ID A0A383YV62_BALAS Unreviewed; 2043 AA.
AC A0A383YV62;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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|RefSeq:XP_007166757.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007166757.1};
RN [1] {ECO:0000313|RefSeq:XP_007166757.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007166757.1};
RG RefSeq;
RL Submitted (JAN-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|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 RefSeq; XP_007166757.1; XM_007166695.2.
DR CTD; 9320; -.
DR OrthoDB; 1093891at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261681; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
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; 3.30.2410.10; 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; 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 SMART; SM00119; HECTc; 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:UP000261681};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 800..887
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1646..2043
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1619..1638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1078
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2010
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2043 AA; 225853 MW; B34B859596E06311 CRC64;
MSNRPNNNPG GSLRRSQRNT AGAQPQDDSI GGRSHLGQAK HKGYSPPESR KSNSKAPKVQ
SNTTSELSRG HLSKRSCSSS SAVIVPQPED PDRANTSERQ KTGQVPKKDN SRGVKRSASP
DYNRTNSPSS AKKPKALQHT ESPSETSKPH SKSKKRHLDQ EQQLKSAQSP STSKAHTRKS
GATASSRSQK RKRTESSCIK SGSVSEATGA EERSAKPTKL ASKSAASAKA GCSTITDSSS
AASTSSSSSA VASASSAVPP GARVKQGKDQ NKARRSRSAS SPSPRRSSRE KEQSKTGGSS
KFDWAARFSP KVSLPKTKLS LPGSSKSETS KPGPSGLQAK LASLRKSTKK RSESPPAELP
SLRRSTRQKT TGSCASASRR GSGLGKRGAA EARRQEKMAD PEGNQEPVNS SAARTDETPQ
GAAASSSVAG AVGMTTSGES ESDDSEMGRL QALLEARGLP PHLFGPLGPR MSQLFHRTIG
SGASSKAQQL LQGLQASDES QQLQAVIEMC QLLVMGNEET LGGFPVKSVV PALITLLQME
HNFDIMNHAC RALTYMMEAL PRSSAVVVDA IPVFLEKLQV IQCIDVAEQA LTALEMLSRR
HSKAILQAGG LADCLLYLEF FSINAQRNAL AIAANCCQSI TPDEFHFVSD SLPLLTQRLT
HQDKKSVEST CLCFARLVDN FQHEENLLQQ VASKDLLTNV QQLLVVTPPI LSSGMFIMVV
RMFSLMCSNC PTLAVQLMKQ SFTDIAETLH FLLCGASNGS CQEQIDLVPR SPQELYELTS
LICELMPCLP KEGIFAVDTM LKKGNAQNTD GAIWQWRDDR GLWHPYNRID SRIIEQINED
TGTARAIQRK PNPLANTNSS GYSELKKDDA RAQLMKEDPE LAKSFIKTLF GVLYEVYSSS
AGPAVRHKCL RAILRIIYFA DAELLKDVLK NHAVSSHIAS MLSSQDLKIV VGALQMAEIL
MQKLPDIFSV YFRREGVMHQ VKHLAESESL LTSPPKACTN GSGSLGSTTS VSSGTATAAT
NASADLGSPS LQHSRDDSLD LSPQGRLSDV LKRKRLPKRG SRRPKYSPPR DDDKVDNQAK
SPTTTQSPKS SFLASLNPKT WGRLSAQSHS NNIEPARAAG VSGLARAASK DTISNNREKI
KGWIKEQAHR FVERYFSSEN MDGSNPALNV LQRLCAATEQ LNLQVDGGAE CLVEIRSIVS
ESDVSSFEIQ HSGFVKQLLL YLTSKSEKDA VSREIRLKRF LHVFFSSPLP GEEPIGRVEP
VGNAPLLALV HKMNNCLSQM EQFPVKVHDF PSGNGTGGSF SLNRGSQALK FFNTHQLKCQ
LQRHPDCANV KQWKGGPVKI DPLALVQAIE RYLVVRGYGR VREDDEDSDD DGSDEEIDES
LAAQFLNSGN VRHRLQFYIG EHLLPYNMTV YQAVRQFSIQ AEDERESTDD ESNPLGRAGI
WTKTHTIWYK PVREDEESNK DCVGGKRGRA QTAPTKTSPR NAKKHDELWN DGVCPSVSNP
LEVYLIPTPP ENITFEDPSL DVILLLRVLH AISRYWYYLY DNAVCKEIIP TSEFINSKLT
AKANRQLQDP LVIMTGNIPT WLTELGKTCP FFFPFDTRQM LFYVTAFDRD RAMQRLLDTN
PEINQSDSQD SRVAPRLDRK KRTVNREELL KQAESVMQDL GSSRAMLEIQ YENEVGTGLG
PTLEFYALVS QELQRADLGL WRGEEVTLSN PKGSQEGTKY IQNLQGLFAL PFGRTAKPAH
IAKVKMKFRF LGKLMAKAIM DFRLVDLPLG LPFYKWMLRQ ETSLTSHDLF DIDPVVARSV
YHLEDIVRQK KRLEQDKSQT KESLQYALET LTMNGCSVED LGLDFTLPGF PNIELKKGGK
DIPVTIHNLE EYLRLVIFWA LNEGVSRQFD SFRDGFESVF PLSHLQYFYP EELDQLLCGS
KADTWDAKTL MECCRPDHGY THDSRAVKFL FEILSSFDNE QQRLFLQFVT GSPRLPVGGF
RSLNPPLTIV RKTFESTENP DDFLPSVMTC VNYLKLPDYS SIEIMREKLL MAAREGQQSF
HLS
//
