HACE1_XENTR
ID HACE1_XENTR Reviewed; 912 AA.
AC Q28BK1; G1K3F9;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=TEgg040h18.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
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=Q28BK1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q28BK1-2; Sequence=VSP_042380;
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DR EMBL; CR942795; CAJ83645.1; -; mRNA.
DR EMBL; AAMC01096447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01096448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01096449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01096450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01096451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01096452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01096453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01096454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01096455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01096456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001039269.1; NM_001045804.2. [Q28BK1-1]
DR AlphaFoldDB; Q28BK1; -.
DR SMR; Q28BK1; -.
DR STRING; 8364.ENSXETP00000029095; -.
DR PaxDb; Q28BK1; -.
DR GeneID; 734146; -.
DR KEGG; xtr:734146; -.
DR CTD; 57531; -.
DR Xenbase; XB-GENE-5757512; hace1.
DR eggNOG; KOG0939; Eukaryota.
DR eggNOG; KOG4177; Eukaryota.
DR HOGENOM; CLU_015878_0_0_1; -.
DR InParanoid; Q28BK1; -.
DR OMA; PLMEDID; -.
DR OrthoDB; 799706at2759; -.
DR TreeFam; TF323417; -.
DR Reactome; R-XTR-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; 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: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 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..912
FT /note="E3 ubiquitin-protein ligase HACE1"
FT /id="PRO_0000280625"
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 577..912
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT ACT_SITE 879
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT VAR_SEQ 358
FT /note="K -> KVRNVYDVFRKINIKEMNLPNHTLIYQATSEQD (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042380"
SQ SEQUENCE 912 AA; 102876 MW; 9769E2A1A50A8B16 CRC64;
MERAMEQLNR LTRSLRRART VELPEDNETA VYTLMPMVMA DQHRSVLELL SNSKFDVNYA
FGRVKRSLLH IAANCGSVEC LVLLLKRGAD PNYQDISGCT PLHLAARNGQ KKCMSKLLEY
NADVNICNNE GLTAIHWLAV NGRTELLHDL VQHVTNVDVE DAMGQTALHV ACQNGHKTTV
LCLLDSGADI NRPNVSGATP LYFACSHGQR DTAQILLLRG AKYLPDKNGV TPLDLCVQGG
YGETCDILIQ HHPRLFQTLI QMTQNEDLRE NTLRQVLEHL SQQSEVQYLK ILTGLAEVAT
TNGHKLLSIS SSYEAQMKSL LRIVRIFCHV FRIGPSSPNN GNDMGYNGNK TPRNQVFKPL
ELLWHSLDEW LVLIATELTK NKRDSSNIAC ILLKQNQLDQ QDISLAHQSA IGESGSYDHL
SSSTRAEDFE SCSAAGKQEP VADGQDVISM TANRLSAVIQ AFYMCCSCQM PQGMTSPRFI
EFVCKHDDVL KCFVTRNPKI IFDHFHFLLE CPELMSRFMH IIKAQPFKER CEWFYEHLLA
GQPDSDMVHR PVNENDILLV HRDSIFRSSC EVVFKSNCEK LKQGIAVRFH GEEGMGQGVV
REWFDILSSE IINPDYALFT QSADGTTFQP NSNSSVNPDH LNYFRFAGEI LGLALYHRQL
VNIYFTRSFY KHILGIPVNY QDVASIDPEY AKNLQWILDN DISDLGLELT FSVETDVFGA
MEEVPLKPGG ASILVTQENK AEYVQLVTEL RMTRAIQPQI NGFLQGFHMF IPPSLIQLFD
EYELELLLSG MPEIDVNDWM KNTEYTSGYE RDDQVIQWFW EVVQELTQEE RVLLLQFVTG
SSRVPHGGFA YIMGGSGLQN FTIAAVAYTP NLLPTSSTCI NMLKLPEYPS KEILKDRLLV
ALHCGSYGYT MA
