ID A0A340X1Z1_LIPVE Unreviewed; 2040 AA.
AC A0A340X1Z1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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_007453324.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007453324.1};
RN [1] {ECO:0000313|RefSeq:XP_007453324.1}
RP IDENTIFICATION.
RG RefSeq;
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|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_007453324.1; XM_007453262.1.
DR STRING; 118797.A0A340X1Z1; -.
DR GeneID; 103069536; -.
DR KEGG; lve:103069536; -.
DR CTD; 9320; -.
DR InParanoid; A0A340X1Z1; -.
DR OrthoDB; 1093891at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000265300; 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:UP000265300};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 797..884
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1643..2040
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 986..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1455..1482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1616..1635
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..260
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 402..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1075
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2007
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2040 AA; 225480 MW; 513765C25E938C07 CRC64;
MSNRPNNNPG GSLRRSQRNT AGAQPQDDSI GGRSHLGQAK HKGYSPPESR KSNSKAPKVQ
SNTTSELSRG HLSKRSCSSS SAVIVPQPED PDRANTSERQ KTGQVPKKDS SRGVKRSASP
DYNRTSSPNS AKKPRALQHT ESPSETSKPH SKSKKRHLDQ EQQLKSAQSP STSKAHTRKS
GATASSRSQK RKRTESSCIK SGSVSEATGA EERSAKPTKL ASKSAASAKA GCSTITDSSS
AASTSSSSSA VASASSTVPP GARVKQGKDQ SKARRSRSAS SPSPRRSSRE KEQSKTGGSS
KFDWAARFSP KVSLPKTKLS LPGSSKSETS KPGPSGLQAK LASLRKSTKK RSESPPAELP
SLRRSTRQKT TGSCASASRR GSGLGKRGAA EARRQEKMAD PEGNQETVNS SAARTDETPQ
GAAASSSVAG AVGMTTSGES ESDDSEMGRL QALLEARGLP PHLFGPLGPR MSQLFHRTIG
SGASSKAQQL LQGLQASDES QQLQAVIEMC QLLVMGNEET LGGFPVKSVV PALITLLQME
HNFDIMNHAC RALTYMMEAL PRSSAVVVDA IPVFLEKLQV IQCIDVAEQA LTALEMLSRR
HSKAILQAGG LADCLLYLEF FSINAQRNAL AIAANCCQSI TPDEFHFVAD SLPLLTQRLT
HQDKKSVEST CLCFARLVDN FQHEENLLQQ VASKDLLTNV QQLLVVTPPI LSSGMFIMVV
RMFSLMCSNC PTLAVQLMKQ NIAETLHFLL CGASNGSCQE QIDLVPRSPQ ELYELTSLIC
ELMPCLPKEG IFAVDTMLKK GNAQNTDGAI WQWRDDRGLW HPYNRIDSRI IEQINEDTGT
ARAIQRKPNP LANTNSSGYS ELKKDDARAQ LMKEDPELAK SFIKTLFGVL YEVYSSSAGP
AVRHKCLRAI LRIIYFADAE LLKDVLKNHA VSSHIASMLS SQDLKIVVGA LQMAEILMQK
LPDIFSVYFR REGVMHQVKH LAESESLLTS PPKACTNGSG SLGSTTSVSS GTATAATNAS
ADLGSPSLQH SRDDSLDLSP QGRLSDVLKR KRLPKRGSRR PKYSPPRDDD KVDNQAKSPT
TTQSPKSSFL ASLNPKTWGR LSAQSHSNNI EPARAAGVSG LARAASKDTI SNNREKIKGW
IKEQAHKFVE RYFSSENMDG SNPALNVLQR LCAATEQLNL QVDGGAECLV EIRSIVSESD
VSSFEIQHSG FVKQLLLYLT SKSEKDAVSR EIRLKRFLHV FFSSPLPGEE PIGRVEPVGN
APLLALVHKM NNCLSQMEQF PVKVHDFPSG NGTGGSFSLN RGSQALKFFN THQLKCQLQR
HPDCANVKQW KGGPVKIDPL ALVQAIERYL VVRGYGRVRE DDEDSDDDGS DEEIDESLAA
QFLNSGNVRH RLQFYIGEHL LPYNMTVYQA VRQFSIQAED ERESTDDESN PLGRAGIWTK
THTIWYKPVR EDEESNKDCV GGKRGRAQTA PTKTSPRNAK KHDELWNDGV CPSVSNPLEV
YLIPTPPENI TFEDPSLDVI LLLRVLHAIS RYWYYLYDNA VCKEIIPTSE FINSKLTAKA
NRQLQDPLVI MTGNIPTWLT ELGKTCPFFF PFDTRQMLFY VTAFDRDRAM QRLLDTNPEI
NQSDSQDSRV APRLDRKKRT VNREELLKQA ESVMQDLGSS RAMLEIQYEN EVGTGLGPTL
EFYALVSQEL QRADLGLWRG EEVTLSNPKG SQEGTKYIQN LQGLFALPFG RTAKPAHIAK
VKMKFRFLGK LMAKAIMDFR LVDLPLGLPF YKWMLRQETS LTSHDLFDID PVVARSVYHL
EDIVRQKKRL EQDKSQTKES LQYALETLTM NGCSVEDLGL DFTLPGFPNI ELKKGGKDIP
VTIHNLEEYL RLVIFWALNE GVSRQFDSFR DGFESVFPLS HLQYFYPEEL DQLLCGSKAD
TWDAKTLMEC CRPDHGYTHD SRAVKFLFEI LSSFDNEQQR LFLQFVTGSP RLPVGGFRSL
NPPLTIVRKT FESTENPDDF LPSVMTCVNY LKLPDYSSIE IMREKLLMAA REGQQSFHLS
//
