ID   HACE1_CHICK             Reviewed;         942 AA.
AC   E1C656; Q5F340;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 73.
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; ORFNames=RCJMB04_37k12;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red jungle fowl;
RX   PubMed=15592404; DOI=10.1038/nature03154;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA   Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA   Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA   Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA   McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA   Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA   Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA   Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA   Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA   Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA   Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA   Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA   Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA   Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA   Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA   Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA   Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA   Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA   Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA   Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA   Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA   Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA   Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA   Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA   Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA   Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA   Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA   Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide unique
RT   perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
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}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=E1C656-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=E1C656-2; Sequence=VSP_042411;
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ851810; CAH65444.1; -; mRNA.
DR   EMBL; AADN02002150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AADN02002151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AADN02002152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001265084.1; NM_001278155.1. [E1C656-1]
DR   AlphaFoldDB; E1C656; -.
DR   SMR; E1C656; -.
DR   STRING; 9031.ENSGALP00000024820; -.
DR   PaxDb; E1C656; -.
DR   PRIDE; E1C656; -.
DR   Ensembl; ENSGALT00000024865; ENSGALP00000024819; ENSGALG00000015415. [E1C656-1]
DR   Ensembl; ENSGALT00000086898; ENSGALP00000060303; ENSGALG00000015415. [E1C656-2]
DR   GeneID; 421788; -.
DR   KEGG; gga:421788; -.
DR   CTD; 57531; -.
DR   VEuPathDB; HostDB:geneid_421788; -.
DR   eggNOG; KOG0939; Eukaryota.
DR   eggNOG; KOG4177; Eukaryota.
DR   GeneTree; ENSGT00940000155839; -.
DR   HOGENOM; CLU_015878_0_0_1; -.
DR   InParanoid; E1C656; -.
DR   OMA; XELLLSG; -.
DR   OrthoDB; 799706at2759; -.
DR   PhylomeDB; E1C656; -.
DR   TreeFam; TF323417; -.
DR   Reactome; R-GGA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:E1C656; -.
DR   Proteomes; UP000000539; Chromosome 3.
DR   Bgee; ENSGALG00000015415; Expressed in spermatid and 13 other tissues.
DR   ExpressionAtlas; E1C656; 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: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; 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   2: Evidence at transcript level;
KW   Alternative splicing; ANK repeat; Cell cycle; Cytoplasm;
KW   Endoplasmic reticulum; Golgi apparatus; Membrane; Reference proteome;
KW   Repeat; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..942
FT                   /note="E3 ubiquitin-protein ligase HACE1"
FT                   /id="PRO_0000415844"
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          607..942
FT                   /note="HECT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   REGION          428..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        909
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   VAR_SEQ         626..942
FT                   /note="GQGVVREWFDILSSEIVNPDYALFTQSADGTTFQPNSNSSVNPDHLNYFRFA
FT                   GQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLG
FT                   LELTFSVETDVFGAMEEVPLKPGGASILVTQENKAEYVQLVTELRMTRAIQPQINAFLQ
FT                   GFHMFIPPSLIQLFDEYELELLLSGMPEIDVNDWLKNTEYTSGYERGDQVIQWFWDVVE
FT                   ELTQEERVLLLQFVTGSSRVPHGGFAHIMGGSGLQNFTIAAVPYTANLLPTSSTCINML
FT                   KLPEYPSKEILKDRLLVALHCGSYGYTMA -> EQPSSQTATLL (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:15642098"
FT                   /id="VSP_042411"
SQ   SEQUENCE   942 AA;  106295 MW;  BF1BB453CAACD295 CRC64;
     MERAMEQLNR LTRSLRRART VELPDDNETA VYTLMPMVMA DQHRSVSELL SNSKFDVNYA
     FGRVKRSLLH IAANCGSVEC LVLLLKKGAN PNYQDISGCT PLHLAARNGQ KKCMSKLLEY
     SADVNICNNE GLTAIHWLAV NGRTELLHDL VQHVSNVDVE DAMGQTALHV ACQNGHKTTV
     QCLLDSGADI NRPNVSGATP LYFACSHGQR DTAQILLMRG AKYLPDKNGI TPLDLCVQGG
     YGETCEVLIQ YHPRLFQTII QMTQNEDLRE NMLRQVLEHL SQQSESQYLK ILTSLAEVAT
     TNGHKLLSLS SNYEAQMKSL LRIVRIFCHV FRIGPSSPSN GNDMGYNGNK TPRSQVFKVR
     KVYDVVRKID VKEMNFTKHA FINQTSHEQE PLELLWHSLD EWLVLIATEL MKNKRDSANI
     TSILLKQKGP DHQDATPTPS FAAAGTESRK ELSTDTGDSK TYEVAGKQEA YADCQDVISM
     TANRLSAVIQ AFYMCCSCQM PQGMTSPRFI EFVCKHDDVL KCFVNRNPKI IFDHFHFLLE
     CPELMSRFMH IIKAQPFKDR CEWFYEHLHS GQPDSDMVHR PVNENDILLV HRDSIFRSSC
     EVVSKANCAK LKQGIAVRFH GEEGMGQGVV REWFDILSSE IVNPDYALFT QSADGTTFQP
     NSNSSVNPDH LNYFRFAGQI LGLALNHRQL VNIYFTRSFY KHILGIPVNY QDVASIDPEY
     AKNLQWILDN DISDLGLELT FSVETDVFGA MEEVPLKPGG ASILVTQENK AEYVQLVTEL
     RMTRAIQPQI NAFLQGFHMF IPPSLIQLFD EYELELLLSG MPEIDVNDWL KNTEYTSGYE
     RGDQVIQWFW DVVEELTQEE RVLLLQFVTG SSRVPHGGFA HIMGGSGLQN FTIAAVPYTA
     NLLPTSSTCI NMLKLPEYPS KEILKDRLLV ALHCGSYGYT MA