UBP48_CAEEL
ID UBP48_CAEEL Reviewed; 1264 AA.
AC G5ECC7; A0A5K1I7W2;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase usp-48 {ECO:0000305};
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q86UV5};
DE AltName: Full=Ubiquitin-specific protease 48 {ECO:0000312|WormBase:F30A10.10a};
GN Name=usp-48 {ECO:0000312|WormBase:F30A10.10a};
GN ORFNames=F30A10.10 {ECO:0000312|WormBase:F30A10.10a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ARG-101; 126-TRP--HIS-1264 AND 136-GLN--HIS-1264.
RX PubMed=31088904; DOI=10.1534/g3.119.400328;
RA Rahe D., Hobert O.;
RT "Restriction of cellular plasticity of differentiated cells mediated by
RT chromatin modifiers, transcription factors and protein kinases.";
RL G3 (Bethesda) 7:2287-2302(2019).
CC -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal
CC Gly of ubiquitin (By similarity). Involved in the processing of poly-
CC ubiquitin precursors as well as that of ubiquitinated proteins (By
CC similarity). Required post-developmentally to restrict the plasticity
CC of epidermal cells, probably by regulating gene expression
CC (PubMed:31088904). {ECO:0000250|UniProtKB:Q86UV5,
CC ECO:0000269|PubMed:31088904}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q86UV5};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31088904}. Chromosome
CC {ECO:0000269|PubMed:31088904}. Note=In pachytene germline cells and
CC oocytes, localizes to chromosomes. {ECO:0000269|PubMed:31088904}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F30A10.10a};
CC IsoId=G5ECC7-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F30A10.10b};
CC IsoId=G5ECC7-2; Sequence=VSP_060727;
CC -!- TISSUE SPECIFICITY: Broadly expressed. Expressed in germline.
CC {ECO:0000269|PubMed:31088904}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000255}.
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DR EMBL; BX284601; CAB03026.2; -; Genomic_DNA.
DR EMBL; BX284601; VWL57635.1; -; Genomic_DNA.
DR PIR; T19899; T19899.
DR RefSeq; NP_492524.2; NM_060123.5.
DR AlphaFoldDB; G5ECC7; -.
DR SMR; G5ECC7; -.
DR STRING; 6239.F30A10.10; -.
DR MEROPS; C19.A29; -.
DR EPD; G5ECC7; -.
DR PaxDb; G5ECC7; -.
DR PeptideAtlas; G5ECC7; -.
DR EnsemblMetazoa; F30A10.10a.1; F30A10.10a.1; WBGene00009267. [G5ECC7-1]
DR EnsemblMetazoa; F30A10.10b.1; F30A10.10b.1; WBGene00009267. [G5ECC7-2]
DR WormBase; F30A10.10a; CE53705; WBGene00009267; usp-48. [G5ECC7-1]
DR WormBase; F30A10.10b; CE53715; WBGene00009267; usp-48. [G5ECC7-2]
DR eggNOG; KOG1863; Eukaryota.
DR GeneTree; ENSGT00940000167744; -.
DR HOGENOM; CLU_263607_0_0_1; -.
DR InParanoid; G5ECC7; -.
DR OrthoDB; 113272at2759; -.
DR PRO; PR:G5ECC7; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00009267; Expressed in adult organism and 4 other tissues.
DR ExpressionAtlas; G5ECC7; baseline and differential.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Coiled coil; Hydrolase; Nucleus;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1264
FT /note="Ubiquitin carboxyl-terminal hydrolase usp-48"
FT /id="PRO_0000448599"
FT DOMAIN 108..430
FT /note="USP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT REGION 390..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 516..547
FT /evidence="ECO:0000255"
FT COMPBIAS 399..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 117
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT ACT_SITE 366
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT VAR_SEQ 844..845
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060727"
FT MUTAGEN 101
FT /note="R->K: In ot872; temperature-sensitive mutant. At the
FT restrictive temperature of 25 degrees Celsius, promotes the
FT acquisition of ASE neuron identity markers in epidermal
FT cells induced by ectopic expression of transcription factor
FT che-1 in L4 larvae."
