ID A0A2Y9Q5R8_DELLE Unreviewed; 957 AA.
AC A0A2Y9Q5R8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=MIB2 {ECO:0000313|RefSeq:XP_022454434.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022454434.1};
RN [1] {ECO:0000313|RefSeq:XP_022454434.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022454434.1};
RG RefSeq;
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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_022454434.1; XM_022598726.2.
DR AlphaFoldDB; A0A2Y9Q5R8; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16726; RING-HC_MIB2_rpt1; 1.
DR CDD; cd02339; ZZ_Mind_bomb; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR042056; MIB1/2_ZZ.
DR InterPro; IPR010606; Mib_Herc2.
DR InterPro; IPR037252; Mib_Herc2_sf.
DR InterPro; IPR040847; SH3_15.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR24202; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR PANTHER; PTHR24202:SF4; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF06701; MIB_HERC2; 2.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF13920; zf-C3HC4_3; 2.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00248; ANK; 9.
DR SMART; SM00184; RING; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF159034; Mib/herc2 domain-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS51416; MIB_HERC2; 2.
DR PROSITE; PS50089; ZF_RING_2; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 1..80
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 86..138
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 149..227
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT REPEAT 464..496
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 497..529
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 530..562
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 633..657
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 667..699
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 834..869
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 913..946
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 957 AA; 103678 MW; B7F862822ACE6017 CRC64;
MEPDPQAGVQ VGMRVVRGVD WKWGQQDGGE GGVGTVVELG RHGSPSTPDR TVVVQWDHGT
RTNYRAGYQG AHDLLLYDNA QIGVRHPNII CDCCKKHGLR GMRWKCRVCF DYDLCTQCYM
HNRHDVAHAF ERYETAHSRP VTLSPRQGLP RIPLRGIFQG AKVVRGPDWE WGSQDGGEGK
PGRVVDIRGW DVETGRSVAS VTWADGTTNV YRVGHKGKVD LKCVGEAAGG FYYREHLPRL
GKPAELRRRV SADGQPFQHG DKVKCLLDAD ILRDMQEGHG GWNPRMAKCI GQMGTVHRIT
DRGDVRVQFS HKTRWTFHPG ALTKHNSCSV GEVVRVIDDL DMVKRLQAGH GEWTDDMAPA
LGHIGRVLKV FGDGNLGVLV NGKLWTFSPS CLVAYRPEED ANLDVAERAR ENKSSLSVVL
DKLRAQKSDL EHPGRLVVEV ALGNVARALD LLRRHPEQVD TKNHGRTALQ VAAYLGQVEL
VRLLLQARAG VDLPDDEGST ALHYAALGNQ PEAARVLLSW GCGANTLNGT RSSALHVAVQ
RGFLEVVRVL CECGCDVNLP DAHADTPLHC AISAGTGASG IVEVLTEVPG IDVTATNSQG
FTLLHHASLK GHTLAVRRIL ARARQLVDAK KEDGFTALHL AALNDHREVA QVLIREGHCD
VNVRNRKLQS PLHLAVQQAH VGLVPLLVDA GCSANAEDEE GDTALHVALQ RHQLLPLATD
GAGGDPGALQ LLSRLQASGL PGSTELTAGA AVACFLALEG ADLSYANHRG RSPLDLAAEG
RLLKALQGCA QRFRERQAGG GGGAAQGPRL ALSAPNTVTN LHVAAPSGPE AAECLVCSEL
ALLVLFSPCQ HRTVCEECAR RMKKCIRCQA VIVKKLRPDG TEVVSAAPAP GPPRQLVEEL
QSRYRQMEER ITCPICIDSH IRLVFQCGHG ACAPCGAALS ACPICRQPIR DRIQIFV
//