ID F6Q9Q6_ORNAN Unreviewed; 2603 AA.
AC F6Q9Q6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 3.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
GN Name=HECTD1 {ECO:0000313|Ensembl:ENSOANP00000022126.4};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000022126.4, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000022126.4, ECO:0000313|Proteomes:UP000002279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000022126.4,
RC ECO:0000313|Proteomes:UP000002279};
RX PubMed=18464734; DOI=10.1038/nature06936;
RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT "Genome analysis of the platypus reveals unique signatures of evolution.";
RL Nature 453:175-183(2008).
RN [2] {ECO:0000313|Ensembl:ENSOANP00000022126.4}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000022126.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates.
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 -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331, ECO:0000256|RuleBase:RU369009}.
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DR STRING; 9258.ENSOANP00000022126; -.
DR Ensembl; ENSOANT00000022130.4; ENSOANP00000022126.4; ENSOANG00000014033.4.
DR eggNOG; KOG4276; Eukaryota.
DR GeneTree; ENSGT00940000156572; -.
DR HOGENOM; CLU_000869_0_0_1; -.
DR InParanoid; F6Q9Q6; -.
DR OMA; INHTLTM; -.
DR TreeFam; TF323674; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002279; Chromosome 14.
DR Bgee; ENSOANG00000014033; Expressed in testis and 8 other cell types or tissues.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central.
DR CDD; cd21062; BTHB_HectD1; 1.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 1.10.720.80; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 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; 2.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR041200; FKBP3_BTHB.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR InterPro; IPR010606; Mib_Herc2.
DR InterPro; IPR037252; Mib_Herc2_sf.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR45670:SF19; E3 UBIQUITIN-PROTEIN LIGASE HECTD1; 1.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF18410; BTHB; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF06701; MIB_HERC2; 1.
DR Pfam; PF07738; Sad1_UNC; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF159034; Mib/herc2 domain-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS51416; MIB_HERC2; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT REPEAT 395..427
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 426..458
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1259..1331
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 2144..2603
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 248..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1426..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1667..1750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1770..1790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2290..2311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1668..1693
