GGYF1_MOUSE
ID GGYF1_MOUSE Reviewed; 1044 AA.
AC Q99MR1; Q571A0; Q6Y7W9;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=GRB10-interacting GYF protein 1;
DE AltName: Full=PERQ amino acid-rich with GYF domain-containing protein 1;
GN Name=Gigyf1; Synonyms=Kiaa4110, Perq1;
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 [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W.,
RA Koop B.F.;
RT "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL Nucleic Acids Res. 29:1352-1365(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH GRB10,
RP MUTAGENESIS OF TRP-500; GLY-504; TYR-505 AND PHE-506, AND FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=12771153; DOI=10.1074/jbc.m211572200;
RA Giovannone B., Lee E., Laviola L., Giorgino F., Cleveland K.A., Smith R.J.;
RT "Two novel proteins that are linked to insulin-like growth factor (IGF-I)
RT receptors by the Grb10 adapter and modulate IGF-I signaling.";
RL J. Biol. Chem. 278:31564-31573(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 308-1041.
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-28; SER-137 AND
RP SER-343, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Liver, Lung, 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).
CC -!- FUNCTION: May act cooperatively with GRB10 to regulate tyrosine kinase
CC receptor signaling. May increase IGF1 receptor phosphorylation under
CC IGF1 stimulation as well as phosphorylation of IRS1 and SHC1.
CC {ECO:0000269|PubMed:12771153}.
CC -!- SUBUNIT: Interacts with GRB10 (PubMed:12771153). This transient binding
CC is increased under IGF1 stimulation and leads to recruitment of
CC GIGYF1/GRB10 complex to IGF1 receptor (PubMed:12771153). Interacts with
CC DDX6 (By similarity). {ECO:0000250|UniProtKB:O75420,
CC ECO:0000269|PubMed:12771153}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Lower expression in skeletal muscle,
CC liver and testis. {ECO:0000269|PubMed:12771153}.
CC -!- SIMILARITY: Belongs to the GIGYF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK28827.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF312033; AAK28827.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY176042; AAO46886.1; -; mRNA.
DR EMBL; AK220289; BAD90214.1; -; mRNA.
DR CCDS; CCDS51673.1; -.
DR RefSeq; NP_113596.2; NM_031408.2.
DR RefSeq; XP_011239256.1; XM_011240954.1.
DR AlphaFoldDB; Q99MR1; -.
DR SMR; Q99MR1; -.
DR BioGRID; 208260; 5.
DR IntAct; Q99MR1; 1.
DR MINT; Q99MR1; -.
DR STRING; 10090.ENSMUSP00000031727; -.
DR iPTMnet; Q99MR1; -.
DR PhosphoSitePlus; Q99MR1; -.
DR EPD; Q99MR1; -.
DR jPOST; Q99MR1; -.
DR MaxQB; Q99MR1; -.
DR PaxDb; Q99MR1; -.
DR PeptideAtlas; Q99MR1; -.
DR PRIDE; Q99MR1; -.
DR ProteomicsDB; 268875; -.
DR Antibodypedia; 16628; 88 antibodies from 17 providers.
DR DNASU; 57330; -.
DR Ensembl; ENSMUST00000031727; ENSMUSP00000031727; ENSMUSG00000029714.
DR GeneID; 57330; -.
DR KEGG; mmu:57330; -.
DR UCSC; uc009acp.1; mouse.
DR CTD; 64599; -.
DR MGI; MGI:1888677; Gigyf1.
DR VEuPathDB; HostDB:ENSMUSG00000029714; -.
DR eggNOG; KOG1862; Eukaryota.
DR GeneTree; ENSGT00940000159845; -.
DR HOGENOM; CLU_007300_0_0_1; -.
DR InParanoid; Q99MR1; -.
DR OMA; FHNTGEC; -.
DR OrthoDB; 412069at2759; -.
DR PhylomeDB; Q99MR1; -.
DR TreeFam; TF325513; -.
DR BioGRID-ORCS; 57330; 8 hits in 72 CRISPR screens.
DR ChiTaRS; Gigyf1; mouse.
DR PRO; PR:Q99MR1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q99MR1; protein.
DR Bgee; ENSMUSG00000029714; Expressed in olfactory tubercle and 246 other tissues.
DR ExpressionAtlas; Q99MR1; baseline and differential.
DR Genevisible; Q99MR1; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IPI:MGI.
DR CDD; cd00072; GYF; 1.
