SENP5_MOUSE
ID SENP5_MOUSE Reviewed; 749 AA.
AC Q6NXL6; Q3ZTK4; Q8BXW0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Sentrin-specific protease 5;
DE EC=3.4.22.-;
DE AltName: Full=SUMO/Smt3-specific isopeptidase 3;
DE Short=Smt3ip3;
DE AltName: Full=Sentrin/SUMO-specific protease SENP5;
GN Name=Senp5; Synonyms=Smt3ip3;
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 [MRNA].
RC STRAIN=BALB/cJ;
RA Nishida T., Miwa T., Yasuda H.;
RT "SMT3IP3, a novel SUMO/Smt3-specific protease that specifically removes
RT SUMO-2/3 from conjugated proteins.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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=Brain, and Embryo;
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).
CC -!- FUNCTION: Protease that catalyzes two essential functions in the SUMO
CC pathway: processing of full-length SUMO3 to its mature form and
CC deconjugation of SUMO2 and SUMO3 from targeted proteins. Has weak
CC proteolytic activity against full-length SUMO1 or SUMO1 conjugates.
CC Required for cell division. {ECO:0000250|UniProtKB:Q96HI0}.
CC -!- SUBUNIT: Interacts with CCAR2. {ECO:0000250|UniProtKB:Q96HI0}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR EMBL; AY522918; AAT01901.1; -; mRNA.
DR EMBL; AK043171; BAC31483.1; -; mRNA.
DR EMBL; BC067014; AAH67014.1; -; mRNA.
DR EMBL; BC080830; AAH80830.1; -; mRNA.
DR CCDS; CCDS28111.1; -.
DR RefSeq; NP_796077.2; NM_177103.4.
DR RefSeq; XP_006522301.1; XM_006522238.3.
DR RefSeq; XP_006522302.1; XM_006522239.3.
DR RefSeq; XP_011244235.1; XM_011245933.2.
DR AlphaFoldDB; Q6NXL6; -.
DR SMR; Q6NXL6; -.
DR STRING; 10090.ENSMUSP00000023457; -.
DR iPTMnet; Q6NXL6; -.
DR PhosphoSitePlus; Q6NXL6; -.
DR EPD; Q6NXL6; -.
DR MaxQB; Q6NXL6; -.
DR PaxDb; Q6NXL6; -.
DR PRIDE; Q6NXL6; -.
DR ProteomicsDB; 261319; -.
DR Antibodypedia; 33951; 334 antibodies from 31 providers.
DR DNASU; 320213; -.
DR Ensembl; ENSMUST00000023457; ENSMUSP00000023457; ENSMUSG00000022772.
DR Ensembl; ENSMUST00000231360; ENSMUSP00000156109; ENSMUSG00000022772.
DR GeneID; 320213; -.
DR KEGG; mmu:320213; -.
DR UCSC; uc007yya.2; mouse.
DR CTD; 205564; -.
DR MGI; MGI:2443596; Senp5.
DR VEuPathDB; HostDB:ENSMUSG00000022772; -.
DR eggNOG; KOG0778; Eukaryota.
DR GeneTree; ENSGT00940000159865; -.
DR HOGENOM; CLU_021414_1_0_1; -.
DR InParanoid; Q6NXL6; -.
DR OMA; QLRHFQC; -.
DR OrthoDB; 1480705at2759; -.
DR PhylomeDB; Q6NXL6; -.
DR TreeFam; TF316289; -.
DR BRENDA; 3.4.22.B73; 3474.
DR Reactome; R-MMU-3065679; SUMO is proteolytically processed.
DR BioGRID-ORCS; 320213; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Senp5; mouse.
DR PRO; PR:Q6NXL6; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q6NXL6; protein.
DR Bgee; ENSMUSG00000022772; Expressed in humerus cartilage element and 225 other tissues.
DR ExpressionAtlas; Q6NXL6; baseline and differential.
DR Genevisible; Q6NXL6; MM.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016929; F:deSUMOylase activity; IBA:GO_Central.
DR GO; GO:0070139; F:SUMO-specific endopeptidase activity; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016926; P:protein desumoylation; IBA:GO_Central.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR InterPro; IPR045577; SENP3_5_cons_dom.
DR InterPro; IPR033465; SENP5.
DR PANTHER; PTHR12606:SF10; PTHR12606:SF10; 1.
DR Pfam; PF02902; Peptidase_C48; 1.
DR Pfam; PF19722; SENP3_5_N; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Hydrolase; Nucleus; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..749
FT /note="Sentrin-specific protease 5"
FT /id="PRO_0000267607"
FT REGION 268..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..718
FT /note="Protease"
FT COMPBIAS 423..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 640
FT /evidence="ECO:0000250"
FT ACT_SITE 657
FT /evidence="ECO:0000250"
FT ACT_SITE 707
FT /evidence="ECO:0000250"
FT CONFLICT 51
FT /note="H -> P (in Ref. 2; BAC31483)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="V -> A (in Ref. 1; AAT01901)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="H -> R (in Ref. 1; AAT01901)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 749 AA; 86100 MW; 9356AC4FB3DE590C CRC64;
MKKQKKILWK KGIHLAFSEK WNAGFGSFKK FYFPQNLCFL KAKLGRPVAW HRQVKHFQCN
KGLHIQKTWI QDVPFCSKTK SGLATQNVST LYPKVKRKDS KHFISSSRSL LKLQADKLLS
SAKSLDHKYC REKSLLKAAP GLSANTVLGR ANGHEPTTDP QASDFPMKFS GESQSPGDSG
KTVVLNKHRK RVCHGCYQGL EHHRNRRPLI PKQFQLNQHR RVRASLMMYE KLSMIRFRYR
IFRSQHFRTK SRVCKLRKAQ RSWVQKVTGD HQENLRDNNT EGDNCNPVPS LEPKDPCRCQ
PYFPDMDSSA VGKGKNCHVP DGHTKENPVL DKEHGLDDTF PDQQNGCVAY NWDQSSSCPK
WECTEQIHEI PLMEHPSSDK FSPETERALM ALGQESGTSA VSDDREKLPV SGADKSVSSV
DGPVSEEPAQ NENFQMEEDG SLKQSILSSK LLDHPYCKSP LDAPLLCSEP KVENQMSGGK
SSQTASPVDD EQLSTCLSGF LDEVMKKYGS LVPLSEKDVL GRLKDVFNED FSNRKPFINR
EITNYRARHQ KCNFRIFYNK HMLDMDDLAT LDGQNWLNDQ VINMYGELIM DAVPDKVHFF
NSFFHRQLVT KGYNGVKRWT KKVDLFKKSL LLIPIHLEVH WSLITVTLSS RIISFYDSQG
IHFKFCVENI RKYLLTEARE KNRPEFLQGW QTAVTKCIPQ QKNDSDCGVF VLQYCKCLAL
EQPFQFSQED MPRVRKRIYK ELCECRLLD
