ID F7HZ46_CALJA Unreviewed; 2610 AA.
AC F7HZ46;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 85.
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|EMBL:JAB08907.1,
GN ECO:0000313|Ensembl:ENSCJAP00000010609.1};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000010609.1, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000010609.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB08907.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Bladder {ECO:0000313|EMBL:JAB08907.1}, Cerebellum
RC {ECO:0000313|EMBL:JAB52508.1}, Cerebral cortex
RC {ECO:0000313|EMBL:JAB31885.1}, Hippocampus
RC {ECO:0000313|EMBL:JAB15949.1}, and Skeletal muscle
RC {ECO:0000313|EMBL:JAB41831.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000010609.1}
RP IDENTIFICATION.
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 EMBL; GAMT01002954; JAB08907.1; -; mRNA.
DR EMBL; GAMS01007187; JAB15949.1; -; mRNA.
DR EMBL; GAMR01002047; JAB31885.1; -; mRNA.
DR EMBL; GAMQ01000020; JAB41831.1; -; mRNA.
DR EMBL; GAMP01000247; JAB52508.1; -; mRNA.
DR RefSeq; XP_002753836.1; XM_002753790.3.
DR RefSeq; XP_009004149.1; XM_009005901.2.
DR RefSeq; XP_009004150.1; XM_009005902.2.
DR RefSeq; XP_009004151.1; XM_009005903.2.
DR RefSeq; XP_017832527.1; XM_017977038.1.
DR RefSeq; XP_017832528.1; XM_017977039.1.
DR RefSeq; XP_017832529.1; XM_017977040.1.
DR STRING; 9483.ENSCJAP00000010609; -.
DR Ensembl; ENSCJAT00000011208.4; ENSCJAP00000010609.1; ENSCJAG00000005631.5.
DR GeneID; 100385615; -.
DR KEGG; cjc:100385615; -.
DR CTD; 25831; -.
DR GeneTree; ENSGT00940000156572; -.
DR HOGENOM; CLU_000869_0_0_1; -.
DR OMA; INHTLTM; -.
DR OrthoDB; 1093891at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008225; Chromosome 10.
DR Bgee; ENSCJAG00000005631; Expressed in cerebellum and 6 other cell types or tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
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; 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 2: Evidence at transcript level;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
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 1266..1338
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 2151..2610
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 246..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1496..1515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1592..1611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1674..1757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1777..1797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2297..2318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1675..1700
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1701..1721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1743..1757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2579
