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Mid1-interacting protein 1 (Gastrulation-specific G12-like protein) (Mid1-interacting G12-like protein) (Protein STRAIT11499 homolog) (Spot 14-related protein) (S14R) (Spot 14-R)

 M1IP1_MOUSE             Reviewed;         182 AA.
Q9CQ20; Q8BHT5;
11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 120.
RecName: Full=Mid1-interacting protein 1;
AltName: Full=Gastrulation-specific G12-like protein;
AltName: Full=Mid1-interacting G12-like protein;
AltName: Full=Protein STRAIT11499 homolog;
AltName: Full=Spot 14-related protein;
Short=S14R;
Short=Spot 14-R;
Name=Mid1ip1; Synonyms=Mig12;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INTERACTION WITH MID1.
PubMed=15070402; DOI=10.1186/1471-2121-5-9;
Berti C., Fontanella B., Ferrentino R., Meroni G.;
"Mig12, a novel Opitz syndrome gene product partner, is expressed in
the embryonic ventral midline and co-operates with Mid1 to bundle and
stabilize microtubules.";
BMC Cell Biol. 5:9-9(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Colon, and Mesenchymal cell;
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).
[4]
IDENTIFICATION, AND TISSUE SPECIFICITY.
PubMed=15890771; DOI=10.1210/en.2005-0204;
Zhu Q., Anderson G.W., Mucha G.T., Parks E.J., Metkowski J.K.,
Mariash C.N.;
"The Spot 14 protein is required for de novo lipid synthesis in the
lactating mammary gland.";
Endocrinology 146:3343-3350(2005).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-74, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
FUNCTION, INTERACTION WITH ACACA AND ACACB, SUBUNIT, INDUCTION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=20457939; DOI=10.1073/pnas.1001292107;
Kim C.W., Moon Y.A., Park S.W., Cheng D., Kwon H.J., Horton J.D.;
"Induced polymerization of mammalian acetyl-CoA carboxylase by MIG12
provides a tertiary level of regulation of fatty acid synthesis.";
Proc. Natl. Acad. Sci. U.S.A. 107:9626-9631(2010).
[8]
FUNCTION, INTERACTION WITH THRSP AND ACACA, AND SUBCELLULAR LOCATION.
PubMed=20952656; DOI=10.1073/pnas.1012736107;
Colbert C.L., Kim C.W., Moon Y.A., Henry L., Palnitkar M.,
McKean W.B., Fitzgerald K., Deisenhofer J., Horton J.D., Kwon H.J.;
"Crystal structure of Spot 14, a modulator of fatty acid synthesis.";
Proc. Natl. Acad. Sci. U.S.A. 107:18820-18825(2010).
-!- FUNCTION: Plays a role in the regulation of lipogenesis in liver.
Up-regulates ACACA enzyme activity. Required for efficient lipid
biosynthesis, including triacylglycerol, diacylglycerol and
phospholipid. Involved in stabilization of microtubules.
{ECO:0000269|PubMed:15070402, ECO:0000269|PubMed:20457939,
ECO:0000269|PubMed:20952656}.
-!- SUBUNIT: Homodimer in the absence of THRSP. Heterodimer with
THRSP. The homodimer interacts with ACACA and ACACB. Promotes
polymerization of Acetyl-CoA carboxylase to form complexes that
contain MID1IP1 and ACACA and/or ACACB. Interaction with THRSP
interferes with ACACA binding. {ECO:0000269|PubMed:15070402,
ECO:0000269|PubMed:20457939, ECO:0000269|PubMed:20952656}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-473024, EBI-473024;
Q13085:ACACA (xeno); NbExp=4; IntAct=EBI-473024, EBI-717681;
Q5SWU9:Acaca; NbExp=2; IntAct=EBI-473024, EBI-773043;
O00763:ACACB (xeno); NbExp=4; IntAct=EBI-473024, EBI-2211739;
G3H9D1:I79_006999 (xeno); NbExp=2; IntAct=EBI-473024, EBI-15884821;
O70583:Mid1; NbExp=8; IntAct=EBI-473024, EBI-472994;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15070402}.
Cytoplasm {ECO:0000269|PubMed:15070402,
ECO:0000269|PubMed:20457939}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:15070402}. Note=Associated with microtubules
(PubMed:15070402).
-!- TISSUE SPECIFICITY: During embryonic development, expressed mainly
in the neuroepithelial midline, urogenital apparatus and digits.
