ID H2MU11_ORYLA Unreviewed; 689 AA.
AC H2MU11;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=E3 ubiquitin-protein ligase Midline-1 {ECO:0000256|ARBA:ARBA00013586};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=RING finger protein Midline-1 {ECO:0000256|ARBA:ARBA00031380};
DE AltName: Full=RING-type E3 ubiquitin transferase Midline-1 {ECO:0000256|ARBA:ARBA00033203};
DE AltName: Full=Tripartite motif-containing protein 18 {ECO:0000256|ARBA:ARBA00032675};
GN Name=MID1 {ECO:0000313|Ensembl:ENSORLP00000022270.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000022270.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000022270.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000022270.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000022270.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000022270.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Has E3 ubiquitin ligase activity towards IGBP1, promoting its
CC monoubiquitination, which results in deprotection of the catalytic
CC subunit of protein phosphatase PP2A, and its subsequent degradation by
CC polyubiquitination. {ECO:0000256|ARBA:ARBA00002369}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR AlphaFoldDB; H2MU11; -.
DR STRING; 8090.ENSORLP00000022270; -.
DR Ensembl; ENSORLT00000022271.2; ENSORLP00000022270.2; ENSORLG00000017792.2.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000155821; -.
DR HOGENOM; CLU_013137_19_4_1; -.
DR InParanoid; H2MU11; -.
DR OrthoDB; 5383069at2759; -.
DR TreeFam; TF333654; -.
DR Proteomes; UP000001038; Chromosome 21.
DR Bgee; ENSORLG00000017792; Expressed in pharyngeal gill and 9 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IBA:GO_Central.
DR CDD; cd19836; Bbox1_MID1_C-I; 1.
DR CDD; cd19822; Bbox2_MID1_C-I; 1.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 4.10.830.40; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR047095; MID1_Bbox1_Zfn.
DR InterPro; IPR027727; MID1_Bbox2_Zfn.
DR InterPro; IPR040859; Midline-1_COS.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24099:SF23; E3 UBIQUITIN-PROTEIN LIGASE MIDLINE-1; 1.
DR PANTHER; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1.
DR Pfam; PF18568; COS; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
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:PRU00024}.
FT DOMAIN 10..60
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 172..214
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 342..401
FT /note="COS"
FT /evidence="ECO:0000259|PROSITE:PS51262"
FT DOMAIN 403..513
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 488..681
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 89..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 689 AA; 77958 MW; B46EF4C473D18819 CRC64;
METLESELTC PICLELFEDP LLLPCAHSLC FNCAHRILVS HCTPSEPIQS ISAFQCPTCR
YVISLNQRGL EGLKRNVTLQ NIIDRYQKAS LSGPNSPSET RRERAGPEQK AMSSPADRVQ
CQFCEQDPPQ NAVKTCVTCE VSYCEECLKA THPNKKPFTG HRLIEPFQDS HLKGIMCLEH
EDEKVNMYCV TDEQLICSLC KLVGRHRDHQ VAALTDRYEK LKKPPHRSLC MGPDRSQQEA
DQKTLDSNLS NLIKRTSELE NLMGKLIQTC QQVEVNASKQ EKKLQEECDL LVNIIQQRRQ
IIAAKIKEGK AMRLRKLAQQ IGSCKQCIER SSSLICHADQ TLKESDHASF LQTAKSICER
VSMATASSQI LLPEINLKDA FDTFTLDFSR EKKTLEGLDY LTAPEPPMIR EELCTASYDT
ITVHWTSDDE FSVVSYELQY TIFTNQSNVV SLCNSIDSWM IVPNIKQNHY TVHGLQCGTK
YVFVVKAINQ AGHRSSEPGK LKTNSQPFKL DPKSAHRKLR VSHDNLTVER DETSSKKSHN
QERFSSHNSY GVTGNVYIDS GRHYWEALIG GSTWFAVGIA YKSAPKHEWI GKNSATWVLA
RCNNSWVVRH NSREIPVEPS PHLRRLGVLL DYDSGSLSFY DAVASQHLHT FEISFAQPVC
PVFNVWNRCL TILSGLPVPD HLEGTDYSH
//
