M1IP1_RAT
ID M1IP1_RAT Reviewed; 183 AA.
AC Q6P7D5;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 {ECO:0000250|UniProtKB:Q9CQ20};
GN Synonyms=Mig12 {ECO:0000312|RGD:1303258};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [2]
RP FUNCTION.
RX PubMed=20233797; DOI=10.1210/en.2009-1058;
RA Aipoalani D.L., O'Callaghan B.L., Mashek D.G., Mariash C.N., Towle H.C.;
RT "Overlapping roles of the glucose-responsive genes, S14 and S14R, in
RT hepatic lipogenesis.";
RL Endocrinology 151:2071-2077(2010).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-75, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:20233797}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9CQ20}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9CQ20}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9CQ20}. Note=Associated with microtubules.
CC {ECO:0000250|UniProtKB:Q9CQ20}.
CC -!- SIMILARITY: Belongs to the SPOT14 family. {ECO:0000255}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
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DR EMBL; BC061715; AAH61715.1; -; mRNA.
DR RefSeq; NP_996833.1; NM_206950.1.
DR RefSeq; XP_006256734.1; XM_006256672.3.
DR RefSeq; XP_017457615.1; XM_017602126.1.
DR AlphaFoldDB; Q6P7D5; -.
DR SMR; Q6P7D5; -.
DR STRING; 10116.ENSRNOP00000004305; -.
DR iPTMnet; Q6P7D5; -.
DR PhosphoSitePlus; Q6P7D5; -.
DR PaxDb; Q6P7D5; -.
DR PRIDE; Q6P7D5; -.
DR Ensembl; ENSRNOT00000004305; ENSRNOP00000004305; ENSRNOG00000003228.
DR Ensembl; ENSRNOT00000105819; ENSRNOP00000086843; ENSRNOG00000003228.
DR GeneID; 404280; -.
DR KEGG; rno:404280; -.
DR UCSC; RGD:1303258; rat.
DR CTD; 58526; -.
DR RGD; 1303258; Mid1ip1.
DR eggNOG; ENOG502S0KR; Eukaryota.
DR GeneTree; ENSGT00500000044890; -.
DR HOGENOM; CLU_066079_1_0_1; -.
DR InParanoid; Q6P7D5; -.
DR OMA; RRDMYSH; -.
DR OrthoDB; 1326063at2759; -.
DR PhylomeDB; Q6P7D5; -.
DR TreeFam; TF326826; -.
DR Reactome; R-RNO-200425; Carnitine metabolism.
DR PRO; PR:Q6P7D5; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000003228; Expressed in stomach and 20 other tissues.
DR ExpressionAtlas; Q6P7D5; baseline and differential.
DR Genevisible; Q6P7D5; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0051351; P:positive regulation of ligase activity; ISS:UniProtKB.
DR GO; GO:0051258; P:protein polymerization; ISS:UniProtKB.
DR GO; GO:0046890; P:regulation of lipid biosynthetic process; IMP: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..183
FT /note="Mid1-interacting protein 1"
FT /id="PRO_0000123779"
FT REGION 51..77
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 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPA3"
SQ SEQUENCE 183 AA; 20414 MW; 0E987B0470CAB319 CRC64;
MMQICDTYNQ KHSLFNAMNR FIGAVNNMDQ TVMVPSLLRD VPLSEPDLDN EVSVEVGGSG
SCLEERTTPA PSPGSANGSF FAPSRDMYSH YVLLKSIRND IEWGVLHQPS SPPAGSEEGT
WKPKDILVGL SHLESTDAGE EDLEQQFHYH LRGLHTVLSK LTRKANILTN RYKQEIGFSN
WGH
