M1IP1_MOUSE
ID M1IP1_MOUSE Reviewed; 182 AA.
AC Q9CQ20; Q8BHT5;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Mid1-interacting protein 1;
DE AltName: Full=Gastrulation-specific G12-like protein;
DE AltName: Full=Mid1-interacting G12-like protein;
DE AltName: Full=Protein STRAIT11499 homolog;
DE AltName: Full=Spot 14-related protein;
DE Short=S14R;
DE Short=Spot 14-R;
GN Name=Mid1ip1; Synonyms=Mig12;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH MID1.
RX PubMed=15070402; DOI=10.1186/1471-2121-5-9;
RA Berti C., Fontanella B., Ferrentino R., Meroni G.;
RT "Mig12, a novel Opitz syndrome gene product partner, is expressed in the
RT embryonic ventral midline and co-operates with Mid1 to bundle and stabilize
RT microtubules.";
RL BMC Cell Biol. 5:9-9(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Mesenchymal cell;
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 [4]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=15890771; DOI=10.1210/en.2005-0204;
RA Zhu Q., Anderson G.W., Mucha G.T., Parks E.J., Metkowski J.K.,
RA Mariash C.N.;
RT "The Spot 14 protein is required for de novo lipid synthesis in the
RT lactating mammary gland.";
RL Endocrinology 146:3343-3350(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-74, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, INTERACTION WITH ACACA AND ACACB, SUBUNIT, INDUCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20457939; DOI=10.1073/pnas.1001292107;
RA Kim C.W., Moon Y.A., Park S.W., Cheng D., Kwon H.J., Horton J.D.;
RT "Induced polymerization of mammalian acetyl-CoA carboxylase by MIG12
RT provides a tertiary level of regulation of fatty acid synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:9626-9631(2010).
RN [8]
RP FUNCTION, INTERACTION WITH THRSP AND ACACA, AND SUBCELLULAR LOCATION.
RX PubMed=20952656; DOI=10.1073/pnas.1012736107;
RA Colbert C.L., Kim C.W., Moon Y.A., Henry L., Palnitkar M., McKean W.B.,
RA Fitzgerald K., Deisenhofer J., Horton J.D., Kwon H.J.;
RT "Crystal structure of Spot 14, a modulator of fatty acid synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18820-18825(2010).
CC -!- FUNCTION: Plays a role in the regulation of lipogenesis in liver. Up-
CC regulates ACACA enzyme activity. Required for efficient lipid
CC biosynthesis, including triacylglycerol, diacylglycerol and
CC phospholipid. Involved in stabilization of microtubules.
CC {ECO:0000269|PubMed:15070402, ECO:0000269|PubMed:20457939,
CC ECO:0000269|PubMed:20952656}.
CC -!- SUBUNIT: Homodimer in the absence of THRSP. Heterodimer with THRSP. The
CC homodimer interacts with ACACA and ACACB. Promotes polymerization of
CC Acetyl-CoA carboxylase to form complexes that contain MID1IP1 and ACACA
CC and/or ACACB. Interaction with THRSP interferes with ACACA binding.
CC {ECO:0000269|PubMed:15070402, ECO:0000269|PubMed:20457939,
CC ECO:0000269|PubMed:20952656}.
CC -!- INTERACTION:
CC Q9CQ20; Q5SWU9: Acaca; NbExp=2; IntAct=EBI-473024, EBI-773043;
CC Q9CQ20; O70583: Mid1; NbExp=8; IntAct=EBI-473024, EBI-472994;
CC Q9CQ20; Q9CQ20: Mid1ip1; NbExp=3; IntAct=EBI-473024, EBI-473024;
CC Q9CQ20; Q13085: ACACA; Xeno; NbExp=4; IntAct=EBI-473024, EBI-717681;
CC Q9CQ20; O00763: ACACB; Xeno; NbExp=4; IntAct=EBI-473024, EBI-2211739;
CC Q9CQ20; G3H9D1: I79_006999; Xeno; NbExp=2; IntAct=EBI-473024, EBI-15884821;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15070402}. Cytoplasm
CC {ECO:0000269|PubMed:15070402, ECO:0000269|PubMed:20457939}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:15070402}. Note=Associated with
CC microtubules (PubMed:15070402).
