ID   HACE1_DANRE             Reviewed;         904 AA.
AC   F8W2M1; E7F3X1;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 2.
DT   03-AUG-2022, entry version 60.
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   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
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. {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   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000250}. Cytoplasm {ECO:0000250}. Endoplasmic reticulum
CC       {ECO:0000250}.
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DR   EMBL; CU928063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F8W2M1; -.
DR   SMR; F8W2M1; -.
DR   STRING; 7955.ENSDARP00000084288; -.
DR   PaxDb; F8W2M1; -.
DR   ZFIN; ZDB-GENE-110411-52; hace1.
DR   eggNOG; KOG0939; Eukaryota.
DR   eggNOG; KOG4177; Eukaryota.
DR   InParanoid; F8W2M1; -.
DR   OMA; XELLLSG; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:F8W2M1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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: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:0003190; P:atrioventricular valve formation; IMP:ZFIN.
DR   GO; GO:0003208; P:cardiac ventricle morphogenesis; IMP:ZFIN.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR   GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR   GO; GO:0061025; P:membrane fusion; ISS:UniProtKB.
DR   GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IMP:ZFIN.
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; 1.
DR   Pfam; PF13637; Ank_4; 1.
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; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..904
FT                   /note="E3 ubiquitin-protein ligase HACE1"
FT                   /id="PRO_0000415845"
FT   REPEAT          34..63
FT                   /note="ANK 1"
FT   REPEAT          68..97
FT                   /note="ANK 2"
FT   REPEAT          101..130
FT                   /note="ANK 3"
FT   REPEAT          134..163
FT                   /note="ANK 4"
FT   REPEAT          167..196
FT                   /note="ANK 5"
FT   REPEAT          200..230
FT                   /note="ANK 6"
FT   REPEAT          232..261
FT                   /note="ANK 7"
FT   DOMAIN          569..904
FT                   /note="HECT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   ACT_SITE        871
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   904 AA;  102165 MW;  EF05A362A6987FE0 CRC64;
     MERAMEHLNV QLNRLTRSLR RARTVELPED SETAVYTLMP MVMADQHRSV SELLLNSKFD
     VNYAFGRVKR SLLHIAANCG SVECLVLLLK RGANPNYQDI SGCTPLHLAA RNGQKKCMGR
     LLEYNADVNI CNNEGLTAIH WLAVNGRTEL LHDLVQHVTN VDVEDAMGQT ALHVACQNGH
     KTTVQCLLDS GADINRPNVS GATPLYFACS HGQRDTAQIL LLRGAKYLPD RNGVTPLDLC
     VQGGYGETCE ILIQHHGRLF QTLIQMTQND DIKENMLRQV LEHVSQQNDS NYQRILTSLA
     EVATTNGHKL LSLSSNFEVQ TKSLLRIIRI FCHVFCLGPS SPNNGNDMGY NGNKTPRSQV
     FKPLELLWHS LDEWLVLIST ELEKEITDTT RSSSGNDIAS LFLKKQEVDH SVSSENPQLL
     LDASSVMKTP EVYADGQDVI SMIANRLSAV IQAFYMCCSC QMPHGMTSPR FIEFVCKHDE
     VLKCFVTRNP KIIFNHFHFL LECPELMSRF MHIIKGQPFK DRCEWFYEHL LAGQPDSDMV
     HRPVNENDIL LVHRDSLFRS SCEVVSKSSN EKLKQGIAVR FHGEEGMGQG VVREWFDILS
     NEIINPDYAL FTQSADGTTF QPNSNSSVNP DHLNYFRFAG QILGLALYHR QLVNIYFTRS
     FYKHILGIPV SYQDVSSIDP EYAKNLQWIL DNDISDLGLE LTFSVETDVF GTMEEVPLKP
     GGTTIQVTQD NKEEYVQLVT ELRMTRAIQP QINAFLQGFH TFIPPSLIQL FDEYELELLL
     SGMPEIDVMD WKRNTEYTSG YDLQEPVIQW FWEVVENLTQ EERVLLLQFV TGSSRVPHGG
     FAFLMGGSGL QKFTVAAVPY TSNLLPTSST CINMLKLPEY PSKDVLRDRL LVALHCGSYG
     YTMA