TRI18_MOUSE
ID TRI18_MOUSE Reviewed; 680 AA.
AC O70583; B1AV00; O35418; Q7TPT6;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=E3 ubiquitin-protein ligase Midline-1;
DE EC=2.3.2.27;
DE AltName: Full=Midin;
DE AltName: Full=RING finger protein Midline-1;
DE AltName: Full=RING-type E3 ubiquitin transferase Midline-1 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 18;
GN Name=Mid1; Synonyms=Fxy, Trim18;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo;
RX PubMed=9467009; DOI=10.1093/hmg/7.3.489;
RA Zotto L.D., Quaderi N.A., Elliott R., Lingerfelter P.A., Carrel L.,
RA Valsecchi V., Montini E., Yen C.-H., Chapman V., Kalcheva I., Arrigo G.,
RA Zuffardi O., Thomas S., Willard H.F., Ballabio A., Disteche C.M.,
RA Rugarli E.I.;
RT "The mouse Mid1 gene: implications for the pathogenesis of Opitz syndrome
RT and the evolution of the mammalian pseudoautosomal region.";
RL Hum. Mol. Genet. 7:489-499(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=9342357; DOI=10.1073/pnas.94.22.12030;
RA Palmer S., Perry J., Kipling D., Ashworth A.;
RT "A gene spans the pseudoautosomal boundary in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:12030-12035(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C3H/He; TISSUE=Osteoblast;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9722948; DOI=10.1006/geno.1998.5350;
RA Van den Veyver I.B., Cormier T.A., Jurecic V., Baldini A., Zoghbi H.Y.;
RT "Characterization and physical mapping in human and mouse of a novel RING
RT finger gene in Xp22.";
RL Genomics 51:251-261(1998).
RN [6]
RP PHOSPHORYLATION.
RX PubMed=11371618; DOI=10.1073/pnas.111154698;
RA Liu J., Prickett T.D., Elliott E., Meroni G., Brautigan D.L.;
RT "Phosphorylation and microtubule association of the Opitz syndrome protein
RT mid-1 is regulated by protein phosphatase 2A via binding to the regulatory
RT subunit alpha 4.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6650-6655(2001).
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:0000250|UniProtKB:O15344}.
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;
CC -!- SUBUNIT: Homodimer or heterodimer with MID2. Interacts with IGBP1.
CC {ECO:0000250|UniProtKB:O15344}.
CC -!- INTERACTION:
CC O70583; Q9CQ20: Mid1ip1; NbExp=8; IntAct=EBI-472994, EBI-473024;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15344}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O15344}.
CC Note=Microtubule-associated. {ECO:0000250|UniProtKB:O15344}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O70583-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O70583-2; Sequence=VSP_005736;
CC Name=3;
CC IsoId=O70583-3; Sequence=VSP_010811, VSP_005736;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in fetus and adult. At 9
CC dpc-10.5 dpc, highest expression found in frontonasal processes,
CC branchial arches and CNS. From 12.5 dpc to 16.5 dpc, high levels found
CC in rostral part of CNS. At 14.5 dpc, begins to be highly expressed in
CC kidney and lung. At 16.5 dpc, highly expressed in the mucosa of the
CC hindgut and cutaneous region of the stomach.
CC {ECO:0000269|PubMed:9722948}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development with
CC highest levels from 7-11 dpc. Also expressed in the adult.
CC {ECO:0000269|PubMed:9722948}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:11371618}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH53704.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y14848; CAA75113.1; -; mRNA.
DR EMBL; AF026565; AAB83986.1; -; mRNA.
DR EMBL; AL672015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR478112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053704; AAH53704.1; ALT_SEQ; mRNA.
DR CCDS; CCDS41215.1; -. [O70583-1]
DR PIR; T09013; T09013.
DR RefSeq; NP_001277433.1; NM_001290504.1. [O70583-2]
DR RefSeq; NP_001277434.1; NM_001290505.1. [O70583-2]
DR RefSeq; NP_001277435.1; NM_001290506.1. [O70583-3]
DR RefSeq; NP_034927.2; NM_010797.3. [O70583-1]
DR RefSeq; XP_011246091.1; XM_011247789.2. [O70583-2]
DR RefSeq; XP_017173897.1; XM_017318408.1. [O70583-1]
DR RefSeq; XP_017173898.1; XM_017318409.1. [O70583-1]
DR RefSeq; XP_017173899.1; XM_017318410.1. [O70583-1]
DR AlphaFoldDB; O70583; -.
DR BMRB; O70583; -.
DR BioGRID; 201417; 4.
DR IntAct; O70583; 2.
DR MINT; O70583; -.
DR STRING; 10090.ENSMUSP00000107733; -.
DR iPTMnet; O70583; -.
DR PhosphoSitePlus; O70583; -.
DR MaxQB; O70583; -.
DR PaxDb; O70583; -.
DR PRIDE; O70583; -.