FT /evidence="ECO:0000269|PubMed:31088904"
FT MUTAGEN 126..1264
FT /note="Missing: In mg457; promotes the acquisition of ASE
FT neuron identity markers in epidermal cells induced by
FT ectopic expression of transcription factor che-1 in
FT adults."
FT /evidence="ECO:0000269|PubMed:31088904"
FT MUTAGEN 163..1264
FT /note="Missing: In ot674; promotes the acquisition of ASE
FT neuron identity markers in epidermal cells induced by
FT ectopic expression of transcription factor che-1 in
FT adults."
FT /evidence="ECO:0000269|PubMed:31088904"
SQ SEQUENCE 1264 AA; 144457 MW; 6B122C05049FFD36 CRC64;
MTKETDKKPK ERPNQRKVAF RNEAINALVN TDEDQVTFSK AMEVAKLDCQ KCLLHDMHSS
KSSNCRDNPF CIHRLGLEKF EKLITQEQET KEEAKKDQKR RDLNDQPAGL INGGNFCYVN
SFLQVWFNVP EFRQLIYDFR PSENFVPPEA PRMNVQATML ALQDIFYTLQ TTPFNETDKT
SNLGKLLRLN SEQQDSQEFG LKFFNALERC LPDHPNGKET LKRLKDLFTG ETCTRIVCKC
GQRSEREETA ISLTLNIEGY CTLLDALDAY FGEEHLDDFK CSKCNKTGDV SKQSDYVKLP
PVIVIQLNRY KYTSKGRQKL KTPMAYPREI PAKAFQRTNN SIPPPAEMYD LFAVTIHEGN
NAECGHYYDL IKSPLNQKWY RYNDEAIEAI PKPPGTEKPT TAKTEKSRKK DKEKYPTDQK
ACYGLLYRRR DAFKPLPHPK LPPEELIIDS KTEIEELFEG LTKKKIEKSE KRLYDLERRI
NKVKISYGKL ETHSDKYKEA NEVVFLPTTL LQDVLAQEYE VAKGEKKKKK KEASENEEKK
KNEEDEALSA AIAASEADQR DKASSEPSTS AAATEAGDDE ELRAESETPN PENAESTQVA
IMETDEIMDT TPTKDIDILA KAMEDNALPT VEVPQPELKK RTRQQNGEVK YVYSQRTPRK
SHNGTNGTNS SPQKQPVSSR VAALLSSHEI PTCGHGKMSI DPILYGDVKA VSRAPAIALL
REYDFRVKIV YDNGENVFPE NEKERDVFIF TAEDICMECV REMREEGNFN NQLEDDEKLV
RRILKEEKQR CSVKCPSERP DGYLYVAKFA LSNFKKSAMS ARENRLAQSH NKQGTLHFDS
HPMFQQKSNS GYLTLSLKRT RGKPRKSLSE IPEKMQKLDE IGSKELPDEI IADEEEISEN
MGSDIPTKPV ESINPDALVP FEKIEFNSEL RCSHGGINFN QFRLSVSPEE WAHLKVYFDE
CYEVKCSDDV CDQCRQMEVD AQNGSENMRG LVREMRKRIS DTLKTVESRA ESKEDGADIK
YGICSVFIDK LRKLTSRQST SPPSICQECL LCPHQQPFKG FLNEDNHKDS HVVGLTEEEW
NTFLTEIRKL EEAGDDQSIA VDPCPIPIEN GQIVDMCEKC FEQHIKFTEE QKYMFENENI
YVKLVNLNVE EDIAKANGKA RRGRAKNLYA IKMSSTNKLM ELKVQLYDKT HQLPNDQLLY
RTAGGEQFDV SNNQKTLFDL RLSPNNNDNP LILIAQQFSP SASQADETGD RAPERGFVDT
ALAH
