USPL1_DANRE
ID USPL1_DANRE Reviewed; 1014 AA.
AC Q6DRC5; A8WFQ9; B0JZK5;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=15256591; DOI=10.1073/pnas.0403929101;
RA Amsterdam A., Nissen R.M., Sun Z., Swindell E.C., Farrington S.,
RA Hopkins N.;
RT "Identification of 315 genes essential for early zebrafish development.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12792-12797(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION IN PROTEIN DESUMOYLATION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22878415; DOI=10.1038/embor.2012.125;
RA Schulz S., Chachami G., Kozaczkiewicz L., Winter U., Stankovic-Valentin N.,
RA Haas P., Hofmann K., Urlaub H., Ovaa H., Wittbrodt J., Meulmeester E.,
RA Melchior F.;
RT "Ubiquitin-specific protease-like 1 (USPL1) is a SUMO isopeptidase with
RT essential, non-catalytic functions.";
RL EMBO Rep. 13:930-938(2012).
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 (PubMed:22878415). Plays a
CC key 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 ECO:0000269|PubMed:22878415}.
CC -!- INTERACTION:
CC Q6DRC5; P61956: SUMO2; Xeno; NbExp=2; IntAct=EBI-8018150, EBI-473220;
CC -!- SUBCELLULAR LOCATION: Nucleus, Cajal body
CC {ECO:0000269|PubMed:22878415}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AY648834; AAT68152.1; -; mRNA.
DR EMBL; BX548163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC154415; AAI54416.1; -; mRNA.
DR EMBL; BC159218; AAI59219.1; -; mRNA.
DR EMBL; BC162319; AAI62319.1; -; mRNA.
DR RefSeq; NP_001003880.1; NM_001003880.1.
DR AlphaFoldDB; Q6DRC5; -.
DR BioGRID; 92515; 2.
DR IntAct; Q6DRC5; 3.
DR MINT; Q6DRC5; -.
DR STRING; 7955.ENSDARP00000043801; -.
DR MEROPS; C98.001; -.
DR PaxDb; Q6DRC5; -.
DR PRIDE; Q6DRC5; -.
DR Ensembl; ENSDART00000043802; ENSDARP00000043801; ENSDARG00000034825.
DR Ensembl; ENSDART00000185626; ENSDARP00000145440; ENSDARG00000034825.
DR GeneID; 445403; -.
DR KEGG; dre:445403; -.
DR CTD; 10208; -.
DR ZFIN; ZDB-GENE-040930-7; uspl1.
DR eggNOG; ENOG502QRFM; Eukaryota.
DR GeneTree; ENSGT00390000002316; -.
DR HOGENOM; CLU_296761_0_0_1; -.
DR InParanoid; Q6DRC5; -.
DR OMA; PTDMETE; -.
DR OrthoDB; 171859at2759; -.
DR PhylomeDB; Q6DRC5; -.
DR TreeFam; TF350670; -.
DR SignaLink; Q6DRC5; -.
DR PRO; PR:Q6DRC5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 10.
DR Bgee; ENSDARG00000034825; Expressed in brain and 20 other tissues.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0016929; F:deSUMOylase activity; IDA:UniProtKB.
DR GO; GO:0032183; F:SUMO binding; IDA:UniProtKB.
DR GO; GO:0030576; P:Cajal body organization; IMP:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0016926; P:protein desumoylation; IDA:UniProtKB.
DR GO; GO:1904867; P:protein localization to Cajal body; IMP:ZFIN.
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; PF15499; Peptidase_C98; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Nucleus; Protease; Reference proteome; Thiol protease.
FT CHAIN 1..1014
FT /note="SUMO-specific isopeptidase USPL1"
FT /id="PRO_0000419648"
FT DOMAIN 355..636
FT /note="USP"
FT REGION 137..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..631
FT /note="SUMO-binding"
FT /evidence="ECO:0000250"
FT REGION 794..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..816
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 364
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 592
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT CONFLICT 97
FT /note="D -> E (in Ref. 3; AAI54416/AAI59219)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="I -> T (in Ref. 3; AAI59219)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="V -> A (in Ref. 3; AAI59219)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="M -> I (in Ref. 3; AAI54416/AAI59219)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="S -> T (in Ref. 3; AAI54416/AAI59219)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="F -> I (in Ref. 3; AAI54416/AAI59219)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="T -> I (in Ref. 3; AAI59219)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="D -> V (in Ref. 3; AAI59219)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="G -> E (in Ref. 3; AAI59219)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="I -> V (in Ref. 3; AAI54416)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="Y -> D (in Ref. 3; AAI59219)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="I -> V (in Ref. 3; AAI59219)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="G -> E (in Ref. 3; AAI54416/AAI59219)"
FT /evidence="ECO:0000305"
FT CONFLICT 671
FT /note="T -> D (in Ref. 3; AAI54416/AAI59219)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="S -> N (in Ref. 3; AAI54416)"
FT /evidence="ECO:0000305"
FT CONFLICT 755
FT /note="G -> V (in Ref. 3; AAI54416/AAI59219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1014 AA; 112532 MW; 14BCCCA22B2BC5A6 CRC64;
MNGEGTGIGA PTPALAGFLG KSKDRNASPG NCPWCLAKGQ TNALRFYAVN LKETVLLCTN
AVCLYPLVSR SLEEVRASLS KGGCKRSISS LPDISDDSCP PKRPREEKLD VLADVSEPCD
AEVNDATLPD DTVKTQTFTD QQSAPAETIS LDKTEEQPVS IEDIKEQPIS HDATEGQPIS
IDQTEEQPVS ILHTEEQPIV LDLIEVKPMS VDHSEEQPIC IDNTKERPVS IVHTEEQSIV
LDLFEVKPMS IAHTEEKPTS FDHIEEKPMS IAHTEEKPVS LVHTEDQHLS IDQTEEQPIS
IDPTEEQQPE ELPAVSDEDV DLCERKEDCV SSTQDEMEEE VLESSSELVP VHSELFWKNE
ENMCWLDAML VMLVHCRTIR GTPCRGIKLS DKLATVPCND SVVWKLCWRY DKTCAYLQAR
KKQSEDKVLR VPAGVLVEAE RRLSALRLSV FKLLQPTLKC EIGQQETPVF ALPLLLRSDK
WAQDIFQHTI RWEFKCTCCD FTVNESVEKT LTTLTCIVKD WHPLKANNRT QCNKCEHKNQ
RRKMVLEKLS SVFALHFVEG LPRKDLTKYG FTFQGFQYSV STIIQYNKHL QHFVTWVRQS
NGFWLELDDL KHPYSPTHKR LPFPSSEFHI LFWETDSFKE EHSEVCLPTA PPEVPNAPDE
HPPKLSDSVA TDTCVISALT VEDTTASSIA DTSIGSTTLL DTFEGLTHKD IVTLTLVNSE
SPKNEPRPMR PGFVSAPRHC PFEASNLLSG IPKTGSRLST PPIPQKSSLV HKPEVAAAAV
SKTHLQPTSL FQRHPSFQST PIRPPPPLPP APKPKPSLQY DKHEDLPVKP ADMFGGFKTK
KLANSQPKQI SLPGGLNPSV KKTAGQEPIS TTEALRLKLM KKLKAKKKKL AKLNQLLGNG
GESVAKPDST ALSSPYSVTS STTTYDSFDD QFLADLLSPA TTVSNLSPDS TGLLEMLNNG
QNGEQQNPAV ATLAPEATLT CSSSTISPLD EYMQSGMCHT ALENADFNSL DIFF
