminal glycine
CC of the mature SUMO and the lysine epsilon-amino group of the target
CC protein. Deconjugates SUMO1 from HIPK2 (By similarity). Deconjugates
CC SUMO1 from HDAC1 and BHLHE40/DEC1, which decreases its transcriptional
CC repression activity (By similarity). Deconjugates SUMO1 from CLOCK,
CC which decreases its transcriptional activation activity (By
CC similarity). Deconjugates SUMO2 from MTA1 (By similarity). Deconjugates
CC SUMO2 from MTA1 (By similarity). Deconjugates SUMO1 from METTL3 (By
CC similarity). Desumoylates CCAR2 which decreases its interaction with
CC SIRT1 (By similarity). Deconjugates SUMO1 from GPS2 (PubMed:29499132).
CC {ECO:0000250|UniProtKB:Q9P0U3, ECO:0000269|PubMed:15923632,
CC ECO:0000269|PubMed:29499132}.
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 -!- DEVELOPMENTAL STAGE: Expression starts at 9.5 dpc.
CC {ECO:0000269|PubMed:15923632}.
CC -!- DISRUPTION PHENOTYPE: Death between 13.5 dpc and 14.5 dpc due to
CC abnormalities in fetal vessels. {ECO:0000269|PubMed:15923632}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR EMBL; AK028565; BAC26011.1; -; mRNA.
DR EMBL; AK035581; BAC29112.1; -; mRNA.
DR EMBL; AK088597; BAC40442.1; -; mRNA.
DR EMBL; BC023129; AAH23129.1; -; mRNA.
DR CCDS; CCDS49717.1; -.
DR RefSeq; NP_659100.1; NM_144851.5.
DR AlphaFoldDB; P59110; -.
DR BMRB; P59110; -.
DR SMR; P59110; -.
DR BioGRID; 230207; 6.
DR IntAct; P59110; 1.
DR STRING; 10090.ENSMUSP00000046598; -.
DR MEROPS; C48.002; -.
DR iPTMnet; P59110; -.
DR PhosphoSitePlus; P59110; -.
DR EPD; P59110; -.
DR jPOST; P59110; -.
DR MaxQB; P59110; -.
DR PaxDb; P59110; -.
DR PRIDE; P59110; -.
DR ProteomicsDB; 261318; -.
DR Antibodypedia; 1710; 448 antibodies from 38 providers.
DR DNASU; 223870; -.
DR Ensembl; ENSMUST00000044189; ENSMUSP00000046598; ENSMUSG00000033075.
DR GeneID; 223870; -.
DR KEGG; mmu:223870; -.
DR UCSC; uc007xls.3; mouse.
DR CTD; 29843; -.
DR MGI; MGI:2445054; Senp1.
DR VEuPathDB; HostDB:ENSMUSG00000033075; -.
DR eggNOG; KOG0778; Eukaryota.
DR GeneTree; ENSGT00940000155489; -.
DR InParanoid; P59110; -.
DR OMA; MIWESEN; -.
DR OrthoDB; 1480705at2759; -.
DR PhylomeDB; P59110; -.
DR TreeFam; TF316289; -.
DR BRENDA; 3.4.22.B70; 3474.
DR Reactome; R-MMU-3065679; SUMO is proteolytically processed.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 223870; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Senp1; mouse.
DR PRO; PR:P59110; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P59110; protein.
DR Bgee; ENSMUSG00000033075; Expressed in animal zygote and 228 other tissues.
DR ExpressionAtlas; P59110; baseline and differential.
DR Genevisible; P59110; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016929; F:deSUMOylase activity; IDA:MGI.
DR GO; GO:0070139; F:SUMO-specific endopeptidase activity; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:0016926; P:protein desumoylation; IDA:UniProtKB.
DR GO; GO:0010724; P:regulation of definitive erythrocyte differentiation; IMP:MGI.
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; Developmental protein; Hydrolase; Nucleus; Phosphoprotein;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..640
FT /note="Sentrin-specific protease 1"
FT /id="PRO_0000101717"
FT REGION 1..200
FT /note="Interaction with CCAR2"
FT /evidence="ECO:0000250|UniProtKB:Q9P0U3"
FT REGION 19..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..610
FT /note="Protease"
FT MOTIF 171..177
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 570..573
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 624..630
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 631..640
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 37..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 529
FT /evidence="ECO:0000250"
FT ACT_SITE 546
FT /evidence="ECO:0000250"
FT ACT_SITE 599
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"
FT CONFLICT 432
FT /note="R -> H (in Ref. 1; BAC40442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 640 AA; 72511 MW; 59B6BB70268A0477 CRC64;
MDDTADGVKM DAGEVTLVNH GSTFRTHRPP QSGFPEEQLL LSDQQSLPFR QGTLDGSFTC
STRSPAYRPD YHSDNPSSDS FLGSGDVRTF GQSANGQWRN STPASGSAPQ KPRNSRSLCL
ETRKTSSGLS NTFVGKSNHH CHMSAYEKSF PIKPAPSPSW SGSCRRSLLS PKKTQRRHFS
TAEETVQEEE KEIYRQLLQM VTGKQFCVAK PTTHFPLRLS RCLSSNKNSL KDSLLRNGNS
CASHVIGSDT SSSGSASILT AQEQLSHSAH SLSSGTPDVA FGSKDSDPHH HLAAPHQPNS
LPASNTQSEG SDSVILLKVK ESQTPASSPT FFQAELWIKE LTSVYDSRAR ERLRRIEEQK
ALALQLQNQR LQEQEHAVLD SVELHLRVPL EKEIPVTAAQ ETRKKSHQLT DSEDEFPEIT
EEMEKEIKNV FRNGNQDEVL SEAFRLTITR KDIQTLNHLN WLNDEIINFY MNMLMERSKE
KGFPSVHAFN TFFFTKLKTA GYQAVKRWTK KVDVFSVDIL LVPIHLGVHW CLAVVDFRRK
SITYYDSMGG INNEACRILL QYLKQESVDK KRKEFDTNGW QLFSKKSQEI PQQMNGSDCG
MFACKYADCI TKDRPINFTQ QHMPYFRKRM VWEILHRKLL
