USPL1_MOUSE
ID USPL1_MOUSE Reviewed; 1089 AA.
AC Q3ULM6; Q0P689; Q3TT12; Q3V2W0; Q5RJG8; Q8BHR4;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=SUMO-specific isopeptidase USPL1;
DE EC=3.4.22.-;
DE AltName: Full=Ubiquitin-specific peptidase-like protein 1;
GN Name=Uspl1;
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] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Thymus;
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] (ISOFORM 4).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Eye, and Mammary tumor;
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: SUMO-specific isopeptidase involved in protein desumoylation.
CC Specifically binds SUMO proteins with a higher affinity for SUMO2 and
CC SUMO3 which it cleaves more efficiently. Also able to process full-
CC length SUMO proteins to their mature forms (By similarity). Plays a key
CC role in RNA polymerase-II-mediated snRNA transcription in the Cajal
CC bodies (By similarity). Is a component of complexes that can bind to U
CC snRNA genes (By similarity). {ECO:0000250|UniProtKB:Q5W0Q7}.
CC -!- SUBUNIT: Interacts with ELL. {ECO:0000250|UniProtKB:Q5W0Q7}.
CC -!- SUBCELLULAR LOCATION: Nucleus, Cajal body {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q3ULM6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3ULM6-2; Sequence=VSP_023480;
CC Name=3;
CC IsoId=Q3ULM6-3; Sequence=VSP_023480, VSP_023481, VSP_023482;
CC Name=4;
CC IsoId=Q3ULM6-4; Sequence=VSP_023481, VSP_023482;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- CAUTION: Probably inactive as a hydrolase due to lack of catalytic Cys
CC and His. {ECO:0000305}.
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DR EMBL; AK050969; BAC34481.2; -; mRNA.
DR EMBL; AK088787; BAE43395.1; -; mRNA.
DR EMBL; AK145409; BAE26422.1; -; mRNA.
DR EMBL; AK161654; BAE36513.1; -; mRNA.
DR EMBL; BC028849; AAH28849.1; -; mRNA.
DR EMBL; BC086664; AAH86664.1; -; mRNA.
DR CCDS; CCDS39406.1; -. [Q3ULM6-4]
DR CCDS; CCDS51704.1; -. [Q3ULM6-1]
DR CCDS; CCDS51705.1; -. [Q3ULM6-3]
DR CCDS; CCDS51706.1; -. [Q3ULM6-2]
DR RefSeq; NP_001013396.2; NM_001013378.2. [Q3ULM6-4]
DR RefSeq; NP_001108621.1; NM_001115149.1.
DR RefSeq; NP_001108622.1; NM_001115150.1.
DR RefSeq; NP_001108623.1; NM_001115151.1. [Q3ULM6-3]
DR RefSeq; NP_001108625.1; NM_001115153.1.
DR RefSeq; NP_001273753.1; NM_001286824.1.
DR RefSeq; NP_001273754.1; NM_001286825.1.
DR RefSeq; XP_017176366.1; XM_017320877.1.
DR AlphaFoldDB; Q3ULM6; -.
DR BioGRID; 231197; 1.
DR STRING; 10090.ENSMUSP00000113247; -.
DR MEROPS; C98.001; -.
DR PhosphoSitePlus; Q3ULM6; -.
DR PaxDb; Q3ULM6; -.
DR PRIDE; Q3ULM6; -.
DR ProteomicsDB; 299658; -. [Q3ULM6-1]
DR ProteomicsDB; 299659; -. [Q3ULM6-2]
DR ProteomicsDB; 299661; -. [Q3ULM6-4]
DR Antibodypedia; 22766; 21 antibodies from 10 providers.
DR Ensembl; ENSMUST00000100410; ENSMUSP00000097978; ENSMUSG00000041264. [Q3ULM6-4]
DR Ensembl; ENSMUST00000117878; ENSMUSP00000113176; ENSMUSG00000041264. [Q3ULM6-3]
DR GeneID; 231915; -.
DR KEGG; mmu:231915; -.
DR UCSC; uc009apl.2; mouse. [Q3ULM6-4]
DR UCSC; uc009apm.2; mouse. [Q3ULM6-3]
DR CTD; 10208; -.
DR MGI; MGI:2442342; Uspl1.
DR VEuPathDB; HostDB:ENSMUSG00000041264; -.
DR eggNOG; ENOG502QRFM; Eukaryota.
DR GeneTree; ENSGT00390000002316; -.
DR HOGENOM; CLU_526705_0_0_1; -.
DR InParanoid; Q3ULM6; -.
DR OrthoDB; 204698at2759; -.
DR PhylomeDB; Q3ULM6; -.
DR BioGRID-ORCS; 231915; 21 hits in 74 CRISPR screens.
DR ChiTaRS; Uspl1; mouse.
DR PRO; PR:Q3ULM6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q3ULM6; protein.
