ID A0A0L8HN89_OCTBM Unreviewed; 949 AA.
AC A0A0L8HN89;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=E3 ubiquitin-protein ligase HACE1 {ECO:0000256|ARBA:ARBA00040370};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE AltName: Full=HECT domain and ankyrin repeat-containing E3 ubiquitin-protein ligase 1 {ECO:0000256|ARBA:ARBA00042378};
DE AltName: Full=HECT-type E3 ubiquitin transferase HACE1 {ECO:0000256|ARBA:ARBA00041409};
GN ORFNames=OCBIM_22010845mg {ECO:0000313|EMBL:KOF90642.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF90642.1};
RN [1] {ECO:0000313|EMBL:KOF90642.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF90642.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF90642.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000256|ARBA:ARBA00037859}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
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DR EMBL; KQ417719; KOF90642.1; -; Genomic_DNA.
DR RefSeq; XP_014770921.1; XM_014915435.1.
DR AlphaFoldDB; A0A0L8HN89; -.
DR STRING; 37653.A0A0L8HN89; -.
DR EnsemblMetazoa; Ocbimv22010845m; Ocbimv22010845m.p; Ocbimv22010845m.g.
DR EnsemblMetazoa; XM_014915435.1; XP_014770921.1; LOC106869625.
DR GeneID; 106869625; -.
DR KEGG; obi:106869625; -.
DR OMA; MPEIDVM; -.
DR OrthoDB; 5480520at2759; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
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 PANTHER; PTHR11254:SF363; E3 UBIQUITIN-PROTEIN LIGASE HACE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
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; 7.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT REPEAT 60..92
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 93..125
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 126..158
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 159..191
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 192..217
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 615..949
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 387..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..440
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 916
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 949 AA; 106910 MW; 642890529EC6321D CRC64;
MEFLQNLASS LKNARTVELP YDDRSAFYML MTMVVANQHK SVLDLLQNSL FDVNYACGRA
QRNLLHIAAN CGSYECLSLL LKKGATVNAR DVSGCTPLHL AARNGKRKCL NKLLEHDADI
NIRNNEGLTT IHWLAVNGRT ELLHDLLLYV NDVDIEDSQG QTAIHVACQN GHNSIVVCLL
DNGSDINRSN HFGSTPLHFA CSHGQRDTAF ILLNRGAKFL PDKKGRTPLD VTVEGGYGET
CALLLSSLPR LFDSLIQMTQ KENIKEKMLY RVLSHLCQHQ SKETADRILL GLAEQAFSIG
QKLFSVSSSL ESEVQCLLRC INFLCKLYQQ VYTTKTKTKS HNLVPLNGTS AANLKANKIF
MPLEVLWKLL GDWLNLLEEE FNNISTKQAG EGPQTQGEGT KIKPADVGES VEVSKDQDNK
EASEDNIDED SCTENTEEGE TSLTEEPKQS EAVVPEEGSE SKDVTENDSS ATTLNIKALP
VRNEDIITAT VPRICAVIQA FYQCCTCLTP KPLTPPTFID FVSRHNKVLK SLVARNPKVI
FDHFHFLLEC PELMSQFLHI IKAQPFEARQ EWFYENLHPE DYNNDMFDSP TSQESLVIDR
QRVFDSSCEM LHKINSGKLK KNISVKFEGE KGMGLGVVRE WFDVLSKEIL NPDYALFTQS
TDGCTFQPNS NSSINPDHLN YFRFAGHILG LALYHRQLLN IYFTRSFYKH ILGIPVNYKD
VSSIDPEYAK NLQWLLDHEI NNLGLNLTFS VQTDVFGMLQ EIELKPGGSK LTVNDSNKHE
YVQLVTELRM TKAIQPQINS FLQGFHEYIP QSLVQMFNEY ELELMLSGLP TIDLLDWKEN
TVYSTYNKDS QVIKWFWDVL DEISVPERIM LLQFVTGSSR VPYGGFANLN GVGTTQKFSV
NHMAYSPGCL PTASTCINLM RLPDYPTMEE LRDRLLVAIH CGSQGYGVA
//
