ID   FARP1_HUMAN             Reviewed;        1045 AA.
AC   Q9Y4F1; Q5JVI9; Q6IQ29;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 188.
DE   RecName: Full=FERM, ARHGEF and pleckstrin domain-containing protein 1;
DE   AltName: Full=Chondrocyte-derived ezrin-like protein;
DE   AltName: Full=FERM, RhoGEF and pleckstrin domain-containing protein 1;
DE   AltName: Full=Pleckstrin homology domain-containing family C member 2;
DE            Short=PH domain-containing family C member 2;
GN   Name=FARP1; Synonyms=CDEP, PLEKHC2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Cartilage;
RX   PubMed=9425278; DOI=10.1006/bbrc.1997.7826;
RA   Koyano Y., Kawamoto T., Shen M., Yan W., Noshiro M., Fujii K., Kato Y.;
RT   "Molecular cloning and characterization of CDEP, a novel human protein
RT   containing the ezrin-like domain of the band 4.1 superfamily and the Dbl
RT   homology domain of rho guanine nucleotide exchange factors.";
RL   Biochem. Biophys. Res. Commun. 241:369-375(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Brain, Placenta, and Skin;
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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17924679; DOI=10.1021/pr070152u;
RA   Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT   "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT   and high confident phosphopeptide identification by cross-validation of
RT   MS/MS and MS/MS/MS spectra.";
RL   J. Proteome Res. 6:4150-4162(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24 AND SER-340, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-889, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18318008; DOI=10.1002/pmic.200700884;
RA   Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA   Zou H., Gu J.;
RT   "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT   and fractionation of phosphopeptides with strong anion exchange
RT   chromatography.";
RL   Proteomics 8:1346-1361(2008).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24; SER-427; SER-510 AND
RP   SER-514, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872 AND SER-889, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373; SER-403; SER-418;
RP   SER-427; SER-833; SER-872; THR-883 AND SER-889, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (4.09 ANGSTROMS) OF 539-1035, AND DOMAIN.
RX   PubMed=23375260; DOI=10.1016/j.str.2013.01.001;
RA   He X., Kuo Y.C., Rosche T.J., Zhang X.;
RT   "Structural basis for autoinhibition of the guanine nucleotide exchange
RT   factor FARP2.";
RL   Structure 21:355-364(2013).
RN   [16]
RP   VARIANT [LARGE SCALE ANALYSIS] LEU-714.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Functions as a guanine nucleotide exchange factor for RAC1.
CC       May play a role in semaphorin signaling. Plays a role in the assembly
CC       and disassembly of dendritic filopodia, the formation of dendritic
CC       spines, regulation of dendrite length and ultimately the formation of
CC       synapses (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CADM1. Interacts with RAC1 (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9Y4F1; Q9NWS0: PIH1D1; NbExp=3; IntAct=EBI-5235630, EBI-357318;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Synapse. Synapse, synaptosome {ECO:0000250}.
CC       Cytoplasm, cytosol {ECO:0000250}. Cell projection, filopodium
CC       {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell
CC       projection, dendritic spine {ECO:0000250}. Note=Recruited to the cell
CC       membrane via interaction with CADM1. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9Y4F1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y4F1-2; Sequence=VSP_017976;
CC       Name=3;
CC         IsoId=Q9Y4F1-3; Sequence=VSP_040989, VSP_040990;
CC   -!- TISSUE SPECIFICITY: Detected in cAMP-treated chondrocytes, but not in
CC       untreated chondrocytes. Detected in fetal brain, heart and spleen, and
CC       in adult testis, kidney and lung. {ECO:0000269|PubMed:9425278}.
CC   -!- INDUCTION: Up-regulated in response to cAMP in cultured embryonic
CC       chondrocytes. {ECO:0000269|PubMed:9425278}.
CC   -!- DOMAIN: Intramolecular interaction between the DH domain and the PH
CC       domains can stabilize the protein in an autoinhibited conformation.
CC       {ECO:0000269|PubMed:23375260}.
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DR   EMBL; AB008430; BAA24267.1; -; mRNA.
DR   EMBL; AL136300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL137249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL161896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL445223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC041595; AAH41595.1; -; mRNA.
DR   EMBL; BC065020; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC071592; AAH71592.1; -; mRNA.
DR   CCDS; CCDS32000.1; -. [Q9Y4F1-3]
DR   CCDS; CCDS66572.1; -. [Q9Y4F1-2]
DR   CCDS; CCDS9487.1; -. [Q9Y4F1-1]
DR   PIR; JC5795; JC5795.
DR   RefSeq; NP_001001715.2; NM_001001715.3. [Q9Y4F1-3]
DR   RefSeq; NP_001273768.1; NM_001286839.1.