DR ProteomicsDB; 258972; -. [O70583-1]
DR ProteomicsDB; 258973; -. [O70583-2]
DR ProteomicsDB; 258974; -. [O70583-3]
DR Antibodypedia; 499; 249 antibodies from 27 providers.
DR DNASU; 17318; -.
DR Ensembl; ENSMUST00000036753; ENSMUSP00000038765; ENSMUSG00000035299. [O70583-1]
DR Ensembl; ENSMUST00000112104; ENSMUSP00000107732; ENSMUSG00000035299. [O70583-1]
DR Ensembl; ENSMUST00000112105; ENSMUSP00000107733; ENSMUSG00000035299. [O70583-1]
DR Ensembl; ENSMUST00000163810; ENSMUSP00000128176; ENSMUSG00000035299. [O70583-1]
DR Ensembl; ENSMUST00000171433; ENSMUSP00000126746; ENSMUSG00000035299. [O70583-1]
DR GeneID; 17318; -.
DR KEGG; mmu:17318; -.
DR UCSC; uc009uya.2; mouse. [O70583-1]
DR UCSC; uc009uyc.2; mouse. [O70583-2]
DR UCSC; uc057ats.1; mouse. [O70583-3]
DR CTD; 4281; -.
DR MGI; MGI:1100537; Mid1.
DR VEuPathDB; HostDB:ENSMUSG00000035299; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000155821; -.
DR HOGENOM; CLU_013137_19_4_1; -.
DR InParanoid; O70583; -.
DR OMA; CANNESV; -.
DR PhylomeDB; O70583; -.
DR TreeFam; TF333654; -.
DR BioGRID-ORCS; 17318; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Mid1; mouse.
DR PRO; PR:O70583; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; O70583; protein.
DR Bgee; ENSMUSG00000035299; Expressed in retinal neural layer and 208 other tissues.
DR ExpressionAtlas; O70583; baseline and differential.
DR Genevisible; O70583; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IGI:MGI.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISO:MGI.
DR GO; GO:0035372; P:protein localization to microtubule; ISO:MGI.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IBA:GO_Central.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 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; IPR027727; MID1.
DR InterPro; IPR040859; Midline-1_COS.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR027370; Znf-RING_LisH.
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; PTHR24099:SF23; 1.
DR Pfam; PF18568; COS; 1.
DR Pfam; PF00041; fn3; 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; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 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 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Metal-binding;
KW Microtubule; Phosphoprotein; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..680
FT /note="E3 ubiquitin-protein ligase Midline-1"
FT /id="PRO_0000056228"
FT DOMAIN 320..379
FT /note="COS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT DOMAIN 384..494
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 495..672
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 10..60
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 116..165
FT /note="B box-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 172..212
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 484..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 205..264
FT /evidence="ECO:0000255"
FT COMPBIAS 484..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15344"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15344"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15344"
FT VAR_SEQ 183..220
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010811"
FT VAR_SEQ 429..442
FT /note="NVACDGTCLLGSAG -> S (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9342357, ECO:0000303|PubMed:9467009"
FT /id="VSP_005736"
FT CONFLICT 65
FT /note="L -> P (in Ref. 4; AAH53704)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="N -> D (in Ref. 4; AAH53704)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="M -> T (in Ref. 2; AAB83986)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="H -> Y (in Ref. 4; AAH53704)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="E -> D (in Ref. 1; CAA75113)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="A -> T (in Ref. 2; AAB83986)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 680 AA; 76136 MW; 47D8551531157308 CRC64;
METLESELTC PICLELFEDP LLLPCAHSLC FNCAHRILVS HCATNEPVES INAFQCPTCR
HVITLSQRGL DGLKRNVTLQ NIIDRFQKAS VSGPNSPSET RRERAFDANT MSSAEKVLCQ
FCDQDPAQDA VKTCVTCEVS YCDECLKATH PNKKPFTGHR LIEPIPDSHI RGLMCLEHED
EKVNMYCVTD DQLICALCKL VGRHRDHQVA ALSERYDKLK QNLESNLTNL IKRNTELETL
LAKLIQTCQH VEVNASRQEA KLTEECDLLI EIIQQRRQII GTKIKEGKVI RLRKLAQQIA
NCKQCLERSA SLISQAEHSL KENDHARFLQ TAKNITERVS MATASSQVLI PEINLNDTFD
TFALDFSREK KLLECLDYLT APNPPAIREE LCTASYDTIT VHWTSEDEFS VVSYELQYTI
FTGQANVVNV ACDGTCLLGS AGLCNSADSW MIVPNIKQNH YTVHGLQSGT KYIFTVKAIN
QAGSRSSEPG KLKTNSQPFR LDPKSAHRKL KVSHDNLTVE RDESSSKKSH APERFAGQGS
YGVAGNVFID SGRHYWEVVT SGSTWYAIGL AYRSAPKHEW IGKNAASWAL CRCHNHWAVR
HDGKETPIAP APHLRRVGVL LDYDNGSIAF YDALSSVHLH TFHAALAQPV CPTFTVWNKC
LTIVTGLPIP DHLDCTEQRP
