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E3 ubiquitin-protein ligase Midline-1 (EC 2.3.2.27) (Midin) (RING finger protein Midline-1) (RING-type E3 ubiquitin transferase Midline-1) (Tripartite motif-containing protein 18)

 TRI18_MOUSE             Reviewed;         680 AA.
O70583; B1AV00; O35418; Q7TPT6;
30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
28-FEB-2018, entry version 169.
RecName: Full=E3 ubiquitin-protein ligase Midline-1;
EC=2.3.2.27;
AltName: Full=Midin;
AltName: Full=RING finger protein Midline-1;
AltName: Full=RING-type E3 ubiquitin transferase Midline-1 {ECO:0000305};
AltName: Full=Tripartite motif-containing protein 18;
Name=Mid1; Synonyms=Fxy, Trim18;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Embryo;
PubMed=9467009; DOI=10.1093/hmg/7.3.489;
Zotto L.D., Quaderi N.A., Elliott R., Lingerfelter P.A., Carrel L.,
Valsecchi V., Montini E., Yen C.-H., Chapman V., Kalcheva I.,
Arrigo G., Zuffardi O., Thomas S., Willard H.F., Ballabio A.,
Disteche C.M., Rugarli E.I.;
"The mouse Mid1 gene: implications for the pathogenesis of Opitz
syndrome and the evolution of the mammalian pseudoautosomal region.";
Hum. Mol. Genet. 7:489-499(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=9342357; DOI=10.1073/pnas.94.22.12030;
Palmer S., Perry J., Kipling D., Ashworth A.;
"A gene spans the pseudoautosomal boundary in mice.";
Proc. Natl. Acad. Sci. U.S.A. 94:12030-12035(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=C3H/He; TISSUE=Osteoblast;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=9722948; DOI=10.1006/geno.1998.5350;
Van den Veyver I.B., Cormier T.A., Jurecic V., Baldini A.,
Zoghbi H.Y.;
"Characterization and physical mapping in human and mouse of a novel
RING finger gene in Xp22.";
Genomics 51:251-261(1998).
[6]
PHOSPHORYLATION.
PubMed=11371618; DOI=10.1073/pnas.111154698;
Liu J., Prickett T.D., Elliott E., Meroni G., Brautigan D.L.;
"Phosphorylation and microtubule association of the Opitz syndrome
protein mid-1 is regulated by protein phosphatase 2A via binding to
the regulatory subunit alpha 4.";
Proc. Natl. Acad. Sci. U.S.A. 98:6650-6655(2001).
-!- FUNCTION: Has E3 ubiquitin ligase activity towards IGBP1,
promoting its monoubiquitination, which results in deprotection of
the catalytic subunit of protein phosphatase PP2A, and its
subsequent degradation by polyubiquitination.
{ECO:0000250|UniProtKB:O15344}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- SUBUNIT: Homodimer or heterodimer with MID2. Interacts with IGBP1.
{ECO:0000250|UniProtKB:O15344}.
-!- INTERACTION:
Q9CQ20:Mid1ip1; NbExp=8; IntAct=EBI-472994, EBI-473024;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15344}.
Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O15344}.
Note=Microtubule-associated. {ECO:0000250|UniProtKB:O15344}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O70583-1; Sequence=Displayed;
Name=2;
IsoId=O70583-2; Sequence=VSP_005736;
Name=3;
IsoId=O70583-3; Sequence=VSP_010811, VSP_005736;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed in fetus and adult. At
E9-E10.5, highest expression found in frontonasal processes,
branchial arches and CNS. From E12.5 to E16.5, high levels found
in rostral part of CNS. At E14.5, begins to be highly expressed in
kidney and lung. At E16.5, highly expressed in the mucosa of the
hindgut and cutaneous region of the stomach.
{ECO:0000269|PubMed:9722948}.
-!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development
with highest levels from E7-E11. Also expressed in the adult.
{ECO:0000269|PubMed:9722948}.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:11371618}.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH53704.1; Type=Erroneous termination; Positions=497; Note=Translated as Gln.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; Y14848; CAA75113.1; -; mRNA.
EMBL; AF026565; AAB83986.1; -; mRNA.
EMBL; AL672015; CAM15638.1; -; Genomic_DNA.
EMBL; CR478112; CAM15638.1; JOINED; Genomic_DNA.
EMBL; CR478112; CAM28195.1; -; Genomic_DNA.
EMBL; AL672015; CAM28195.1; JOINED; Genomic_DNA.
EMBL; BC053704; AAH53704.1; ALT_SEQ; mRNA.
CCDS; CCDS41215.1; -. [O70583-1]
PIR; T09013; T09013.
RefSeq; NP_001277433.1; NM_001290504.1. [O70583-2]
RefSeq; NP_001277434.1; NM_001290505.1. [O70583-2]
RefSeq; NP_001277435.1; NM_001290506.1. [O70583-3]
RefSeq; NP_034927.2; NM_010797.3. [O70583-1]
RefSeq; XP_011246091.1; XM_011247789.2. [O70583-2]
RefSeq; XP_017173897.1; XM_017318408.1. [O70583-1]
RefSeq; XP_017173898.1; XM_017318409.1. [O70583-1]
RefSeq; XP_017173899.1; XM_017318410.1. [O70583-1]
UniGene; Mm.34441; -.
ProteinModelPortal; O70583; -.
SMR; O70583; -.
BioGrid; 201417; 2.