DR   RefSeq; NP_005757.1; NM_005766.3. [Q9Y4F1-1]
DR   RefSeq; XP_016875801.1; XM_017020312.1.
DR   PDB; 4H6Y; X-ray; 4.09 A; A/B=539-1035.
DR   PDBsum; 4H6Y; -.
DR   AlphaFoldDB; Q9Y4F1; -.
DR   SMR; Q9Y4F1; -.
DR   BioGRID; 115462; 148.
DR   IntAct; Q9Y4F1; 58.
DR   MINT; Q9Y4F1; -.
DR   STRING; 9606.ENSP00000486285; -.
DR   CarbonylDB; Q9Y4F1; -.
DR   iPTMnet; Q9Y4F1; -.
DR   PhosphoSitePlus; Q9Y4F1; -.
DR   BioMuta; FARP1; -.
DR   DMDM; 74762059; -.
DR   EPD; Q9Y4F1; -.
DR   jPOST; Q9Y4F1; -.
DR   MassIVE; Q9Y4F1; -.
DR   MaxQB; Q9Y4F1; -.
DR   PaxDb; 9606-ENSP00000471242; -.
DR   PeptideAtlas; Q9Y4F1; -.
DR   ProteomicsDB; 86186; -. [Q9Y4F1-1]
DR   ProteomicsDB; 86187; -. [Q9Y4F1-2]
DR   ProteomicsDB; 86188; -. [Q9Y4F1-3]
DR   Pumba; Q9Y4F1; -.
DR   Antibodypedia; 619; 255 antibodies from 20 providers.
DR   DNASU; 10160; -.
DR   Ensembl; ENST00000319562.11; ENSP00000322926.6; ENSG00000152767.17. [Q9Y4F1-1]
DR   Ensembl; ENST00000376581.9; ENSP00000365765.4; ENSG00000152767.17. [Q9Y4F1-3]
DR   GeneID; 10160; -.
DR   KEGG; hsa:10160; -.
DR   MANE-Select; ENST00000319562.11; ENSP00000322926.6; NM_005766.4; NP_005757.1.
DR   UCSC; uc001vni.5; human. [Q9Y4F1-1]
DR   AGR; HGNC:3591; -.
DR   CTD; 10160; -.
DR   DisGeNET; 10160; -.
DR   GeneCards; FARP1; -.
DR   HGNC; HGNC:3591; FARP1.
DR   HPA; ENSG00000152767; Low tissue specificity.
DR   MIM; 602654; gene.
DR   neXtProt; NX_Q9Y4F1; -.
DR   OpenTargets; ENSG00000152767; -.
DR   PharmGKB; PA28004; -.
DR   VEuPathDB; HostDB:ENSG00000152767; -.
DR   eggNOG; KOG3531; Eukaryota.
DR   GeneTree; ENSGT00940000155318; -.
DR   HOGENOM; CLU_012301_0_0_1; -.
DR   InParanoid; Q9Y4F1; -.
DR   OrthoDB; 2876516at2759; -.
DR   PhylomeDB; Q9Y4F1; -.
DR   TreeFam; TF351276; -.
DR   PathwayCommons; Q9Y4F1; -.
DR   Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR   Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR   Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR   Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR   SignaLink; Q9Y4F1; -.
DR   BioGRID-ORCS; 10160; 15 hits in 1145 CRISPR screens.
DR   ChiTaRS; FARP1; human.
DR   GeneWiki; FARP1; -.
DR   GenomeRNAi; 10160; -.
DR   Pharos; Q9Y4F1; Tbio.
DR   PRO; PR:Q9Y4F1; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; Q9Y4F1; Protein.
DR   Bgee; ENSG00000152767; Expressed in renal medulla and 204 other cell types or tissues.
DR   ExpressionAtlas; Q9Y4F1; baseline and differential.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0098890; C:extrinsic component of postsynaptic membrane; IEA:Ensembl.
DR   GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR   GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
DR   GO; GO:0007167; P:enzyme-linked receptor protein signaling pathway; IEA:Ensembl.
DR   GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; IEA:Ensembl.
DR   GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0016601; P:Rac protein signal transduction; IEA:Ensembl.
DR   GO; GO:1905606; P:regulation of presynapse assembly; IEA:Ensembl.
DR   GO; GO:0098942; P:retrograde trans-synaptic signaling by trans-synaptic protein complex; IEA:Ensembl.
DR   GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13193; FERM_C_FARP1-like; 1.
DR   CDD; cd01220; PH1_FARP1-like; 1.
DR   CDD; cd13235; PH2_FARP1-like; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   DisProt; DP02833; -.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 3.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR000798; Ez/rad/moesin-like.
DR   InterPro; IPR014847; FA.
