ID D3K5N2_PIG Unreviewed; 909 AA.
AC D3K5N2; A0A287ASW0; F1RYQ6;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 90.
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 Name=HACE1 {ECO:0000313|EMBL:ADC38910.1,
GN ECO:0000313|Ensembl:ENSSSCP00000047186.2,
GN ECO:0000313|VGNC:VGNC:88769};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:ADC38910.1};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000047186.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000047186.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADC38910.1}
RP NUCLEOTIDE SEQUENCE.
RA Yg L.;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:HCZ93612.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [4] {ECO:0000313|Ensembl:ENSSSCP00000047186.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; GU373710; ADC38910.1; -; mRNA.
DR EMBL; DQIR01038137; HCZ93612.1; -; Transcribed_RNA.
DR EMBL; DQIR01088828; HDA44304.1; -; Transcribed_RNA.
DR EMBL; DQIR01320751; HDC76225.1; -; Transcribed_RNA.
DR EMBL; DQIR01321642; HDC77116.1; -; Transcribed_RNA.
DR RefSeq; NP_001182269.1; NM_001195340.1.
DR PaxDb; 9823-ENSSSCP00000004709; -.
DR Ensembl; ENSSSCT00000048824.3; ENSSSCP00000047186.2; ENSSSCG00000004364.5.
DR GeneID; 100156102; -.
DR KEGG; ssc:100156102; -.
DR CTD; 57531; -.
DR VGNC; VGNC:88769; HACE1.
DR eggNOG; KOG0939; Eukaryota.
DR eggNOG; KOG4177; Eukaryota.
DR GeneTree; ENSGT00940000155839; -.
DR OMA; MPEIDVM; -.
DR OrthoDB; 5480520at2759; -.
DR Proteomes; UP000008227; Chromosome 1.
DR Bgee; ENSSSCG00000004364; Expressed in hindlimb bud and 45 other cell types or 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: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; 2.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF00632; HECT; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
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; 5.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50237; HECT; 1.
PE 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:D3K5N2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT REPEAT 64..96
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 97..129
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 130..162
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 163..195
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 196..221
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 574..909
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 395..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 876
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 909 AA; 102148 MW; 8EEAC8A0ACFFCC66 CRC64;
MERAMEQLNR LTRSLRRART VELPDDNETA VYTLMPMVMA DQHRSVSELL SNSKFDVNYA
FGRVKRSLLH IAANCGSVEC LVLLLKKGAN PNYQDISGCT PLHLAARNGQ KKCMSKLLEY
CADVNICNNE GLTAIHWLAV NGRTELLHDL VQHVSDVDVE DAMGQTALHV ACQNGHKTTV
QCLLDSGADI NRPNVSGATP LYFACSHGQR DTAQILLLRG AKYLPDKNGV TPLDLCVQGG
YGETCEVLIQ YHPRLFQTII QMTQNEDLRE NMLRQVLEHL SQQSESQYLK ILTSLAEVAT
TNGHKLLSIS SNYDAQMKSL LRIVRIFCHV FRIGPSSPSN GIDMGYNGNK TPRSQVFKPL
ELLWHSLDEW LVLIATELMK NKKDSTDITS ILLKQKGQDQ DGTSIPSFEP PGPGSYENLS
TGTGESKPDA LGGKQETSAD CQDVISMTAN RLSAVIQAFY MCCSCQMPPG MTSPRFIEFV
CKHDEVLKCF VNRNPKIIFD HFHFLLECPE LMSRFMHIIK AQPFKDRCEW FYEHLHSGQP
DSDMVHRPVN ENDILLVHRD SIFRSSCEVV SKANCAKLKQ GIAVRFHGEE GMGQGVVREW
FDILSNEIVN PDYALFTQSA DGTTFQPNSN SYVNPDHLNY FRFAGQILGL ALNHRQLVNI
YFTRSFYKHI LGIPVNYQDV ASIDPEYAKN LQWILDNDIS DLGLELTFSV ETDVFGAMEE
VPLKPGGGSI LVTQNNKAEY VQLVTELRMT RAIQPQINAF LQGFHMFIPP SLIQLFDEYE
LELLLSGMPE IDVSDWIKNT EYTSGYERED PVIQWFWEVV EDITPEERVL LLQFVTGSSR
VPHGGFANIM GGSGLQNFTI AAVPYTPNLL PTSSTCINML KLPEYPSKEI LKDRLLVALH
CGSYGYTMA
//
