HACE1_XENLA
ID HACE1_XENLA Reviewed; 944 AA.
AC Q6DCL5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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; BC077993; AAH77993.1; -; mRNA.
DR RefSeq; NP_001087077.1; NM_001093608.1.
DR AlphaFoldDB; Q6DCL5; -.
DR SMR; Q6DCL5; -.
DR DNASU; 446912; -.
DR GeneID; 446912; -.
DR KEGG; xla:446912; -.
DR CTD; 446912; -.
DR Xenbase; XB-GENE-5757545; hace1.L.
DR OMA; XELLLSG; -.
DR OrthoDB; 799706at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 446912; Expressed in egg cell and 19 other tissues.
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:0031267; F:small GTPase binding; ISS:UniProtKB.
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:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
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 ANK repeat; Cell cycle; Cytoplasm; Endoplasmic reticulum; Golgi apparatus;
KW Membrane; Reference proteome; Repeat; Transferase; Ubl conjugation pathway.
FT CHAIN 1..944
FT /note="E3 ubiquitin-protein ligase HACE1"
FT /id="PRO_0000280624"
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 609..944
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT ACT_SITE 911
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 944 AA; 106585 MW; 1E87E6F0E6C5E21F 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 QMTQNEELRE NMLRQVLEHL SQQSEVQYLK ILTGLAEVAT
TNGHKLLSIS SSYEAQMKSL LRIVRIFCHV FRIGPSSPNN GNDMGYNGNK TPRNQVFKVR
NVSDVFRKIN IKEMNLPKHT LIYQATSEQD PLELLWHSLD EWLVLIATEL TKNKRDSSNI
ACILLKQSPL DQQDISLAHQ SAIGESGNHD HLLASTRAGD LESCSAIGIQ EPVADGQDVI
SMTANRLSAV IQAFYMCCSC QMPQGMTSPR FIEFVCKHDE VLKCFVTRNP KIIFDHFHFL
LECPELMSRF MHIIKAQPFK ERCEWFYEHL LAGQPDTDMV HRPVNENDIL LVHRDSIFRS
SCEVVFKSNC EKLKQGIAVR FHGEEGMGQG VVREWFDILS SEMINPDYAL FTQSADGTTF
QPNSNSSVNP DHLNYFRFAG EILGLALYHR QLVNIYFTRS FYKHILGIPV NYQDVASIDP
EYAKNLQWIL DNDISDLGLE LTFSVETDVF GAMEEVPLKP GGASILVTQE NKAEYVQLVT
ELRMTRAIQP QINGFLQGFH MFIPPSLIQL FDEYELELLL SGMPEIDVND WMKNTEYTSG
YERDDQVIQW FWEVVQELTQ EERVLLLQFV TGSSRVPHGG FAYIMGGSGL QNFTIAAVAY
TANLLPTSST CINMLKLPEY PSKEILKDRL LVALHCGSYG YTMA