DR Bgee; ENSMUSG00000041264; Expressed in manus and 222 other tissues.
DR ExpressionAtlas; Q3ULM6; baseline and differential.
DR Genevisible; Q3ULM6; MM.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0016929; F:deSUMOylase activity; ISS:UniProtKB.
DR GO; GO:0032183; F:SUMO binding; ISS:UniProtKB.
DR GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR GO; GO:0030576; P:Cajal body organization; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0016926; P:protein desumoylation; ISS:UniProtKB.
DR GO; GO:0009301; P:snRNA transcription; ISO:MGI.
DR InterPro; IPR029388; DUF4650.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR028890; Peptidase_C98.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR033505; USPL1.
DR PANTHER; PTHR15294; PTHR15294; 1.
DR Pfam; PF15509; DUF4650; 1.
DR Pfam; PF15499; Peptidase_C98; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease.
FT CHAIN 1..1089
FT /note="SUMO-specific isopeptidase USPL1"
FT /id="PRO_0000279527"
FT DOMAIN 215..488
FT /note="USP"
FT REGION 90..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..483
FT /note="SUMO-binding"
FT /evidence="ECO:0000250"
FT REGION 687..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 224
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 444
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Q7"
FT VAR_SEQ 1..199
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023480"
FT VAR_SEQ 512..517
FT /note="EEQPTC -> IEVPGN (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023481"
FT VAR_SEQ 518..1089
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023482"
FT CONFLICT 47
FT /note="C -> S (in Ref. 2; AAH86664)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="A -> V (in Ref. 2; AAH28849)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="Q -> R (in Ref. 1; BAE26422)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="L -> P (in Ref. 2; AAH28849)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="D -> G (in Ref. 2; AAH28849)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="D -> A (in Ref. 2; AAH28849)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="A -> V (in Ref. 2; AAH28849)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="I -> V (in Ref. 2; AAH28849)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="A -> V (in Ref. 2; AAH28849)"
FT /evidence="ECO:0000305"
FT CONFLICT 1014
FT /note="L -> Q (in Ref. 1; BAE43395)"
FT /evidence="ECO:0000305"
FT CONFLICT Q3ULM6-4:514
FT /note="V -> A (in Ref. 2; AAH28849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1089 AA; 118390 MW; ABECA307AB47F129 CRC64;
MTDDSLKIGN GLPLVGPGTD VGISSLPMLG YLGKNYASAK VTTDGHCPAC RAKGKLSALK
PYRISFQESV FLCEDLQCIY PLGSESLTNL ISPDSEDCPT PSKPQKRKRL ETNCRNSPLP
VHSKKTRSHI VTDSEPIVNG KYNGEVCDDF SASFPDTSAH QDPASTAASV EQSEALEADD
VVVAATEDPA TVSVTSELEM PAKSRCLPLC QTLCVQWKNT QALCWLDCIL SALVHLEVLR
KTVLEACSRE ECVFGRLFEM YHQADELLHT HHLHGVTGED CKKLTSEIFT EIDTCLNKVR
DEIFAKLQPK LRCTLGDMES PVFALPVLLK LEPHVESLFT YSFSWNFECS HCGHQYQNRC
VKSLVTFTNI VPEWHPLNAA HFGPCNSCNS KSQIRKMVLE RASPILMLHF VEGLPRRDLQ
HYAFHFEGSL YQVTSVIQYQ ANNHFITWFL DADGSWLECD DLKGPCAKRH VTCEVPASET
HIVIWERKSQ VPIEEAACLP CMKPNVQPVS GEEQPTCPAL CSLAGTATSE PSVAHPTSMA
GAPQTLPEIQ AVAHGDSVLS GAKGMVDSIL PSALEETIQE TASVSQVDSK DCLLEDKPVA
GSAALVRVLA FQPQDSPGSS GSSLVSSLCE GKLVAPCVDS SFPSQAVSTD LQAVLSQAGD
TVVPNPVTDA PVPVLVQELK SLATEKDSQT QLLPLKTEKL DPEQPGKSQA SNLRKRETTA
SSKTVAARSA QNQPRKEDQK RAFVGSWVKG LLSRGGAFMP TCVLSQSRAV SDLQPSVKGA
SNFDGFKTKS ISRRSKRMSR KAKHMEELSP RNSSPPLSWT AALTQAAENA TSALLREQEG
SRPAPLRHRS PGNESAISPA SRGDAAEDQV HKLRLKLLKK LKAKKKKLAA LISSPHREPS
LSDHSEPASH CGTPASDQSE PVSHCGSPND CESIEDLLKE LQHQIDLADS KSGCTSAPDA
TSNNSQSHEE ILAELLSPTA MSEPSESGEL ELRYLEMGDS TPAQAPSEFS VVSLNTCLKQ
DHDYCSPEKG QREVDLHSVM DSACIRTLNL GSPMKTDIFD DFFSTSALNS LTNDTLDIPH
FDDSLFENC
