ID S7QC29_MYOBR Unreviewed; 1110 AA.
AC S7QC29;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=D623_10034706 {ECO:0000313|EMBL:EPQ18667.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ18667.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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; KE164550; EPQ18667.1; -; Genomic_DNA.
DR AlphaFoldDB; S7QC29; -.
DR Proteomes; UP000052978; Unassembled WGS sequence.
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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT REPEAT 173..205
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 206..238
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 239..271
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 272..304
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 305..330
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 775..1110
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 33..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1077
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1110 AA; 124523 MW; 15B7AF8C5F649210 CRC64;
MLEECYRMLL QIVIYKFCHM MSLKLLCSKE SDRIEGQGSG SRTTLENQSS GRGDTPKVSP
GSWGTPRHGI AFRTHRPGFC GARVRSHPHT QRGSARVESP GSELRFPEGC ASRGGKGRGG
RKSTRGDGAG CSLRDNETAV YTLMPMVMAD QHRSVSELLS NSKFDVNYAF GRVKRSLLHI
AANCGSVECL VLLLKKGANP NYQDISGCTP LHLAARNGQK KCMSKLLEYS ADVNICNNEG
LTAIHWLAVN GRTELLHDLV QHVSDVDVED AMGQTALHVA CQNGHKTTVQ CLLDSGADIN
RPNVSGATPL YFACSHGQRD TAQILLLRGA KYLPDKNGVT PLDLCVQGGY GETCEVLIQY
HPRLFQTIIQ MTQNEDLREN MLRQVLEHLS QQSESQYLRI LTSLAEVATT NGHKLLSLSS
NYDAQMKSLL RIVRIFCHVF RIGPSSPSNG IDMGYNGNKT PRSQVFKVRK VYDVVMKIDV
KEMNLTKHAF INQKPHTQDP LELLWHSLDE WLVLIATELM KNKKDSTDIT SILLKQKGQD
QDGTSIPPFE PPGPGSYENL STGTRESKPD ALGGKQEAGA DCQDVISMTA NRLSAVIQAF
YMCCSCQMPP GMTSPRFIEF VCKHDEVLKC FVNRNPKIIF DHFHFLLECP ELMSRFMHII
KAQCWHMLAT QQYFLSNHKK IANHMQLHIW QMNKRSSCEV VSKANCAKLK QGIAVRFHGE
EGMPFKDRCE WFYEHLHSGQ ADSDMVHRPV SENDILLVHR DSIFRSSCEV VSKANCAKLK
QGIAVRFHGE EGMGQGVVRE WFDILSNEIV NPDYALFTQS ADGTTFQPNS NSYVNPDHLN
YFRFAGQILG LALNHRQLVN IYFTRSFYKH ILGIPVNYQD VASIDPEYAK NLQWILDNDI
SDLGLELTFS VETDVFGAME EVPLKPGGGS ILVTQNNKEE YVQLVTELRM TRAIQPQINA
FLQGFHMFIP PSLIQLFDEF ELELLLSGMP EIDVSDWIKN TEYTSGYERQ DPVIQWFWEV
VEDITPEERV LLLQFVTGSS RVPHGGFANI MGGSGLQNFT IAAVPYTPNL LPTSSTCINM
LKLPEYPSKE ILKDRLLVAL HCGSYGYTMA
//