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2610 AA; 289358 MW; B3944569AD5071A7 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
AAAGGTVSGP SSACKPGRST TGAPSTTADS KLSNQVSTIV SLLSTLCRGS PVVTHDLLRS
ELPDSIESAL QGDERCVLDT MRLVDLLLVL LFEGRKALPK SSAGSTGRIP GLRRLDSSGE
RSHRQLIDCI RSKDTDALID AIDTGAFEVN FMDDVGQTLL NWASAFGTQE MVEFLCERGA
DVNRGQRSSS LHYAACFGRP QVAKTLLRHG ANPDLRDEDG KTPLDKARER GHSEVVAILQ
SPGDWMCPVN KGDDKKKKDT NKDEEECNEP KGDPEMAPIY LKRLLPVFAQ TFQQTMLPSI
RKASLALIRK MIHFCSEALL KEVCDSDVGH NLPTILVEIT ATVLDQEDDD DGHLLALQII
RDLVDKGGDI FLDQLARLGV ISKVSTLAGP SSDDENEEES KPEKEDEPQE DAKELQQGKP
YHWRDWSIIR GRDCLYIWSD AAALELSNGS NGWFRFILDG KLATMYSSGS PEGGSDSSES
RSEFLEKLQR ARGQVKPSTS SQPILSAPGS TKLTVGNWSL TCLKEGEIAI HNSDGQQATI
LKEDLPGFVF ESNRGTKHSF TAETSLGSEF VTGWTGKRGR KLKSKLEKTK QKVRTMARDL
YDDHFKAVES MPRGVVVTLR NIATQLESSW ELHTNRQCIE SENTWRDLMK TALENLIVLL
KDENTISPYE MCSSGLVQAL LTVLNNSMDL DMKQDCSQLV ERINVFKTAF SENEDDESRP
AVALIRKLIA VLESIERLPL HLYDTPGSTY NLQILTRRLR FRLERAPGET ALIDRTGRML
KMEPLATVES LEQYLLKMVA KQWYDFDRSS FVFVRKLREG QNFIFRHQHD FDENGIIYWT
GTNAKTAYEW VNPAAYGLVV VTSSEGRNLP YGRLEDILSR DNSALNCHSN DDKNAWFAID
LGLWVIPSAY TLRHARGYGR SALRNWVFQV SKDGQNWTSL YTHVDDCSLN EPGSTATWPL
DPPKDEKQGW RHVRIKQMGK NASGQTHYLS LSGFELYGTV NGVCEDQLGK AAKEAEANLR
RQRRLVRSQV LKYMVPGARV IRGLDWKWRD QDGSPQGEGT VTGELHNGWI DVTWDAGGSN
SYRMGAEGKF DLKLAPGYDP DTVASPKPVS STVSGTTQSW SSLVKNNCPD KTSAAAGSSS
RKGSSSSVCS VASSSDISLG STKTERRSEI VMEHSIVSGA DVHEPIVVLS SAENVPQTEV
GSSSSASTST LTAETGSENA ERKLGPDSSV RTPGESSAIS MGIVSVSSPD VSSVSELTNK
EAASQRPLSS SASNRLSVSS LLAAGAPMSS SASVPNLSSR ETSSLESFVR RVANIARTNA
TNNMNLSRSS SDNNTNTLGR NVMSTATSPL MGAQSFPNLT TPGTTSTVTM STSSVTSSSN
VATATTVLSV GQSLSNTLTT SLTSTSSESD TGQEAEYSLY DFLDSCRAST LLAELDDDED
LPEPDEEDDE NEDDNQEDQE YEEVMILRRP SLQRRAGSRS DVTHHAVTSQ LPQVPAGAGS
RPIGEQEEEE YETKGGRRRT WDDDYVLKRQ FSALVPAFDP RPGRTNVQQT TDLEIPPPGT
PHSELLEEVE CTPSPRLALT LKVTGLGTTR EVELPLINFR STIFYYVQKL LQLSCNGNVK
SDKLRRIWEP TYTIMYREMK DSDKEKENGK MGCWSLEHVE QYLGTDELPK NDLITYLQKN
ADAAFLRHWK LTGTNKSIRK NRNCSQLIAA YKDFCEHGTK SGLNQGAIST LQSSDILNLT
KEQPQAKAGN GQNSCGVEDV LQLLRILYIV ASDPYSRISQ EDGDEQPQFT FPPDEFTSKK
ITTKILQQIE EPLALASGAL PDWCEQLTSK CPFLIPFETR QLYFTCTAFG ASRAIVWLQN
RREATVERTR TTSSVRRDDP GEFRVGRLKH ERVKVPRGES LMEWAENVMQ IHADRKSVLE
VEFLGEEGTG LGPTLEFYAL VAAEFQRTDL GAWLCDDNFP DDESRHVDLG GGLKPPGYYV
QRSCGLFTAP FPQDSDELER ITKLFHFLGI FLAKCIQDNR LVDLPISKPF FKLMCMGDIK
SNMSKLIYES RGDRDLHCTE SQSEASTEEG HDSLSVGSFE EDSKSEFILD PPKPKPPAWF
NGILTWEDFE LVNPHRARFL KEIKDLAIKR RQILSNKGLS EDEKNTKLQE LVLKNPSGSG
PPLSIEDLGL NFQFCPSSRI YGFTAVDLKP SGEDEMITMD NAEEYVDLMF DFCMHTGIQK
QMEAFRDGFN KVFPMEKLSS FSHEEVQMIL CGNQSPSWAA EDIINYTEPK LGYTRDSPGF
LRFVRVLCGM SSDERKAFLQ FTTGCSTLPP GGLANLHPRL TVVRKVDATD ASYPSVNTCV
HYLKLPEYSS EEIMRERLLA ATMEKGFHLN
//