DR   InterPro; IPR041788; FARP1/FARP2/FRMD7_FERM_C.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR45858; FERM DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45858:SF2; FERM, ARHGEF AND PLECKSTRIN DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01195; FA; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 3.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   Genevisible; Q9Y4F1; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW   Cytoplasm; Developmental protein; Guanine-nucleotide releasing factor;
KW   Membrane; Phosphoprotein; Reference proteome; Repeat; Synapse; Synaptosome.
FT   CHAIN           1..1045
FT                   /note="FERM, ARHGEF and pleckstrin domain-containing
FT                   protein 1"
FT                   /id="PRO_0000232753"
FT   DOMAIN          40..320
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   DOMAIN          540..730
FT                   /note="DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT   DOMAIN          759..856
FT                   /note="PH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          932..1029
FT                   /note="PH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          864..903
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..515
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT   MOD_RES         24
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         340
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         373
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         389
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT   MOD_RES         403
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         418
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         427
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17924679,
FT                   ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         433
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT   MOD_RES         510
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         514
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         833
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         872
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         878
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT   MOD_RES         883
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         889
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18318008,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT   MOD_RES         896
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT   MOD_RES         899
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT   VAR_SEQ         58..129
FT                   /note="QRAPGKVLLDAVCNHLNLVEGDYFGLEFPDHKKITVWLDLLKPIVKQIRRPK
FT                   HVVVKFVVKFFPPDHTQLQE -> MVSSSSFLKATGSSWTGWVLRCSMKPKHHSHLIEK
FT                   FGEDRILTHLTGSISYTNWAGSRSLAVTVTEELLNLF (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_040989"
FT   VAR_SEQ         130..1045
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_040990"
FT   VAR_SEQ         758
FT                   /note="R -> RPGSFSLMRTPHLGQARRIPCAPERRPLLLVK (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_017976"
FT   VARIANT         8
FT                   /note="P -> L (in dbSNP:rs9300466)"
FT                   /id="VAR_048362"
FT   VARIANT         714
FT                   /note="R -> L (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs1458028855)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035851"
FT   CONFLICT        644
FT                   /note="H -> Y (in Ref. 3; AAH71592)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1045 AA;  118633 MW;  0E8B2D61C0F58417 CRC64;
     MGEIEQRPTP GSRLGAPENS GISTLERGQK PPPTPSGKLV SIKIQMLDDT QEAFEVPQRA
     PGKVLLDAVC NHLNLVEGDY FGLEFPDHKK ITVWLDLLKP IVKQIRRPKH VVVKFVVKFF
     PPDHTQLQEE LTRYLFALQV KQDLAQGRLT CNDTSAALLI SHIVQSEIGD FDEALDREHL
     AKNKYIPQQD ALEDKIVEFH HNHIGQTPAE SDFQLLEIAR RLEMYGIRLH PAKDREGTKI
     NLAVANTGIL VFQGFTKINA FNWAKVRKLS FKRKRFLIKL RPDANSAYQD TLEFLMASRD
     FCKSFWKICV EHHAFFRLFE EPKPKPKPVL FSRGSSFRFS GRTQKQVLDY VKEGGHKKVQ
     FERKHSKIHS IRSLASQPTE LNSEVLEQSQ QSTSLTFGEG AESPGGQSCR RGKEPKVSAG
     EPGSHPSPAP RRSPAGNKQA DGAASAPTEE EEEVVKDRTQ QSKPQPPQPS TGSLTGSPHL
     SELSVNSQGG VAPANVTLSP NLSPDTKQAS PLISPLLNDQ ACPRTDDEDE GRRKRFPTDK
     AYFIAKEVST TERTYLKDLE VITSWFQSTV SKEDAMPEAL KSLIFPNFEP LHKFHTNFLK
     EIEQRLALWE GRSNAQIRDY QRIGDVMLKN IQGMKHLAAH LWKHSEALEA LENGIKSSRR
     LENFCRDFEL QKVCYLPLNT FLLRPLHRLM HYKQVLERLC KHHPPSHADF RDCRAALAEI
     TEMVAQLHGT MIKMENFQKL HELKKDLIGI DNLVVPGREF IRLGSLSKLS GKGLQQRMFF
     LFNDVLLYTS RGLTASNQFK VHGQLPLYGM TIEESEDEWG VPHCLTLRGQ RQSIIVAASS
     RSEMEKWVED IQMAIDLAEK SSSPAPEFLA SSPPDNKSPD EATAADQESE DDLSASRTSL
     ERQAPHRGNT MVHVCWHRNT SVSMVDFSIA VENQLSGNLL RKFKNSNGWQ KLWVVFTNFC
     LFFYKSHQDN HPLASLPLLG YSLTIPSESE NIQKDYVFKL HFKSHVYYFR AESEYTFERW
     MEVIRSATSS ASRPHVLSHK ESLVY
//