ID W5QHF3_SHEEP Unreviewed; 2026 AA.
AC W5QHF3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:ENSOARP00000022153.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000022153.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000022153.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000022153.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000022153.1}
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; AMGL01056554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01056555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9940.ENSOARP00000022153; -.
DR PaxDb; 9940-ENSOARP00000022153; -.
DR Ensembl; ENSOART00000022458.1; ENSOARP00000022153.1; ENSOARG00000020614.1.
DR eggNOG; KOG0168; Eukaryota.
DR eggNOG; KOG0170; Eukaryota.
DR OMA; AEPLSQF; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002356; Chromosome 2.
DR Bgee; ENSOARG00000020614; Expressed in testis and 55 other cell types or tissues.
DR ExpressionAtlas; W5QHF3; baseline.
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:UP000002356};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 756..832
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1629..2026
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1441..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1602..1621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..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..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1061
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1993
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2026 AA; 223942 MW; 276B637D7CB1D225 CRC64;
MSNRPNNNPG GSLRRSQRNT AGAQPQDDSI GGRSCSSSSV VIVPQPEDPD RANTSEKQKT
GQVPKKDNSR GVKRSASPDY NRTNSPSSAK KPKALQHTES PSETSKPHSK SKKRHLDQEP
QLKSAPSPST SKAHTRKSGA AAGSRSQKRK RTESSCIKSA SVSEATGAEE RSAKPTKLAS
KSAASAKAGC STITDSSSAA STSSSSSAVA SASSAVPPGA RVKQGKDQNK ARRSRSASSP
SPRRSSREKE QSKTGGSSKF DWAARFSPKV SLPKTKLSLP GSSKSEASKP GPSGLQAKLA
SLRKSTKKRS ESPPAELPSL RRSTRQKTTG SCASASSRRG SGLGKRGAAE ARRQEKMADP
EGNQETVNSS AARTDETPQG AAASSSVAGA VGMTTSGESE SDDSEMGRLQ ALLEARGLPP
HLFGPLGPRM SQLFHRTIGS GASSKAQQLL QGLQASDESQ QLQAVIEMCQ LLVMGNEETL
GGFPVKSVVP ALITLLQMEH NFDIMNHACR ALTYMMEALP RSSAVVVDAI PVFLEKLQVI
QCIDVAEQAL TALEMLSRRH SKAILQAGGL ADCLLYLEFF SINAQRNALA IAANCCQSIT
PDEFHFVADS LPLLTQRLTH QDKKSVESTC LCFARLVDNF QHEENLLQQV ASKDLLTNVQ
QLLVVTPPIL SSGMFIMVVR MFSLMCSNCP TLAVQLMKQN IAETLHFLLC GASNGSCQEQ
IDLVPRSPQE LYELTSLICE LMPCLPKEGI FAVDTMLKKG NAQNTDGAIW QWRDDRGLWH
PYNRIDSRII EAAHQVGEDE ISLSTLGRVY TIDFNSMQQI NEDTGTARAI QRKPNPLANT
NTSGYSELKK DDARAQLMKE DPELAKSFIK TLFGVLYEVY SSSAGPAVRH KCLRAILRII
YFADAELLKD VLKNHAVSSH IASMLSSQDL KIVVGALQMA EILMQKLPDI FSVYFRREGV
MHQVKHLAES ESLLTSPPKA CTNGSGSLGS TPLVNCGTAT AATNASADLG SPSLQHSRDD
SLDLSPQGRL SDVLKRKRLP KRGSRRPKYS PPRDDDKVDN QAKSPTTTQS PKSSFLASLN
PKTWGRLSAQ SNSNNIEPAR TAGVSGLARA ASKDTISNNR EKIKGWIKEQ AHKFVERYFS
SENMDGSNPA LNVLQRLCAA TEQLNLQVDG GAECLVEIRS IVSESDVSSF EIQHSGFVKQ
LLLYLTSKSE KDAVSREIRL KRFLHVFFSS PLPGEEPIER VEPVGNAPLL ALVHKMNNCL
SQMEQFPVKV HDFPSGNGTG GSFSLNRGSQ ALKFFNTHQL KCQLQRHPDC ANVKQWKGGP
VKIDPLALVQ AIERYLVVRG YGRVRDDDED SDDDGSDEEI DESLAAQFLN SGNVRHRLQF
YIGEHLLPYN MTVYQAVRQF SIQAEDERES TDDESNPLGR AGIWTKTHTI WYKPVREDEE
SNKDCVGGKR GRAQTAPTKT SPRNAKKHDE LWNDGVCPSV SNPLEVYLIP TAPENITFED
PSLDVILLLR VLHAVSRYWY YLYDNAMCKE IIPTSEFINS KLTAKANRQL QDPLVIMTGN
IPTWLTELGK TCPFFFPFDT RQMLFYVTAF DRDRAMQRLL DTNPEINQSD SQDSRVAPRL
DRKKRTVNRE ELLKQAESVM QDLGSSRAML EIQYENEVGT GLGPTLEFYA LVSQELQRAD
LGLWRGEEVT LSNPKGSQEG TKYIQNLQGL FALPFGRTAK PAHIAKVKMK FRFLGKLMAK
AIMDFRLVDL PLGLPFYKWM LRQETSLTSH DLFDIDPVVA RSVYHLEDIV RQKKRLEQDK
SQTKESLQYA LETLTMNGCS VEDLGLDFTL PGFPNIELKK GGKDIPVTIH NLEEYLRLVI
FWALNEGVSR QFDSFRDGFE SVFPLSHLQY FYPEELDQLL CGSKADTWDA KTLMECCRPD
HGYTHDSRAV KFLFEILSSF DNEQQRLFLQ FVTGSPRLPV GGFRSLNPPL TIVRKTFEST
ENPDDFLPSV MTCVNYLKLP DYSSLEIMRE KLLMAAREGQ QSFHLS
//
