ID HECD3_MOUSE Reviewed; 861 AA.
AC Q3U487; B1AUL1; Q3TN76; Q641P3; Q8BQ74; Q8R1L6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 24-JAN-2024, entry version 144.
DE RecName: Full=E3 ubiquitin-protein ligase HECTD3;
DE EC=2.3.2.26;
DE AltName: Full=HECT domain-containing protein 3;
DE AltName: Full=HECT-type E3 ubiquitin transferase HECTD3;
GN Name=Hectd3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Cerebellum, Egg, Kidney, and Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Colon, and Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH STX8.
RX PubMed=18821010; DOI=10.1007/s10571-008-9303-0;
RA Zhang L., Kang L., Bond W., Zhang N.;
RT "Interaction between syntaxin 8 and HECTd3, a HECT domain ligase.";
RL Cell. Mol. Neurobiol. 29:115-121(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: E3 ubiquitin ligases accepts ubiquitin from an E2 ubiquitin-
CC conjugating enzyme in the form of a thioester and then directly
CC transfers the ubiquitin to targeted substrates. Mediates ubiquitination
CC of TRIOBP and its subsequent proteasomal degradation, thus facilitating
CC cell cycle progression by regulating the turn-over of TRIOBP (By
CC similarity). Mediates also ubiquitination of STX8.
CC {ECO:0000250|UniProtKB:Q5T447, ECO:0000269|PubMed:18821010}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with TRIOBP (By similarity). Interacts with STX8.
CC {ECO:0000250|UniProtKB:Q5T447, ECO:0000269|PubMed:18821010}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:18821010}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3U487-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U487-2; Sequence=VSP_019441;
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DR EMBL; AK051385; BAC34620.1; -; mRNA.
DR EMBL; AK139305; BAE23948.1; -; mRNA.
DR EMBL; AK154378; BAE32546.1; -; mRNA.
DR EMBL; AK155290; BAE33170.1; -; mRNA.
DR EMBL; AK155676; BAE33384.1; -; mRNA.
DR EMBL; AK163323; BAE37300.1; -; mRNA.
DR EMBL; AK165482; BAE38213.1; -; mRNA.
DR EMBL; AK170930; BAE42122.1; -; mRNA.
DR EMBL; AL671671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024415; AAH24415.1; -; mRNA.
DR EMBL; BC070411; AAH70411.1; -; mRNA.
DR EMBL; BC082276; AAH82276.1; -; mRNA.
DR CCDS; CCDS18522.1; -. [Q3U487-1]
DR RefSeq; NP_780453.1; NM_175244.3. [Q3U487-1]
DR AlphaFoldDB; Q3U487; -.
DR SMR; Q3U487; -.
DR BioGRID; 218202; 1.
DR STRING; 10090.ENSMUSP00000051922; -.
DR iPTMnet; Q3U487; -.
DR PhosphoSitePlus; Q3U487; -.
DR SwissPalm; Q3U487; -.
DR EPD; Q3U487; -.
DR MaxQB; Q3U487; -.
DR PaxDb; 10090-ENSMUSP00000051922; -.
DR PeptideAtlas; Q3U487; -.
DR ProteomicsDB; 269556; -. [Q3U487-1]
DR ProteomicsDB; 269557; -. [Q3U487-2]
DR Pumba; Q3U487; -.
DR Antibodypedia; 32577; 143 antibodies from 25 providers.
DR DNASU; 76608; -.
DR Ensembl; ENSMUST00000050067.10; ENSMUSP00000051922.10; ENSMUSG00000046861.10. [Q3U487-1]
DR GeneID; 76608; -.
DR KEGG; mmu:76608; -.
DR UCSC; uc008uht.1; mouse. [Q3U487-1]
DR AGR; MGI:1923858; -.
DR CTD; 79654; -.
DR MGI; MGI:1923858; Hectd3.
DR VEuPathDB; HostDB:ENSMUSG00000046861; -.
DR eggNOG; KOG0939; Eukaryota.
DR GeneTree; ENSGT00940000159923; -.
DR HOGENOM; CLU_002173_11_0_1; -.
DR InParanoid; Q3U487; -.
DR OMA; PAWDYTL; -.
DR OrthoDB; 2899647at2759; -.
DR PhylomeDB; Q3U487; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 76608; 1 hit in 78 CRISPR screens.
DR ChiTaRS; Hectd3; mouse.
DR PRO; PR:Q3U487; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q3U487; Protein.
DR Bgee; ENSMUSG00000046861; Expressed in small intestine Peyer's patch and 176 other cell types or tissues.
DR Genevisible; Q3U487; MM.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd08666; APC10-HECTD3; 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; 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR042469; HECTD3.
DR PANTHER; PTHR46654; E3 UBIQUITIN-PROTEIN LIGASE HECTD3; 1.
DR PANTHER; PTHR46654:SF1; E3 UBIQUITIN-PROTEIN LIGASE HECTD3; 1.
DR Pfam; PF03256; ANAPC10; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM01337; APC10; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS50237; HECT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q5T447"
FT CHAIN 2..861
FT /note="E3 ubiquitin-protein ligase HECTD3"
FT /id="PRO_0000241446"
FT DOMAIN 219..397
FT /note="DOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00614"
FT DOMAIN 512..857
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT ACT_SITE 823
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q5T447"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T447"
FT VAR_SEQ 1..651
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019441"
FT CONFLICT 549
FT /note="A -> V (in Ref. 1; BAE32546)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="D -> G (in Ref. 1; BAE38213)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 861 AA; 97347 MW; 305112B035FB9922 CRC64;
MAGPGPGAAL ESPRQLLGRV RFLAEAARSL RAGLPLPAAL AFVPREVLYK LYKDPAGPSR
VLLPVWEAEG LGLRVGAVGA APGTGSGPLR AARDSIELRR GACVRTTGEE LCNGHGLWVK
LTKEQLAEHL SDCSLDEGWL LVCRPAEGGA RLVPIDTPDH LQRQQQLFGV DYRPVLRWEQ
VVDLTYSHRL GSRPQPAEAY TEAIQRLLYV PPTWTYECDE DLIHFLYDHL GKEDENLGSV
KQYVESIDVS SYTEEFNVSC LTDSNADTYW ESDGSQCQHW VRLTMKKGTI VKKLLLTVDT
TDDNFMPKRV VVYGGEGDNL KKLSDVNIDE TLIGDVCVLE DMTVHLPIIE IRIVECRDDG
IDVRLRGVKI KSSRQRELGL NADLFQPASL VRYPRLEGTD PEVLYRRAVL LQRFIKILDS
VLHHLVPAWD HTLGTFSEIK QVKQFLLLSR QRPSLVAQCL RDSESSKPSF MPRLYINRRL
AMEHRACPSR DPACKNAVFT QVYEGLKPSD KYEKPLDYRW PMRYDQWWEC KFIAEGIIDQ
GGGFRDSLAD MSEELCPSSA DTPVPLPFFV RTANQGNGTG EARDMYVPNP SCRDFAKYEW
IGQLMGAALR GKEFLVLALP GFVWKQLSGE EVSWSKDFPA VDSVLVKLLE VMEGVDKETF
EFKFGKELTF TTVLSDQQVV ELIPGGTGIV VEYEDRSRFI QLVRKARLEE SKEQVAAMQA
GLLKVVPQAV LDLLTWQELE KKVCGDPEVT VDALRKLTRF EDFEPSDTRV QYFWEALNNF
TNEDRSRFLR FVTGRSRLPA RIYIYPDKLG YETTDALPES STCSSTLFLP HYASAKVCEE
KLRYAAYNCV AIDTDMSPWE E
//