CC -!- TISSUE SPECIFICITY: During embryonic development, expressed mainly in
CC the neuroepithelial midline, urogenital apparatus and digits. Detected
CC in adult white fat, liver, heart, brain and kidney. Expressed at very
CC low levels in lactating mammary gland. {ECO:0000269|PubMed:15070402,
CC ECO:0000269|PubMed:15890771, ECO:0000269|PubMed:20457939}.
CC -!- INDUCTION: Down-regulated by fasting. Up-regulated by a carbohydrate-
CC rich diet. {ECO:0000269|PubMed:20457939}.
CC -!- SIMILARITY: Belongs to the SPOT14 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP87014.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY263385; AAP87014.1; ALT_INIT; mRNA.
DR EMBL; AK014143; BAB29178.1; -; mRNA.
DR EMBL; AK004021; BAB23129.1; -; mRNA.
DR EMBL; AK090003; BAC41039.1; -; mRNA.
DR EMBL; BC004014; AAH04014.1; -; mRNA.
DR EMBL; BC010778; AAH10778.1; -; mRNA.
DR EMBL; BC052899; AAH52899.1; -; mRNA.
DR CCDS; CCDS30018.1; -.
DR RefSeq; NP_001160107.1; NM_001166635.1.
DR RefSeq; NP_080800.1; NM_026524.4.
DR AlphaFoldDB; Q9CQ20; -.
DR SMR; Q9CQ20; -.
DR BioGRID; 212621; 1.
DR DIP; DIP-31345N; -.
DR IntAct; Q9CQ20; 8.
DR STRING; 10090.ENSMUSP00000111186; -.
DR iPTMnet; Q9CQ20; -.
DR PhosphoSitePlus; Q9CQ20; -.
DR EPD; Q9CQ20; -.
DR jPOST; Q9CQ20; -.
DR MaxQB; Q9CQ20; -.
DR PaxDb; Q9CQ20; -.
DR PRIDE; Q9CQ20; -.
DR ProteomicsDB; 291986; -.
DR Antibodypedia; 24940; 187 antibodies from 33 providers.
DR DNASU; 68041; -.
DR Ensembl; ENSMUST00000008179; ENSMUSP00000008179; ENSMUSG00000008035.
DR Ensembl; ENSMUST00000115524; ENSMUSP00000111186; ENSMUSG00000008035.
DR GeneID; 68041; -.
DR KEGG; mmu:68041; -.
DR UCSC; uc009sqn.2; mouse.
DR CTD; 58526; -.
DR MGI; MGI:1915291; Mid1ip1.
DR VEuPathDB; HostDB:ENSMUSG00000008035; -.
DR eggNOG; ENOG502S0KR; Eukaryota.
DR GeneTree; ENSGT00500000044890; -.
DR HOGENOM; CLU_066079_1_0_1; -.
DR InParanoid; Q9CQ20; -.
DR OMA; RRDMYSH; -.
DR OrthoDB; 1326063at2759; -.
DR PhylomeDB; Q9CQ20; -.
DR TreeFam; TF326826; -.
DR Reactome; R-MMU-200425; Carnitine metabolism.
DR BioGRID-ORCS; 68041; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9CQ20; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9CQ20; protein.
DR Bgee; ENSMUSG00000008035; Expressed in epithelium of stomach and 271 other tissues.
DR ExpressionAtlas; Q9CQ20; baseline and differential.
DR Genevisible; Q9CQ20; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IGI:MGI.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0051351; P:positive regulation of ligase activity; IDA:UniProtKB.
DR GO; GO:0051258; P:protein polymerization; IDA:UniProtKB.
DR GO; GO:0046890; P:regulation of lipid biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR009786; Spot_14.
DR PANTHER; PTHR14315; PTHR14315; 1.
DR Pfam; PF07084; Spot_14; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoskeleton; Lipid biosynthesis; Lipid metabolism;
KW Microtubule; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..182
FT /note="Mid1-interacting protein 1"
FT /id="PRO_0000123778"
FT REGION 55..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPA3"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPA3"
FT CONFLICT 15
FT /note="F -> V (in Ref. 1; BAC41039)"
FT /evidence="ECO:0000305"
SQ 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