IntAct; O70583; 2.
MINT; O70583; -.
STRING; 10090.ENSMUSP00000038765; -.
iPTMnet; O70583; -.
PhosphoSitePlus; O70583; -.
MaxQB; O70583; -.
PaxDb; O70583; -.
PRIDE; O70583; -.
Ensembl; ENSMUST00000036753; ENSMUSP00000038765; ENSMUSG00000035299. [O70583-1]
Ensembl; ENSMUST00000112104; ENSMUSP00000107732; ENSMUSG00000035299. [O70583-1]
Ensembl; ENSMUST00000112105; ENSMUSP00000107733; ENSMUSG00000035299. [O70583-1]
Ensembl; ENSMUST00000163810; ENSMUSP00000128176; ENSMUSG00000035299. [O70583-1]
Ensembl; ENSMUST00000171433; ENSMUSP00000126746; ENSMUSG00000035299. [O70583-1]
GeneID; 17318; -.
KEGG; mmu:17318; -.
UCSC; uc009uya.2; mouse. [O70583-1]
UCSC; uc009uyc.2; mouse. [O70583-2]
UCSC; uc057ats.1; mouse. [O70583-3]
CTD; 4281; -.
MGI; MGI:1100537; Mid1.
eggNOG; KOG2177; Eukaryota.
eggNOG; ENOG4111G04; LUCA.
GeneTree; ENSGT00760000118878; -.
HOGENOM; HOG000049193; -.
HOVERGEN; HBG056432; -.
InParanoid; O70583; -.
KO; K08285; -.
OMA; WALCRCH; -.
OrthoDB; EOG091G02K9; -.
TreeFam; TF333654; -.
ChiTaRS; Mid1; mouse.
PRO; PR:O70583; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000035299; -.
CleanEx; MM_MID1; -.
ExpressionAtlas; O70583; baseline and differential.
Genevisible; O70583; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
GO; GO:0005874; C:microtubule; ISO:MGI.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0008017; F:microtubule binding; ISO:MGI.
GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; IGI:MGI.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISO:MGI.
GO; GO:0035372; P:protein localization to microtubule; ISO:MGI.
CDD; cd00021; BBOX; 1.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR003649; Bbox_C.
InterPro; IPR003879; Butyrophylin_SPRY.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR017903; COS_domain.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR027727; MID1.
InterPro; IPR006574; PRY.
InterPro; IPR003877; SPRY_dom.
InterPro; IPR027370; Znf-RING_LisH.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
PANTHER; PTHR44073:SF3; PTHR44073:SF3; 1.
Pfam; PF00041; fn3; 1.
Pfam; PF13765; PRY; 1.
Pfam; PF00622; SPRY; 1.
Pfam; PF00643; zf-B_box; 1.
Pfam; PF13445; zf-RING_UBOX; 1.
PRINTS; PR01407; BUTYPHLNCDUF.
SMART; SM00502; BBC; 1.
SMART; SM00336; BBOX; 2.
SMART; SM00060; FN3; 1.
SMART; SM00184; RING; 1.
SMART; SM00449; SPRY; 1.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS50188; B302_SPRY; 1.
PROSITE; PS51262; COS; 1.
PROSITE; PS50853; FN3; 1.
PROSITE; PS50119; ZF_BBOX; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Metal-binding; Microtubule; Phosphoprotein;
Reference proteome; Repeat; Transferase; Ubl conjugation pathway;
Zinc; Zinc-finger.
CHAIN 1 680 E3 ubiquitin-protein ligase Midline-1.
/FTId=PRO_0000056228.
DOMAIN 320 379 COS. {ECO:0000255|PROSITE-
ProRule:PRU00586}.
DOMAIN 384 494 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 495 672 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
ZN_FING 10 60 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 116 165 B box-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
ZN_FING 172 212 B box-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
COILED 205 264 {ECO:0000255}.
METAL 119 119 Zinc 1. {ECO:0000250}.
METAL 122 122 Zinc 1. {ECO:0000250}.
METAL 134 134 Zinc 2. {ECO:0000250}.
METAL 137 137 Zinc 2. {ECO:0000250}.
METAL 142 142 Zinc 1. {ECO:0000250}.
METAL 145 145 Zinc 1. {ECO:0000250}.
METAL 150 150 Zinc 2. {ECO:0000250}.
METAL 159 159 Zinc 2. {ECO:0000250}.
MOD_RES 92 92 Phosphoserine.
{ECO:0000250|UniProtKB:O15344}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000250|UniProtKB:O15344}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000250|UniProtKB:O15344}.
VAR_SEQ 183 220 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_010811.
VAR_SEQ 429 442 NVACDGTCLLGSAG -> S (in isoform 2 and
isoform 3). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9342357,
ECO:0000303|PubMed:9467009}.
/FTId=VSP_005736.
CONFLICT 65 65 L -> P (in Ref. 4; AAH53704).
{ECO:0000305}.
CONFLICT 109 109 N -> D (in Ref. 4; AAH53704).
{ECO:0000305}.
CONFLICT 174 174 M -> T (in Ref. 2; AAB83986).
{ECO:0000305}.
CONFLICT 464 464 H -> Y (in Ref. 4; AAH53704).
{ECO:0000305}.
CONFLICT 523 523 E -> D (in Ref. 1; CAA75113).
{ECO:0000305}.
CONFLICT 633 633 A -> T (in Ref. 2; AAB83986).
{ECO:0000305}.
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


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