F120A_MOUSE
ID F120A_MOUSE Reviewed; 1112 AA.
AC Q6A0A9; A0PJK6; B3DFJ0; Q91Z16;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Constitutive coactivator of PPAR-gamma-like protein 1;
DE AltName: Full=Oxidative stress-associated Src activator;
DE AltName: Full=Protein FAM120A;
GN Name=FAM120A; Synonyms=Kiaa0183, Ossa;
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 [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-1112.
RC STRAIN=FVB/N; TISSUE=Brain, and Mammary tumor;
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 [3]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH PURA, AND
RP FUNCTION.
RX PubMed=18413649; DOI=10.1369/jhc.2008.950733;
RA Kobayashi Y., Suzuki K., Kobayashi H., Ohashi S., Koike K., Macchi P.,
RA Kiebler M., Anzai K.;
RT "C9orf10 protein, a novel protein component of Puralpha-containing mRNA-
RT protein particles (Puralpha-mRNPs): characterization of developmental and
RT regional expressions in the mouse brain.";
RL J. Histochem. Cytochem. 56:723-731(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-930, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-871; ARG-882; ARG-884 AND
RP ARG-980, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Critical component of the oxidative stress-induced survival
CC signaling. Activates src family kinases and acts as a scaffolding
CC protein enabling src family kinases to phosphorylate and activate PI3-
CC kinase. Binds RNA and promotes the secretion of IGF-II (By similarity).
CC May participate in mRNA transport in the cytoplasm. {ECO:0000250,
CC ECO:0000269|PubMed:18413649}.
CC -!- SUBUNIT: Interacts with YES1, SRC, FYN. Upon tyrosine phosphorylation,
CC interacts with PIK3R1 (By similarity). Interacts with PURA.
CC {ECO:0000250, ECO:0000269|PubMed:18413649}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=Translocates to plasma membrane upon
CC ultraviolet exposure. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Present in Purkinje cells in the cerebellum, and in
CC cortical neurons (at protein level). {ECO:0000269|PubMed:18413649}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing brain at 12 dpc.
CC Expression increases postnatally and is maintained at an adult level
CC beyond 4 weeks after birth. {ECO:0000269|PubMed:18413649}.
CC -!- PTM: Arg-980 is dimethylated, probably to asymmetric dimethylarginine.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine by src family kinases upon ultraviolet
CC exposure. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the constitutive coactivator of PPAR-gamma
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32187.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK172909; BAD32187.1; ALT_INIT; mRNA.
DR EMBL; BC010304; AAH10304.1; -; mRNA.
DR EMBL; BC042582; AAH42582.1; -; mRNA.
DR EMBL; BC158134; AAI58135.1; -; mRNA.
DR CCDS; CCDS49259.1; -.
DR RefSeq; NP_001028440.2; NM_001033268.2.
DR AlphaFoldDB; Q6A0A9; -.
DR BioGRID; 230005; 17.
DR IntAct; Q6A0A9; 8.
DR MINT; Q6A0A9; -.
DR STRING; 10090.ENSMUSP00000053877; -.
DR iPTMnet; Q6A0A9; -.
DR PhosphoSitePlus; Q6A0A9; -.
DR SwissPalm; Q6A0A9; -.
DR EPD; Q6A0A9; -.
DR jPOST; Q6A0A9; -.
DR MaxQB; Q6A0A9; -.
DR PaxDb; Q6A0A9; -.
DR PeptideAtlas; Q6A0A9; -.
DR PRIDE; Q6A0A9; -.
DR ProteomicsDB; 275494; -.
DR Antibodypedia; 13858; 135 antibodies from 30 providers.
DR DNASU; 218236; -.
DR Ensembl; ENSMUST00000060805; ENSMUSP00000053877; ENSMUSG00000038014.
DR GeneID; 218236; -.
DR KEGG; mmu:218236; -.
DR UCSC; uc007qio.1; mouse.
DR CTD; 23196; -.
DR MGI; MGI:2446163; Fam120a.
DR VEuPathDB; HostDB:ENSMUSG00000038014; -.
DR eggNOG; ENOG502QQNQ; Eukaryota.
DR GeneTree; ENSGT00530000063168; -.
