ID K7FWJ6_PELSI Unreviewed; 2024 AA.
AC K7FWJ6;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
GN Name=TRIP12 {ECO:0000313|Ensembl:ENSPSIP00000012406.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000012406.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000012406.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in ubiquitin fusion
CC degradation (UFD) pathway and regulation of DNA repair. Part of the
CC ubiquitin fusion degradation (UFD) pathway, a process that mediates
CC ubiquitination of protein at their N-terminus, regardless of the
CC presence of lysine residues in target proteins.
CC {ECO:0000256|RuleBase:RU369009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885,
CC ECO:0000256|RuleBase:RU369009};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369009}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642, ECO:0000256|RuleBase:RU369009}.
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331, ECO:0000256|RuleBase:RU369009}.
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DR EMBL; AGCU01063879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01063880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01063881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01063882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01063883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01063884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01063885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01063886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01063887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01063888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006119942.1; XM_006119880.2.
DR Ensembl; ENSPSIT00000012467.1; ENSPSIP00000012406.1; ENSPSIG00000010747.1.
DR GeneID; 102458825; -.
DR CTD; 9320; -.
DR GeneTree; ENSGT00940000156517; -.
DR HOGENOM; CLU_000366_2_0_1; -.
DR OrthoDB; 1093891at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 3.30.720.50; -; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR037197; WWE_dom_sf.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00678; WWE; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50918; WWE; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369009};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 754..830
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1627..2024
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1600..1619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1059
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1991
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2024 AA; 224316 MW; 16DE50754F5AFE69 CRC64;
MSNRPNNNPG GSLRRSQRNT AGAQPQDDTV GGRGCSSSAI IIPQEDPDRV STSEKQRTGQ
VPKKDHSRGV KRSASPDYNR TNSPSSAKKP KALQYTETFS ETNKPHTKSK KRHLDQEQQL
KSAQLPSTSK AHTRKGGATG SSRSQKRKRT ESSSCIKSGT AVDSTGVEER SAKPSKLASK
SATSAKAGCS NITDSSSSAS TSSSSSAVAS ASSTVPQGAR VKQGKDQSKA RRSRSASSPS
PRRSSRDKEQ SKTGGSSKFD WAARFSPKVS LPKTKLSLPG SSKSEASKPG PSGLQAKLAS
LRKSTKKRSE SPPAELPSLR RSTRQKTTGS CASTSRRGSG LGKRGAAEAR RQEKMADPDN
NQDGVNSSAA RTDETPQGAA ASSSVAGAVG MTTSGESESD DSEMGRLQAL LEARGLPPHL
FGPLGPRMSQ LFHRTIGSGA SSKAQQLLQG LQATDESQQL QAVIEMCQLL VMGNEETLGG
FPVKSVVPAL ITLLQMEHNF DIMNHACRAL TYMMEALPRS SAVVVDAIPV FLEKLQVIQC
IDVAEQALTA LEMLSRRHSK AILQAGGLAD CLLYLEFFSI NAQRNALAIA ANCCQSITPD
EFHFVADSLP LLTQRLTHQD KKSVESTCLC FARLVDNFQH EENLLQQVAS KDLLTNIQQL
LVVTPPILSS GMFIMVVRMF SLMCSNCPTL AVQLMKQNIA ETLHFLLCGA SNGNCQEQID
LVPRSPQELY ELTSLICELM PCLPKEGIFA VDTMLKKGNA QNTDGAIWQW RDDRGLWHPY
NRIDSRIIEA AHQVGEDEIS LSTLGRVYTI DFNSMQQINE DTGTARAIQR KPNPLVNTNT
SGHSELKKDD ARAQLMKEDP ELAKSFIKTL FGVLYEVYSS SAGPAVRHKC LRAILRIIYF
ADAELLKDVL KNHAVSSHIA SMLSSQDLKI VVGALQMAEI LMQKLPDIFS VYFRREGVMH
QVKNLAESEA LLTSPPKACT NGSGTLGTTT TISTGTATSA SNAAADLGSP SLQHSREDSL
DLSPQGRLSD VLKRKRLPKR GPRRPKYSPP RDDDKVDNQA KSPTTTQSPK SSFLASLNPK
TWGRLSTQSN SNNIEPARTA GVSGLARAAS KDTISNNREK IKGWIKEQAH KFVERYFSSE
NMDGSNPALN VLQRLCTATE QLNLQVDGGA ECLVEIRSIV SESDVSSFEI QHSGFVKQLL
LYLTSKSEKD AVSRDIRLKR FLHVFFSSPP PEEEPVGRLE PVGNAPLLAL VHKMNNCLSQ
MEQFPVKVHD FPSGNGTGSS FSLNRGSQAL KFFNTHQLKC QLQRHPDCAN VKQWKGGPVK
IDPLALVQAI ERYLVVRGYG RVREDDEDSD DDGSDEEIDE SLAAQFLNSG NVRHRLQFYI
GDHLLPYNMT VYQAVRQFSL QAEEERESTD DESNPLGRAG IWTKTHTIWY KPVREDEDGN
KDCVGGKRGR AQTAPTKTSP RNSKKHDELW HDGVCPSVSN PLEAYLVFTP PENITFEDPS
LDVILLLRVL HAISRYWYYL YENAVCKEII PTTEFINSKL TAKANRQLQD PLVIMTGNIP
IWLTELGKTC PFFFPFDTRQ MLFYVTAFDR DRAMQRLLDT NPEINQSDSQ DSRVAPRLDR
KKRTVNREEL LKQAESVMQD LGSSRAMLEI QYENEVGTGL GPTLEFYALV SQELQRADLG
LWRGEEVTLS NPKGNQEGTK YIHNLQGLFA LPFGRTAKPA HIAKVKMKFR FLGKLMAKAI
MDFRLVDLPL GLPFYKWMLR QETSLTSHDL FNIDPVVARS VYHLEDIVRQ KKRLEQDKSQ
TKESLQYALE TLNMNGCSVE DLGLDFTLPG FPNIELKKGG KDIPVTIHNL EEYLRLVIFW
ALNEGVSRQF DSFRDGFESV FPLSHLQYFY PEELDQLLCG SKTDTWDAKT LMECCRPDHG
YTHDSRAVKY LFEILSSFDS EQQRLFLQFV TGSPRLPVGG FRSLNPPLTI VRKTFESTEN
PDDFLPSVMT CVNYLKLPDY SSIEIMREKL LIAAREGQQS FHLS
//
