##gff-version 3 Q3V6T2 UniProtKB Chain 1 1871 . . . ID=PRO_0000287429;Note=Girdin Q3V6T2 UniProtKB Domain 12 132 . . . Note=Calponin-homology (CH);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00044 Q3V6T2 UniProtKB Region 816 842 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q3V6T2 UniProtKB Region 1010 1035 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q3V6T2 UniProtKB Region 1390 1408 . . . Note=Phosphoinositide-binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16139227;Dbxref=PMID:16139227 Q3V6T2 UniProtKB Region 1407 1459 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q3V6T2 UniProtKB Region 1559 1601 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q3V6T2 UniProtKB Region 1713 1823 . . . Note=SH2-like%3B required for interaction with growth factor receptors;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25187647;Dbxref=PMID:25187647 Q3V6T2 UniProtKB Region 1736 1871 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q3V6T2 UniProtKB Coiled coil 196 425 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q3V6T2 UniProtKB Coiled coil 458 1385 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q3V6T2 UniProtKB Motif 1672 1702 . . . Note=GBA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30194280;Dbxref=PMID:30194280 Q3V6T2 UniProtKB Compositional bias 1416 1459 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q3V6T2 UniProtKB Compositional bias 1743 1759 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q3V6T2 UniProtKB Compositional bias 1767 1819 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q3V6T2 UniProtKB Compositional bias 1839 1856 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q3V6T2 UniProtKB Compositional bias 1857 1871 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q3V6T2 UniProtKB Modified residue 233 233 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q3V6T2 UniProtKB Modified residue 237 237 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SNZ0 Q3V6T2 UniProtKB Modified residue 449 449 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q3V6T2 UniProtKB Modified residue 1020 1020 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q3V6T2 UniProtKB Modified residue 1387 1387 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 Q3V6T2 UniProtKB Modified residue 1417 1417 . . . Note=Phosphoserine%3B by PKB/AKT1;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:16139227,ECO:0007744|PubMed:23186163;Dbxref=PMID:16139227,PMID:23186163 Q3V6T2 UniProtKB Modified residue 1421 1421 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q3V6T2 UniProtKB Modified residue 1673 1673 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q3V6T2 UniProtKB Modified residue 1675 1675 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27621449;Dbxref=PMID:27621449 Q3V6T2 UniProtKB Modified residue 1690 1690 . . . Note=Phosphoserine%3B by PKC/PRKCQ;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23509302,ECO:0000269|PubMed:27621449;Dbxref=PMID:23509302,PMID:27621449 Q3V6T2 UniProtKB Modified residue 1717 1717 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q3V6T2 UniProtKB Modified residue 1765 1765 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21954290;Dbxref=PMID:21954290 Q3V6T2 UniProtKB Modified residue 1799 1799 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21954290;Dbxref=PMID:21954290 Q3V6T2 UniProtKB Modified residue 1820 1820 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q3V6T2 UniProtKB Modified residue 1837 1837 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q3V6T2 UniProtKB Alternative sequence 952 952 . . . ID=VSP_040129;Note=In isoform 3%2C isoform 4 and isoform 5. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:16139227,ECO:0000303|PubMed:17974005;Dbxref=PMID:15489334,PMID:16139227,PMID:17974005 Q3V6T2 UniProtKB Alternative sequence 1463 1491 . . . ID=VSP_052409;Note=In isoform 2 and isoform 4. MVALKRLPFLRNRPKDKDKMKACYRRSMS->T;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:15882442,ECO:0000303|PubMed:17974005,ECO:0000303|Ref.3;Dbxref=PMID:15489334,PMID:15882442,PMID:17974005 Q3V6T2 UniProtKB Alternative sequence 1733 1806 . . . ID=VSP_044943;Note=In isoform 5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q3V6T2 UniProtKB Mutagenesis 1417 1417 . . . Note=Phosphorylation-deficient mutant which disrupts actin organization%2C cell migration and lamellipodia formation but has no effect on tyrosine phosphorylation. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16139227,ECO:0000269|PubMed:21954290;Dbxref=PMID:16139227,PMID:21954290 Q3V6T2 UniProtKB Mutagenesis 1417 1417 . . . Note=Phosphomimetic mutant which has no effect on tyrosine phosphorylation. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21954290;Dbxref=PMID:21954290 Q3V6T2 UniProtKB Mutagenesis 1675 1675 . . . Note=Phosphorylation-deficient mutant which disrupts binding to GNAI3 and GNAS. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27621449;Dbxref=PMID:27621449 Q3V6T2 UniProtKB Mutagenesis 1675 1675 . . . Note=Phosphomimetic mutant which results in slight increase in binding to GNAI3 and GNAS. Increased inhibition of GNAS%3B when associated with D-1690. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27621449;Dbxref=PMID:27621449 Q3V6T2 UniProtKB Mutagenesis 1684 1684 . . . Note=No effect on guanine nucleotide exchange factor activity. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31363053;Dbxref=PMID:31363053 Q3V6T2 UniProtKB Mutagenesis 1686 1686 . . . Note=Abolishes interaction with and activation of GNAI3 and also abolishes recruitment of GNAI3 to EGFR. Reduced EGFR autophosphorylation and SH2 adapter recruitment%2C reduced localization of EGFR at the cell membrane following ligand stimulation with increased endosomal localization%2C reduced cell migration and increased cell proliferation. Abolishes enhancement of AKT signaling. Abolishes interaction with GNAS. F->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19211784,ECO:0000269|PubMed:20462955,ECO:0000269|PubMed:23509302,ECO:0000269|PubMed:27621449;Dbxref=PMID:19211784,PMID:20462955,PMID:23509302,PMID:27621449 Q3V6T2 UniProtKB Mutagenesis 1689 1689 . . . Note=Abolishes interaction with GNAI3. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19211784;Dbxref=PMID:19211784 Q3V6T2 UniProtKB Mutagenesis 1690 1690 . . . Note=Phosphorylation-deficient mutant which retains the ability to bind GNAI3. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23509302;Dbxref=PMID:23509302 Q3V6T2 UniProtKB Mutagenesis 1690 1690 . . . Note=Phosphomimetic mutant which abolishes interaction with GNAI3%2C inhibits guanine nucleotide exchange factor activity%2C inhibits cell migration and triggers cell proliferation. Retains ability to bind to GNAS. Increased inhibition of GNAS%3B when associated with D-1675. S->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23509302,ECO:0000269|PubMed:27621449;Dbxref=PMID:23509302,PMID:27621449 Q3V6T2 UniProtKB Mutagenesis 1723 1723 . . . Note=Abolishes binding to phosphorylated EGFR. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25187647;Dbxref=PMID:25187647 Q3V6T2 UniProtKB Mutagenesis 1725 1725 . . . Note=Does not affect binding to phosphorylated EGFR. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25187647;Dbxref=PMID:25187647 Q3V6T2 UniProtKB Mutagenesis 1746 1746 . . . Note=Abolishes binding to phosphorylated EGFR. R->K%2CL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25187647;Dbxref=PMID:25187647 Q3V6T2 UniProtKB Mutagenesis 1750 1750 . . . Note=Abolishes binding to phosphorylated EGFR. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25187647;Dbxref=PMID:25187647 Q3V6T2 UniProtKB Mutagenesis 1765 1765 . . . Note=Abolishes phosphorylation and leads to reduced AKT phosphorylation%2C impaired formation of actin stress fibers and impaired cell migration abolishes interaction with PIK3R1 and activation of PI3K%2C reduces phosphorylation of Ser-1417 but does not affect interaction with or activation of GNAI3%3B when associated with F-1799. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21954290;Dbxref=PMID:21954290 Q3V6T2 UniProtKB Mutagenesis 1766 1766 . . . Note=Increases binding to phosphorylated EGFR. F->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25187647;Dbxref=PMID:25187647 Q3V6T2 UniProtKB Mutagenesis 1778 1778 . . . Note=Abolishes binding to phosphorylated EGFR. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25187647;Dbxref=PMID:25187647 Q3V6T2 UniProtKB Mutagenesis 1799 1799 . . . Note=Abolishes phosphorylation and leads to reduced AKT phosphorylation%2C impaired formation of actin stress fibers and impaired cell migration%2C abolishes interaction with PIK3R1 and activation of PI3K activity%2C reduces phosphorylation of Ser-1417 but does not affect interaction with or activation of GNAI3%3B when associated with F-1765. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21954290;Dbxref=PMID:21954290 Q3V6T2 UniProtKB Sequence conflict 1066 1066 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q3V6T2 UniProtKB Sequence conflict 1081 1081 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q3V6T2 UniProtKB Sequence conflict 1661 1661 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q3V6T2 UniProtKB Sequence conflict 1710 1710 . . . Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q3V6T2 UniProtKB Sequence conflict 1799 1799 . . . Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q3V6T2 UniProtKB Sequence conflict 1836 1836 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q3V6T2 UniProtKB Beta strand 1679 1682 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6MHF Q3V6T2 UniProtKB Helix 1683 1690 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6MHF