ID A0A2Y9RQ96_TRIMA Unreviewed; 2026 AA.
AC A0A2Y9RQ96;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
GN Name=LOC101351365 {ECO:0000313|RefSeq:XP_023595851.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023595851.1};
RN [1] {ECO:0000313|RefSeq:XP_023595851.1}
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|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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_023595851.1; XM_023740083.1.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000248480; 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: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:UP000248480};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 755..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 972..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1441..1467
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 121..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..294
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 344..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..996
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..1078
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; 224056 MW; D61D9D78F5F9B1DE CRC64;
MSNRPSNNPG GSLRRSQRNS AGAQPQDDST GGRSCSSSSA VIVPQPEDPD RANTSERQKT
GQVPKKDSSR GVKRSASPDY NRTNSPSSAK KPKALQHTES PSETNKPHSK SKKRHLDQEQ
QLKSAQSPST SKAHTRKSGA TGSSRSQKRK RTESSCIKSG SVSESTGAEE RSAKPTKLAS
KSAASAKAGC STITDSSSAA STSSSSSAVA SASSTVPPGA RVKQGKDQNK ARRSRSASSP
SPRRSSREKE QSKTGGSSKF DWAARFSPKV SLPKTKLSLP GSSKSETSKP GPSGLQAKLA
SLRKSTKKRS ESPPAELPSL RRSTRQKTTG SCASTSRRGS GLGKRGAAEA RRQEKMADPE
SNQETVNSSA ARTDETPQGA AASSSVAGAV SMTTSGESES DDSEMGRLQA LLEARGLPPH
LFGPLGPRMS QLFHRTIGSG ASSKAQQLLQ GLQATDESQQ LQAVIEMCQL LVMGNEETLG
GFPVKSVVPA LITLLQMEHN FDIMNHACRA LTYMMEALPR SSAVVVDAIP VFLEKLQVIQ
CIDVAEQALT ALEMLSRRHS KAILQAGGLA DCLLYLEFFS INAQRNALAI AANCCQSITP
DEFHFVADSL PLLTQRLTHQ DKKSVESTCL CFARLVDNFQ HEENLLQQVA SKDLLTNVQQ
LLVVTPPILS SGMFIMVVRM FSLMCSNCPT LAVQLMKQNI AETLHFLLCG ASNGSCQEQI
DLVPRSPQEL YELTSLICEL MPCLPKEGIF AVDTMLKKGN AQNTDGAIWQ WRDDRGLWHP
YNRIDSRIIE VAAHQVGEDE ISLSTLGRVY TIDFNSMQQI NEDTGTARAI QRKPNPLANT
NTSGYSELKK DDARAQLMKE DPELAKSFIK TLFGVLYEVY SSSAGPAVRH KCLRAILRII
YFADAELLKD VLKNHAVSSH IASMLSSQDL KIVVGALQMA EILMQKLPDI FSVYFRREGV
MHQVKHLAES ESLLTSPPKA CTNGSGTLGS TTSVSSGTAT AATNAAADLG SPSLQHSRDD
SLDLSPQGRL SDVLKRKRLP KRGPRRPKYS PPRDDDKVDN QAKSPTTTQS PKSSFLASLN
PKTWGRLSAQ SNSNNIEPAR TAGVSGLARA ASKDTISNNR EKIKGWIKEQ AHKFVERYFS
SENMDGSNPA LNVLQRLCAA TEQLNLQVDG GAECLVEIRS IVSESDVSSF EIQHSGFVKQ
LLLYLTSKSE KDAVSREIRL KRFLHVFFAS PLPGEEPIGR VEPMGNAPLL ALVHKMNNCL
SQMEQFPVKV HDFPSGNGTG GSFSLNRGSQ ALKFFNTHQL KCQLQRHPDC ANVKQWKGGP
VKIDPLALVQ AIERYLVVRG YGRVREDDED SDDDGSDEEI DESLAAQFLN SGNVRHRLQF
YIGEHLLPYN MTVYQAVRQF SIQAEDERES TDDESNPLGR AGIWTKTHTI WYKPVREDEE
SNKDCVGGKR GRAQTAPTKT SPRNAKKHDE LWHDGVCPSV 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 DLFDVDPVVA RSVYHLEDIV RQKKRLEQDT
SQTKESLQYS LETLTMNGCS VEDLGLDFTL PGFPNIELKK GGKDIPVTIH NLEEYLRLVI
FWALNEGVSR QFDSFRDGFE SVFPLSHLQY FYPEELDQLL CGSKADTWDA KTLMECCRPD
HGYTHDSRAV KFLFEILSSF DNEQQRLFLQ FVTGSPRLPV GGFRSLNPPL TIVRKTFEST
ENPDDFLPSV MTCVNYLKLP DYSSIEIMRE KLLIAAREGQ QSFHLS
//
