ID   F1LVT6_RAT              Unreviewed;       645 AA.
AC   F1LVT6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=SUMO specific peptidase 1 {ECO:0000313|Ensembl:ENSRNOP00000031127.5};
GN   Name=Senp1 {ECO:0000313|Ensembl:ENSRNOP00000031127.5,
GN   ECO:0000313|RGD:1310275};
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 {ECO:0000313|Ensembl:ENSRNOP00000031127.5, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000031127.5, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000031127.5,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000031127.5}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000031127.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase C48 family.
CC       {ECO:0000256|ARBA:ARBA00005234}.
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DR   RefSeq; XP_017458989.1; XM_017603500.1.
DR   AlphaFoldDB; F1LVT6; -.
DR   STRING; 10116.ENSRNOP00000031127; -.
DR   MEROPS; C48.002; -.
DR   PaxDb; 10116-ENSRNOP00000031127; -.
DR   Ensembl; ENSRNOT00000030943.7; ENSRNOP00000031127.5; ENSRNOG00000022260.7.
DR   AGR; RGD:1310275; -.
DR   RGD; 1310275; Senp1.
DR   VEuPathDB; HostDB:ENSRNOG00000022260; -.
DR   eggNOG; KOG0778; Eukaryota.
DR   GeneTree; ENSGT00940000155489; -.
DR   HOGENOM; CLU_022541_0_0_1; -.
DR   InParanoid; F1LVT6; -.
DR   PhylomeDB; F1LVT6; -.
DR   TreeFam; TF316289; -.
DR   Reactome; R-RNO-3065679; SUMO is proteolytically processed.
DR   Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000022260; Expressed in spleen and 18 other cell types or tissues.
DR   ExpressionAtlas; F1LVT6; baseline.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016929; F:deSUMOylase activity; ISO:RGD.
DR   GO; GO:0070139; F:SUMO-specific endopeptidase activity; ISO:RGD.
DR   GO; GO:0097190; P:apoptotic signaling pathway; ISO:RGD.
DR   GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD.
DR   GO; GO:0016926; P:protein desumoylation; ISO:RGD.
DR   GO; GO:0010724; P:regulation of definitive erythrocyte differentiation; ISO:RGD.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR003653; Peptidase_C48_C.
DR   PANTHER; PTHR12606:SF30; SENTRIN-SPECIFIC PROTEASE 1; 1.
DR   PANTHER; PTHR12606; SENTRIN/SUMO-SPECIFIC PROTEASE; 1.
DR   Pfam; PF02902; Peptidase_C48; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50600; ULP_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW   Protease {ECO:0000256|ARBA:ARBA00022807};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT   DOMAIN          451..615
FT                   /note="Ubiquitin-like protease family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50600"
FT   REGION          70..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   645 AA;  72861 MW;  E064EE304A89B855 CRC64;
     MWSLSLEDTA DGVKMDAGEV TLVNHSSAFR AHLLPHSGFP EDQLALSDQQ ILPFRQGTLH
     RAFTGSTSSA AYNPDYHSDN PSSDSFLGSG DIRTFGQSAN GQWRNSTPAS GSALQKPRNS
     RSLYLETRKT SSGLSNTFVG KSNHHCHVSA YEKSFPIKPA PSPSWSGSCR RSLLSPKKTQ
     RRHFSTAEET VQEEEKEIYR QLLQMVTGKQ FSVAKPTTHF PLHLSRCLSS NKNSLKDSLL
     RNGNSCASHV IGSDTSSSGS ASILTAQEQL SHSAHSLISG TPDVAFGSKD SALHHHLSAP
     HQPDSLPASN PQSEGSDSVI LLKVKESQTP ASSPTFFQAE LWIKELTSVY DSRARERLRQ
     IEEQKALALQ LQNQRLQEQE HAVLDSVELH LRVPLEKEVP VTAAQETRKK SHQLTDSEDE
     FPEITEEMEK EIKNVFRNGN QDEVLSEAFR LTITRKDIQT LNHLNWLNDE IINFYMNMLM
     ERSKEKGFPS VHAFNTFFFT KLKAAGYQAV KRWTKKVDVF SVDILLVPIH LGVHWCLAVV
     DFRKKSVTYY DSMGGVNNEA CRILLQYLKQ ESVDKKRKEF DTNGWQLFSK KSQEIPQQMN
     GSDCGMFACK YADCITKDRP INFTQQHMPY FRKRMVWEIL HRKLL
//