ID A0A2I2UH72_FELCA Unreviewed; 2007 AA.
AC A0A2I2UH72;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 30.
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:ENSFCAP00000031863.3,
GN ECO:0000313|VGNC:VGNC:66560};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000031863.3, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000031863.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000031863.3,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000031863.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000031863.3,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000031863.3}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000031863.3};
RG Ensembl;
RL Submitted (SEP-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 EMBL; AANG04002752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSFCAT00000038365.3; ENSFCAP00000031863.3; ENSFCAG00000011714.6.
DR VGNC; VGNC:66560; TRIP12.
DR GeneTree; ENSGT00940000156517; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000011712; Chromosome C1.
DR Bgee; ENSFCAG00000011714; Expressed in testis and 10 other cell types or tissues.
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; 3.30.2160.10; Hect, E3 ligase catalytic domain; 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:UP000011712};
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 1621..2007
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..1481
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..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..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 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 1974
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2007 AA; 221661 MW; ECF1497122489FC3 CRC64;
MSNRPNNNPG GSLRRSQRNT AGAQPQDDSI GGRSHLGQAK HKGYSPPESR KSNSKAPKVQ
SNTTSELSRG HLSKRSCSSS SAVIVPQPED PDRANPSERQ KTGQVPKKDN SRGVKRSASP
DYNRTNSPSS AKKPKALQRT ESPSETNKPH SKSKKRHLDQ EQQLKSAHSP STSKAHTRKS
GAAGSSRSQK RKRTESSCIK SGSVSESTGA EERSAKPTKL ASKSAASAKA GCSSITDSSS
AASTSSSSSA VASASSAVPP GARVKQGKDQ NKARRSRSAS SPSPRRSSRE KEQSKTGGSS
KFDWAARFSP KVSLPKTKLS LPGSSKSETS KPGPSGLQAK LASLRKSTKK RSESPPAELP
SLRRSTRQKT TGSCASASRR GSGLGKRGAA EARRQEKMAD PESNQETVNS 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 LANTNTSGYS ELKKDDARAQ LMKEDPELAK AFIKTLFGVL YEVYSSSAGP
AVRHKCLRAI LRIIYFADAE LLKDVLKNHA VSSHIASMLS SQDLKIVVGA LQMAEILMQK
LPDIFSVYFR REGVMHQVKH LAESESLLTS PPKACTNGSG SLGSTTSVSS GTATAATNAA
ADVGSPSLQH SRDDSLDLSP QGRLSDVLKR KRLPKRGPRR PKYSPPRDDD KVDNQAKSPT
TTQSPKSSFL ASLNPKTWGR LSAQSNSNNI EPARTAGVSG 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 KHDELWHDGV CPSVANPLEV
YLISTPPENI TFEDPSLDVI LLLRVLHAIS RYWYYLYDNA MCKEIIPTSE FINSKLTAKA
NRQLQDPLVI MTGNIPTWLT ELGKTCPFFF PFDTRQMLFY VTAFDRDRAM QRLLDTNPEI
NQSDSQDSRV APRLDRKKVG TGLGPTLEFY ALVSQELQRA DLGLWRGEEV TLSNPKGSQE
GTKYIQNLQG LFALPFGRTA KPAHIAKVKM KFRFLGKLMA KAIMDFRLVD LPLGLPFYKW
MLRQETSLTS HDLFDIDPVV ARSVYHLEDI VRQKKRLEQD KSQTKESLQY ALETLTMNGC
SVEDLGLDFT LPGFPNIELK KGGKDIPVTI HNLEEYLRLV IFWALNEGVS RQFDSFRDGF
ESVFPLSHLQ YFYPEELDQL LCGSKADTWD AKTLMECCRP DHGYTHDSRA VKFLFEILSS
FDNEQQRLFL QFVTGSPRLP VGGFRSLNPP LTIVRKTFES TENPDDFLPS VMTCVNYLKL
PDYSSIEIMR EKLLIAAREG QQSFHLS
//
