ID A0A3P8TTR9_AMPPE Unreviewed; 2012 AA.
AC A0A3P8TTR9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000026457.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000026457.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000026457.1}
RP IDENTIFICATION.
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|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 STRING; 161767.ENSAPEP00000026457; -.
DR Ensembl; ENSAPET00000027162.1; ENSAPEP00000026457.1; ENSAPEG00000018695.1.
DR GeneTree; ENSGT00940000156517; -.
DR OMA; AEPLSQF; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000265080; Chromosome 9.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.30.2160.10; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369009};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000265080};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT TRANSMEM 483..506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 653..673
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 747..823
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1615..2012
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1423..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1765..1799
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1979
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2012 AA; 222198 MW; FE7D3A6429B5371B CRC64;
MSNRPNSNPG GSLRRSQRNT AAAQPQDHTV AGRSGLTLSV ASFVLQDDPE AAGTSEQERT
GHQSKSEGTR GLKRSAAPDQ ISTFAPTPAK KPKSLPPPRD NTSETKKGPT KSKKRSLPSE
PPASSGRGQS KKSVAAGASP IQKRKKADSL PGLSSTVGSL PNRTEGKTAK PTKLASKSAA
SAKAGCSNVT DSSSSASTSS SSSTTGTNSA ATQGARVKQG KDQTKARRSR SASSPSPRRS
TRDKEQAKAA SSSKFEWASR FNPKVNLPKP KLSLPGSSKT ETSKPGPSGL QAKLASLRKS
TKKRSESPPA ELPSFRRSTR QKTTGSCAST SRRGSGLGKR GAADARRQEK MADSDNNQDG
ANSSAARTDE ASQGASASSS VAGAVGMTTS GESESDDSEM GRLQALLEAR GLPPHLFGPL
GPRMSQLFHR TIGSGASSKA QQLLQGLQAT GDESQQLQAA IEMCQLLVMG NEETLGGFPV
KSVVPALVGL AVFIVPHLCM NLFYIMNHAS RALTYMMEAL PRSSAVVVDA IPVFLEKLQV
IQFIDVAEQA LTALEMLSRR HSKAILQAGG LADCLVYLEF FSINAQRNAL AIAANCCQSI
TPDEFHFVAD SLPLLTQRLT HQVSSLYLCL GLNQQNLLQE VASRDLLTNI QQLLVVTPPV
LSSGMFIMVV RMFSLMCSNC PCLAVQLMKQ NIAETLRFLL CGASNGSCQE QIELVPRSPQ
ELYELTSLIC ELMPCLPREG IFAVDVMLKK GSAQTTEGAI WQWRDDRGLW HPYNRIDSRI
IETAHQNGED EISLSTLGRV YTIDFNSMQQ INEDTGTARG IQRKPNPLAN PNTGSHQEVR
REDARAQLMK EDPELAKCFI KTLFGVLYEV YSSSAGPAVR HKCLRAILRI IYFADAELLK
DVLRNHAVSS HIASMLSSQD LKIVVGSLQM AEILMQKLPD VFSVYFRREG VMHQVKNLAE
SESFLVTSPP KACPSGTASL CTTTISTAST TSANNATPDL GSPSFQHSMD DSLDLSPQGR
LSDVLKRKRL PKRGPRRPKY SPPRDDDKVD NQAKSPTSTQ SPKSSFLASL NPKTWGKLGA
QTNNANSEPS RTAGVSGLAR APPKDSISNN RDKIKAWIKE QASKFVERYF NSENVDGSNP
ALNVLQRLCT ATEQLSLQAD GGMECLVEIS SIVSESDVSS FEIQHSGLVK QLLVYLTSNT
DRDLLSRDVR LKRFLHVFAG CPVPGMEPVG RLDPTENAPY LALVHKMNSC LSQMEQFPVK
VHDFPSGNGN GSRGSQALKF FNTHQLKCQL QRHPDCTNVK QWKGGPVKID PLALVQAIER
YLVVRGYGRI REEDEDSDDD GSDDEIDESL AAQFLNSGSV RHRLQFYIGD HLLPYNMTVY
QAVRQYSLQA EEERESTDDE ANPLGRAGIW TKTHTIWYKP VREDEDGSKD AVGGKRGRAQ
TAPTKTSPRN AKKQDELWHD GVCPSVINPL ETYLTSEPPE TITFDDPSLE VNLLLRVLHS
ISRYWFYLYD NAACKEIIPT SEFINSKLTA KANRQLQDPL VIMTGNIPTW LIELGKTCPF
FFPFDTRQML FYVTAFDRDR AMQRLLDTNP EINQSDSQDS RVAPRLDRKK RTINRDELLK
QAESVMQDLG SSRAMLEIQY ENEVGTGLGP TLEFYALVSQ ELQRADLGLW RGEEVTLANP
KGNQEGTKYM FSSRGLFAVP FGRTTKPAHI AKIKMKFRFL GKLMAKAIMD FRLLDLPLGL
PFYKWMLRHE MSISSHDLVN IDPSVAKSIQ HLEDIIRQKK RLEQDRSQTR ETLQQALESL
NMNGCSVEDL GLDFTLPGFP NIELKKGGKD IPVTIYNLEE YLRLVVYWTL NEGVSRQFES
FREGFESVFP LHHLQYFYPE ELDQLLCGSK SETWDVKTLM ECCRPDHGYT HDSRAVRFLF
EVLSSFDAEQ QRLFLQFVTG SPRLPVGGFR SLNPPLTIVR KTFESTENPD DFLPSVMTCV
NYLKLPDYSS IEIMREKLLI AAREGQQSFH LS
//