Detected in adult white fat, liver, heart, brain and kidney.
Expressed at very low levels in lactating mammary gland.
{ECO:0000269|PubMed:15070402, ECO:0000269|PubMed:15890771,
ECO:0000269|PubMed:20457939}.
-!- INDUCTION: Down-regulated by fasting. Up-regulated by a
carbohydrate-rich diet. {ECO:0000269|PubMed:20457939}.
-!- SIMILARITY: Belongs to the SPOT14 family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAP87014.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AY263385; AAP87014.1; ALT_INIT; mRNA.
EMBL; AK014143; BAB29178.1; -; mRNA.
EMBL; AK004021; BAB23129.1; -; mRNA.
EMBL; AK090003; BAC41039.1; -; mRNA.
EMBL; BC004014; AAH04014.1; -; mRNA.
EMBL; BC010778; AAH10778.1; -; mRNA.
EMBL; BC052899; AAH52899.1; -; mRNA.
CCDS; CCDS30018.1; -.
RefSeq; NP_001160107.1; NM_001166635.1.
RefSeq; NP_080800.1; NM_026524.4.
UniGene; Mm.29429; -.
ProteinModelPortal; Q9CQ20; -.
SMR; Q9CQ20; -.
BioGrid; 212621; 1.
DIP; DIP-31345N; -.
IntAct; Q9CQ20; 8.
STRING; 10090.ENSMUSP00000008179; -.
iPTMnet; Q9CQ20; -.
PhosphoSitePlus; Q9CQ20; -.
EPD; Q9CQ20; -.
MaxQB; Q9CQ20; -.
PaxDb; Q9CQ20; -.
PRIDE; Q9CQ20; -.
Ensembl; ENSMUST00000008179; ENSMUSP00000008179; ENSMUSG00000008035.
Ensembl; ENSMUST00000115524; ENSMUSP00000111186; ENSMUSG00000008035.
GeneID; 68041; -.
KEGG; mmu:68041; -.
UCSC; uc009sqn.2; mouse.
CTD; 58526; -.
MGI; MGI:1915291; Mid1ip1.
eggNOG; ENOG410IGNP; Eukaryota.
eggNOG; ENOG4111NGS; LUCA.
GeneTree; ENSGT00500000044890; -.
HOGENOM; HOG000001157; -.
HOVERGEN; HBG002528; -.
InParanoid; Q9CQ20; -.
OMA; IEWGVLQ; -.
OrthoDB; EOG091G0Z4G; -.
PhylomeDB; Q9CQ20; -.
TreeFam; TF326826; -.
Reactome; R-MMU-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
PRO; PR:Q9CQ20; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000008035; -.
ExpressionAtlas; Q9CQ20; baseline and differential.
Genevisible; Q9CQ20; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008022; F:protein C-terminus binding; IPI:MGI.
GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; IGI:MGI.
GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IMP:UniProtKB.
GO; GO:0051351; P:positive regulation of ligase activity; IDA:UniProtKB.
GO; GO:0051258; P:protein polymerization; IDA:UniProtKB.
GO; GO:0046890; P:regulation of lipid biosynthetic process; ISS:UniProtKB.
InterPro; IPR009786; Spot_14.
PANTHER; PTHR14315; PTHR14315; 1.
Pfam; PF07084; Spot_14; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Cytoskeleton;
Lipid biosynthesis; Lipid metabolism; Microtubule; Nucleus;
Phosphoprotein; Reference proteome.
CHAIN 1 182 Mid1-interacting protein 1.
/FTId=PRO_0000123778.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9NPA3}.
MOD_RES 71 71 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 74 74 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 78 78 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NPA3}.
CONFLICT 15 15 F -> V (in Ref. 1; BAC41039).
{ECO:0000305}.
SEQUENCE 182 AA; 20356 MW; D5652B81ECEB6003 CRC64;
MMQICDTYNQ KHSLFNAMNR FIGAVNNMDQ TVMVPSLLRD VPLSEPEIDE VSVEVGGSGG
CLEERTTPAP SPGSANESFF APSRDMYSHY VLLKSIRNDI EWGVLHQPSS PPAGSEESTW
KPKDILVGLS HLESADAGEE DLEQQFHYHL RGLHTVLSKL TRKANILTNR YKQEIGFSNW
GH


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