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1694..1714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1736..1750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2572
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2603 AA; 288590 MW; 63775A23FC2179D1 CRC64;
MADVDPDTLL EWLQMGQGDE RDMQLIALEQ LCMLLLMSDN VDRCFETCPP RTFLPALCKI
FLDESAPDNV LEVTARAITY YLDVSAECTR RIVGVDGAIK ALCNRLVVVE LNNRTSRDLA
EQCVKVLELI CTRESGAVFE AGGLNCVLTF IRDSGHLVHK DTLHSAMAVV SRLCGKMEPQ
DSSLEICVES LSSLLKHEDH QVSDGALRCF ASLADRFTRR GVDPAPLAKH GLTEELLSRM
AAAGGAVSGP SSACKPGRST TGAPSTAADS KLSNQVSTIV SLLSTLCRGS PVVTHDLLRS
ELPDSIESAL QGDERCVLDT MRLVDLLLVL LFEGRKALPK SSAGSTGRIP GLRRLDSSGE
RSHRQLIDCI RSKDTDALID AIDTGAFEVN FMDDVGQTLL NWASAFGTQE MVEFLCERGA
DVNRGQRSSS LHYAACFGRP QVAKTLLRHG ANPDLRDEDG KTPLDKARER GHSEVVDWMC
PVNKGDDKKK KDANKDEEEC NEPKGDPEMA PIYLKRLLPV FAQTFQQTML PSIRKASLAL
IRKMIHFCSE ALLKEVCDSD AGHNLPTILV EITATILDQE DDDDGHLLAL QIIRDLVDKG
GDLFLDQLAR LGVISKVSTL AGPSSDDENE EESKPEKEDE PQEDAKELQQ GKPYHWRDWS
IIRGRDCLYI WSDAAALELS NGSNGWFRFI LDGKLATMYS SGSPEGGSDS SESRSEFLEK
LQRARSQVKP STSSQPILSA PGPIKLTVGN WSLTCLKEGE IAIHNSDGQQ ATILKEDLPG
FVFESNRGTK HSFTAETSLG SEFVTGWTGK RGRKLKSKLE KTKQKVRTMA RDLYDDHFKA
VESMPRGVVV TLRNIATQLE SSWELHTNRQ CIEGENTWRD LMKTALENLI VLLKDENTIS
PYEMCSSGLV QALLTVLNNS MDLDMKQDCT QLVERINVFK TAFSENEDDE SRPAVALIRK
LIAVLESIER LPLHLYDTPG STYNLQILTR RLRFRLERAS GETSLIDRTG RMLKMEPLAT
VESLEQYLLK MVAKQWYDFD RSSFVFVRKL REGQTFIFRH QHDFDENGII YWIGTNAKTA
YEWVNPAAYG LVVVTSSEGR NLPYGRLEDI LSRDSSALNC HSNDDKNAWF AIDLGLWVIP
SAYTLRHARG YGRSALRNWV FQVSKDGQNW TTLYTHVDDC SLNEPGSTAT WPLDPPKDEK
QGWRHVRIKQ MGKNASGQTH YLSLSGFELY GTVSGVCEDQ LGKAAKEAEA NLRRQRRLVR
SQVLKYMVPG ARVIRGIDWK WRDQDGSPQG EGTVTGELHN GWIDVTWDAG GSNSYRMGAE
GKFDLKLAPG YDPDTAASPK PVSSTVSGTT QSWSSLVKNN CPDKTSAAAG SSSRKGSSSS
VCSVASSSDI SLGSTKMERR SESVTEQSVV SGPDVHEPIV VLSSAENVPQ AEVGSSSSAS
TSTLTAEAGC ENAERKLGPE SSVRTPGETS AISMGIVSVS SPDVSSVSEL TNKEAASQRP
LSSSASNRLS VSSLLAAGAP MSSSASVPNL SSRETSSLES FVRRVANIAR TNATNNMNLS
RSSSDNNTNT LGRNVMSTAT SPLMGAQSFP NLTTTGTTST VTMSTSSVTS SSNVATATTV
LSVGQSLSNT LTTSLTSTSS ESDTGQEAEY SLYDFLDSCR ASTLLAELDD DEDLPEPDEE
DDENEDDNQE DQEYEEVMIL RRPSLQRRAG SRSDVTHHAV TSQLPQVPAG AGSRPIGEQE
EEEYETKGGR RRTWDDDYVL KRQFSALVPA FDPRPGRTNV QQTTDLEIPP PGTPHSELLE
EVECTPSPRL ALTLKVTGLG TTREVELPLS NFRSTIFYYV QKLLQFSCNG SVKSDKLRRI
WEPTYTIMYR EMKDSDKEKE SGKMGCWSIE HVEQFLGTDE LPKNDLITYL QKNADSAFLR
HWKLTGTNKS IRKNRNCSQL IAAYKDFCEH GSKSGLSQGA ISTLQNCDIL SLVKEQPQAK
AGNGQNSCGV EDVLQLLRIL YIVASDPYTR TSHEEGDEQL QFHFPPDEFT SKKLTTKILQ
QIEEPLALAS GALPDWCEQL TSKCPFLIPF ETRQLYFTCT AFGASRAIVW LQNRREATVE
RTRTTSTVRR DDPGEFRVGR LKHERVKVPR GESLMEWAEN VMQIHADRKS VLEVEFLGEE
GTGLGPTLEF YALVAAEFQR TELGTWLCDD DFPDDESRHV DLGGGLKPPG YYVQRSCGLF
TAPFPQDSDE LERITKLFHF LGIFLAKCIQ DNRLVDLPIS KPFFKLMCMG DIKSNMSKLI
YESRGDRDLH CTESQSEAST EEGHDSLSVG SFEEDSKSEF ILDPPKPKPP AWFNGILTWE
DFELVNPHRA RFLKEIKDLA IKRRQILSNK SLSEDEKNTK LQDLMLKNPS GSGPSLSIED
LGLNFQFCPS SRVYGFTAVD LKPSGEDEMI TMDNAEEYVD LMFDFCMQTG IQKQMDAFRD
GFNKVFPMEK LSSFSHEEVQ MILCGNQSPS WAAEDIINYT EPKLGYTRDS PGFLRFVRVL
CGMSSDERKA FLQFTTGCST LPPGGLANLH PRLTVVRKVD ATDASYPSVN TCVHYLKLPE
YSSEEIMRER LLAATMEKGF HLN
//