ID A0A3P8YJ21_ESOLU Unreviewed; 684 AA.
AC A0A3P8YJ21;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 28.
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:ENSELUP00000016574.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000016574.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000016574.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000016574.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3P8YJ21; -.
DR Ensembl; ENSELUT00000039817.2; ENSELUP00000016574.2; ENSELUG00000016370.2.
DR GeneTree; ENSGT00940000155821; -.
DR OrthoDB; 5383069at2759; -.
DR Proteomes; UP000265140; LG20.
DR Bgee; ENSELUG00000016370; Expressed in nose and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 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; 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; 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; 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, ECO:0000256|SAM:Coils};
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:UP000265140};
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 173..215
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 323..382
FT /note="COS"
FT /evidence="ECO:0000259|PROSITE:PS51262"
FT DOMAIN 483..676
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 89..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 216..243
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 491..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 684 AA; 77043 MW; 09D1C1EA667BDCFD CRC64;
METLESELTC PICLELFEDP LLLPCAHSLC FNCAHRILVS HCTPNEPVRS IGAFQCPTCR
YVITLSHRGL EGLKRNVTLQ NIIDRFQKAS VSGPNSPSET RRERATAPDS EVMTSCGERV
QCQFCEQDPP QDAVKTCVTC EVSYCDECLK ATHPNKKPFT GHRLIEPMAD CHLRGLMCLE
HEDEKVNMYC VTDEQLICAL CKLVGRHRDH QVAALSDRYE KLKQTLDANL SNLIRRNNEL
ETLMGKLIQT CQHVECNASR QENKLLEECD LLIEIIQQRR QIIATKIKEG KAVRLRKLAQ
QIASCKQIIE RSSSLITQAD HTLKETDPAR FLQTAKNICE RVSMATASSQ ILIPEINLND
TFDTFALDFT REKKMLESLD YLTAPNPPVI REELCTASYD TITVHWTSDD EFCVVSYELQ
YAIFTGQANV VSKYTALVYF STVPLGLCSS ADSWMIVPNI KQNQYTVHGL QCGTKYMFIV
KAINLAGNRN SEPGKLKTNS QPFKLDPKSA HKKLKVSHDN LTVERDETSS KKSHTQDRFT
SQGSYGVTGN VYIDSGRHYW EALIGGSTWF AVGIAYKSAP KHEWIGKNSA SWVLSRCNNS
WVVRHNSKEM PIEPSPHLRR VGVLLDYDAG SLAFYDGAGS QHLYTFDIAF SQPVCPVFNV
WNKCLTVLTG LPIPDHLEAT DCQD
//