DR HOGENOM; CLU_008339_2_0_1; -.
DR InParanoid; Q6A0A9; -.
DR OMA; NDGLMRG; -.
DR OrthoDB; 203269at2759; -.
DR PhylomeDB; Q6A0A9; -.
DR TreeFam; TF328642; -.
DR BioGRID-ORCS; 218236; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Fam120a; mouse.
DR PRO; PR:Q6A0A9; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q6A0A9; protein.
DR Bgee; ENSMUSG00000038014; Expressed in ciliary body and 257 other tissues.
DR Genevisible; Q6A0A9; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR026784; Coact_PPARg.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR PANTHER; PTHR15976; PTHR15976; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Membrane; Methylation;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..1112
FT /note="Constitutive coactivator of PPAR-gamma-like protein
FT 1"
FT /id="PRO_0000363780"
FT REGION 339..403
FT /note="Interaction with YES1, SRC and FYN"
FT /evidence="ECO:0000250"
FT REGION 372..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..1112
FT /note="RNA binding"
FT /evidence="ECO:0000250"
FT REGION 919..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 653
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZB2"
FT MOD_RES 871
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 882
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 884
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 930
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 958
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZB2"
FT MOD_RES 980
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 984
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZB2"
FT MOD_RES 1021
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZB2"
FT MOD_RES 1042
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZB2"
SQ SEQUENCE 1112 AA; 121646 MW; 5B9086869336B9D6 CRC64;
MGVQGFQDYI EKHCPSAVVP VELQKLARGS LVGGGRQRPP QTPLRLLVDA DNCLHRLYGG
FYTDWVSGGQ WNHMLGYLAA LAKACFGGNI ELFVFFNGAL EKARLHEWVK RQGNERQTAQ
QIVSHVQNKG TPPPKVWFLP PVCMAHCIRL ALIRFHVKVA QSIEDHHQEV IGFCRENGFH
GLVAYDSDYA LCNIPYYFSA HALKLSRNGK SLTTSQYLMH EVAKQLDLNP NRFPIFAALL
GNHILPDEDL ASFHWSLLGP EHPLASLKVR AHQLVLPPCD VVIKAVADYV RNIHDTSDLD
AIAKDVFQHS QSRTDDKVIR FKRAVGYYSA TSKPMPFHPP HYLARPNPFG MPGMVPPYVP
PQMLNIPQTS LQAKPAVPQV PSPGGTPGQA PYPYSLSEPA LTLDTSGKNL TEQNSYSNIP
HEGKHTPLYE RSSPINLAQS GSPNHVDSAY FPGSSTSSSS DNDEGGGGAT NHISGNKIGW
EKTGSHAEPL ARGDPGDQVK VEGSSTASSG SQLAEGKGSH MGTVQPIPCL LSMPTRNHMD
ITTPPLPPVA PEVLRVAEHR HKKGLMYPYI FHILTKGEIK IAVSIEDEAN KDLPPAALLY
RPVRQYVYGV LFSLAESRKK TERLAFRKNR LPPEFSPLII KEWAAYKGKS PQTPELVEAL
AFREWTCPNL KRLWLGKAVE DKNRRMRAFL ACMRSDTPAM LNPANVPTHL MVLCCVLRYM
VQWPGARILR RQELDAFLAQ ALSPKLYEPD QLQELKIDNL DPRGIQLSAL FMSGVDMALF
ANDACGQPIP WEHCCPWMYF DGKLFQSKLL KASREKTPLI DLCDGQAEQA AKVEKMRQSI
LEGLSFSRQN HPLPFPPPPA LPFYPASVYP RHFGPVPPSQ GRGRGFAGVC GFGGHYGETV
ATGPYRAFRV TAASGHCGAF SGSDSSRTSK SQGGVQPIPS QGGKLEIAGT VVGHWAGSRR
GRGGRGPFPL QVVSVGGPAR GRPRGVISTP VIRTFGRGGR YYGRGYKSQG AIQGRPPYAA
SAEEVAKELK SKSGESKSSA VSLAENGVMA EEKPVPQLNG STGDPRVPSH SESALNNDSK
PCNTNPHLNA LSTDSACRRE AALEAAVLNK EE