DR Gene3D; 3.30.1490.40; -; 1.
DR InterPro; IPR003169; GYF.
DR InterPro; IPR035445; GYF-like_dom_sf.
DR Pfam; PF02213; GYF; 1.
DR SMART; SM00444; GYF; 1.
DR SUPFAM; SSF55277; SSF55277; 1.
DR PROSITE; PS50829; GYF; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1044
FT /note="GRB10-interacting GYF protein 1"
FT /id="PRO_0000058315"
FT DOMAIN 476..524
FT /note="GYF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00101"
FT REGION 104..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..347
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75420"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75420"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75420"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75420"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75420"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75420"
FT MUTAGEN 500
FT /note="W->A: Decreases binding to GRB10."
FT /evidence="ECO:0000269|PubMed:12771153"
FT MUTAGEN 504
FT /note="G->A: Decreases binding to GRB10."
FT /evidence="ECO:0000269|PubMed:12771153"
FT MUTAGEN 505
FT /note="Y->A: Decreases binding to GRB10."
FT /evidence="ECO:0000269|PubMed:12771153"
FT MUTAGEN 506
FT /note="F->A: Abolishes binding to GRB10."
FT /evidence="ECO:0000269|PubMed:12771153"
FT CONFLICT 58
FT /note="Missing (in Ref. 2; AAO46886)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="R -> K (in Ref. 2; AAO46886)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="S -> A (in Ref. 2; AAO46886)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="G -> A (in Ref. 2; AAO46886)"
FT /evidence="ECO:0000305"
FT CONFLICT 895
FT /note="G -> S (in Ref. 1; AAK28827)"
FT /evidence="ECO:0000305"
FT CONFLICT 973..975
FT /note="Missing (in Ref. 1; AAK28827)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1044 AA; 116238 MW; 3EE2247C7C760065 CRC64;
MAAETLNFGP EWLRALSSGG SVASPPPSPA MPKYKLADYR YGREEMLALY VKENKVPEEL
QDKEFAAVLQ EEPLQPLALE PLTEEEQRNF SLSVNSVAVL RLMGKGAGPP LPATSRGRGS
TRSRGRGRGD SCFYQRSIEE GDGAFGRNPR EIQRSQSWDD RGERRFEKPA RRDGVRSGFE
EGGAGPRKEH ARSDSENWRS LREEQEDDGS WRLGAGPRRD GDRWRSTSPD GGPRSAGWRE
HGERRRKFDF DLRGERGGCG EEDGRVGGGN SHLRRCRGLD GFEDDKDGLP EWCLEDEDEE
MGTFDASGAF LPLKKGPKEA IPEEQELDFR GLEEEEEEEE EPSEGVDEER PEAGGKEATP
LPPPENSSSP SSLPALGPLW TTNEEGGEAV EKELPPAEGD ELRGLSLSPR ISSPPGPPGD
LEDEEGLKHL QQEAEKLVAS LQDSSLEEEQ FTAAMQTQGL RHSTAATALP LSHGAARKWF
YKDPQGEIQG PFTTQEMAEW FQAGYFSMSL LVKRGCDEGF QPLGEVIKMW GRVPFAPGPS
PPPLLGNMDQ ERLKKQQELA AAALYQQLQH QHFLQLVGSR QLPQCTTLRE KAAMGDLTPP
QQQQLTTFLQ QLQALKTPRG GDQNLLPTMS RSLSVPDSGP LWDLHTSASS QSGGEASLWD
IPINSSTQGP ILEQLQLQHK FQERREVELR AKREEEERKR REEKRRQQQQ QQEEQKRRQE
EEELFRRKQV RQQELLLKLL QQQQATNVPV PPAPSSPPPL WAGLAKQGLS MKTLLELQME
SERQLHKQAA PREPLRAQAP NHRVQLGGLG SAPLNQWVSE AGPLWGGPDK SGGSSGGNLG
LWEDTLKSGG SLARSLGLKS SRSSPSLSDS YSHLSGRPVR KKTEEEEKLL KLLQGIPRPQ
DGFTQWCEQM LHTLSTAGSL DVPMAVAILK EVESPYDVHD YIRSCLGDTL EAKEFAKQFL
ERRAKQKASQ QRQQQQQQQQ QQQQEAWLSS TSLQTAFQAN HSTKLGPGEG SKAKRRALML
HSDPSILGYS LHGPSGEIES VDDY
