HACE1_BOVIN
ID HACE1_BOVIN Reviewed; 909 AA.
AC F1N6G5;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 3.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=E3 ubiquitin-protein ligase HACE1;
DE EC=2.3.2.26;
DE AltName: Full=HECT domain and ankyrin repeat-containing E3 ubiquitin-protein ligase 1;
DE AltName: Full=HECT-type E3 ubiquitin transferase HACE1;
GN Name=HACE1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in Golgi membrane fusion
CC and regulation of small GTPases. Acts as a regulator of Golgi membrane
CC dynamics during the cell cycle: recruited to Golgi membrane by Rab
CC proteins and regulates postmitotic Golgi membrane fusion. Acts by
CC mediating ubiquitination during mitotic Golgi disassembly,
CC ubiquitination serving as a signal for Golgi reassembly later, after
CC cell division. Specifically interacts with GTP-bound RAC1, mediating
CC ubiquitination and subsequent degradation of active RAC1, thereby
CC playing a role in host defense against pathogens. May also act as a
CC transcription regulator via its interaction with RARB.
CC {ECO:0000250|UniProtKB:Q8IYU2}.
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 RARB. Interacts with RAB1 (RAB1A, RAB1B or
CC RAB1C), RAB4 (RAB4A or RAB4B) and RAB11 (RAB11A or RAB11B); in a GTP-
CC dependent manner. Interacts with RAC1; in a GTP-dependent manner.
CC Interacts with the 26S proteasomal complex through the 20S core
CC proteasomal subunit. {ECO:0000250|UniProtKB:Q3U0D9,
CC ECO:0000250|UniProtKB:Q8IYU2}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Endoplasmic reticulum
CC {ECO:0000250}. Note=A significant portion localizes to the endoplasmic
CC reticulum. Targeted to Golgi membrane via its interaction with Rab
CC proteins. {ECO:0000250}.
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DR EMBL; DAAA02026050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026052; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02026053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001179574.2; NM_001192645.2.
DR AlphaFoldDB; F1N6G5; -.
DR SMR; F1N6G5; -.
DR BioGRID; 184176; 1.
DR STRING; 9913.ENSBTAP00000002010; -.
DR PaxDb; F1N6G5; -.
DR PRIDE; F1N6G5; -.
DR Ensembl; ENSBTAT00000002010; ENSBTAP00000002010; ENSBTAG00000001533.
DR GeneID; 527565; -.
DR KEGG; bta:527565; -.
DR CTD; 57531; -.
DR VEuPathDB; HostDB:ENSBTAG00000001533; -.
DR VGNC; VGNC:29739; HACE1.
DR eggNOG; KOG0939; Eukaryota.
DR eggNOG; KOG4177; Eukaryota.
DR GeneTree; ENSGT00940000155839; -.
DR InParanoid; F1N6G5; -.
DR OMA; XELLLSG; -.
DR OrthoDB; 799706at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000001533; Expressed in oocyte and 109 other tissues.
DR ExpressionAtlas; F1N6G5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0061025; P:membrane fusion; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF00632; HECT; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50237; HECT; 1.
PE 3: Inferred from homology;
KW ANK repeat; Cell cycle; Cytoplasm; Endoplasmic reticulum; Golgi apparatus;
KW Membrane; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation pathway.
FT CHAIN 1..909
FT /note="E3 ubiquitin-protein ligase HACE1"
FT /id="PRO_0000415842"
FT REPEAT 64..93
FT /note="ANK 1"
FT REPEAT 97..126
FT /note="ANK 2"
FT REPEAT 130..159
FT /note="ANK 3"
FT REPEAT 163..192
FT /note="ANK 4"
FT REPEAT 196..226
FT /note="ANK 5"
FT REPEAT 228..257
FT /note="ANK 6"
FT DOMAIN 574..909
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 396..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 876
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 909 AA; 102053 MW; 534963EB37072451 CRC64;
MERAMEQLNR LTRSLRRART VELPDDNETA VYTLMPMVMA DQHRSVSELL SNSKFDVNYA
FGRVKRSLLH IAANCGSVEC LVLLLKKGAN PNYQDISGCT PLHLAARNGQ KKCMSKLLEY
SADVNICNNE GLTAIHWLAV NGRTELLHDL VQHVSDVDVE DAMGQTALHV ACQNGHKTTV
QCLLDSGADI NRPNVSGATP LYFACSHGQR DTAQILLLRG AKYLSDKNGV TPLDLCVQGG
YGETCEVLIQ YHPRLFQTII QMTQNEDLRE NMLRQVLEHL SQQSESQYLK ILTSLAEVAT
TNGHKLLSIS SNYDAQMKSL LRIVRIFCHV FRIGPSSPSN GIDMGYNGNK TPRSQVFKPL
ELLWHSLDEW LVLIATELMK NKKDSTDITS ILLKQKGQDQ DGTSIPPFEP PGPGSYENLS
TGTGESKPDV LGGKQEASAD CQDVISMTAN RLSAVIQAFY MCCSCQMPPG MTSPRFIEFV
CKHDEVLKCF VNRNPKIIFD HFHFLLECPE LMSRFMHIIK AQPFKDRCEW FYEHLHSGQP
DSDMVHRPVN ENDILLVHRD SIFRSSCEVV SKANCAKLKQ GIAVRFHGEE GMGQGVVREW
FDILSNEIVN PDYALFTQSA DGTTFQPNSN SSVNPDHLNY FRFAGQILGL ALNHRQLVNI
YFTRSFYKHI LGIPVNYQDV ASIDPEYAKN LQWILDNDIS DLGLELTFSV ETDVFGAMEE
VPLKPGGGSI LVTQNNKAEY VQLVTELRMT RAIQPQINAF LQGFHMFIPP SLIQLFDEYE
LELLLSGMPE IDVSDWIKNT EYTSGYERED PVIQWFWEVV EDITPEERVL LLQFVTGSSR
VPHGGFANIM GGSGLQNFTI AAVPYTPNLL PTSSTCINML KLPEYPSKEI LKDRLLVALH
CGSYGYTMA
