ID F7BZN4_HORSE Unreviewed; 1040 AA.
AC F7BZN4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 4.
DT 27-MAR-2024, entry version 75.
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|Ensembl:ENSECAP00000012797.4,
GN ECO:0000313|VGNC:VGNC:20170};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000012797.4, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000012797.4, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000012797.4,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000012797.4}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000012797.4};
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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR AlphaFoldDB; F7BZN4; -.
DR STRING; 9796.ENSECAP00000012797; -.
DR PaxDb; 9796-ENSECAP00000012797; -.
DR Ensembl; ENSECAT00000015876.4; ENSECAP00000012797.4; ENSECAG00000014796.4.
DR VGNC; VGNC:20170; MIB2.
DR GeneTree; ENSGT00940000158097; -.
DR HOGENOM; CLU_007287_2_0_1; -.
DR InParanoid; F7BZN4; -.
DR OMA; HDAIGKD; -.
DR TreeFam; TF324147; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002281; Chromosome 2.
DR Bgee; ENSECAG00000014796; Expressed in synovial membrane of synovial joint and 21 other cell types or tissues.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
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); 1.
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; 1.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
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; 1.
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; 1.
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:UP000002281};
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 REGION 879..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..941
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1040 AA; 111827 MW; 19550D5188A6E008 CRC64;
MEPDPQAGVQ VGMRVVRGMD WKWGQQDGGE GGVGTVVELG RHGSPSTPDR TVVVQWDHGT
RTNYRAGYQG AHDLLLYDNA QIGVRHPNII CDCCKKHGLR GMRWKCRVCF DYDLCTQCYM
HSKHDLAHAF ERYETAHSRP VMLSPRQGLP RIPLRGIFQG AKVVRGPDWE WGSQDGGEGK
PGRVVDIRGW DVETGRSVAS VTWADGTTNV YRVGHKGKVD LKCVGEAAGG FYYKEHLPRL
GKPAELQRRV SVDGQPFQHG DKVKCLLDPD ILREMQEGHG GWNPRMAEFI GQTGTVHRIT
DCGDVRVQFS HETRWTFHPG ALTKHNSFWV GDVVRVIDDL DTVKRLQAGH GEWTDDMAPA
LGRVGKVVKV FGDGNLRVAV GGQLWTFSPS CLLAYRPEED ANLDVAERAR ENKSSLSVAL
DKLRAQKSDP EHPGRLVVEV ALGNMARSLD LLRRHPEQVD TKNQGRTALL VAAYLGQVEL
LRLLLKARAD VDLPDDEGNT ALHYAALGNQ PEAARVLLSS GCGANALNGT RSAALHVAVQ
RGFLEVVRVL CEHGCDVNLP DAHADTPLHC AISVGAGASG IVEILTEVPA IDVTATNSQG
FTLLHHASLK GHTLAVRRIL ARARQLVDAK KEDGFTALHL AALNNHREVA QILIREGRCD
VNVRNRKLQS ALHLAVQQAH VGLVPLLVDA GCSVNAEDEE GDTALHVALQ RHQLLPLAAD
GAGGDPGPLQ LLSRLQASGL PGSAELTVGA AMACFLALEG ADVSYSNHRG RSPLDLAVEG
RVLKALQGCA QRCRERQAGG PGGAAPGPRL ALSTPNTVTN LHVAPPSGPE AAECLVCSEL
ALLVLFSPCQ HRTVCEECAR RMKKCIRCQA VIGKKLRPGG WGGAGRASAP PPPPPRCSRP
TRRSPTATGP FAAHAPPPAV RARRIPAPDP DRPPQTARRW PARPPRPARR GSWWRSCRAA
IGKWRSASPA PSASTATSAS CSSAATARAR PAAPRSAPAP SAASPSATAS RSSCSLAAPR
LAPEPRPAFF FASCSPPRVL
//