CYFP1_MOUSE
ID CYFP1_MOUSE Reviewed; 1253 AA.
AC Q7TMB8; O88558; Q3U7Q7; Q5DU50; Q7TSZ5; Q80VN6; Q8CE85; Q99LY1;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cytoplasmic FMR1-interacting protein 1;
DE AltName: Full=Specifically Rac1-associated protein 1;
DE Short=Sra-1;
GN Name=Cyfip1 {ECO:0000312|EMBL:AAH54429.1, ECO:0000312|MGI:MGI:1338801};
GN Synonyms=Kiaa0068 {ECO:0000312|EMBL:BAD90235.1},
GN Shyc {ECO:0000312|EMBL:AAC25773.1}, Sra1 {ECO:0000312|EMBL:CAD99196.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAC25773.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAC25773.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAC25773.1};
RX PubMed=9756361; DOI=10.1016/s0304-3940(98)00531-x;
RA Koester F., Schinke B., Niemann S., Hermans-Borgmeyer I.;
RT "Identification of shyc, a novel gene expressed in the murine developing
RT and adult nervous system.";
RL Neurosci. Lett. 252:69-71(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAD99196.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, COMPONENT OF WAVE2
RP COMPLEX, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:CAD99196.1};
RC TISSUE=Brain {ECO:0000312|EMBL:CAD99196.1};
RX PubMed=14765121; DOI=10.1038/sj.emboj.7600084;
RA Steffen A., Rottner K., Ehinger J., Innocenti M., Scita G., Wehland J.,
RA Stradal T.E.B.;
RT "Sra-1 and Nap1 link Rac to actin assembly driving lamellipodia
RT formation.";
RL EMBO J. 23:749-759(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAE34191.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE34191.1};
RC TISSUE=Amnion {ECO:0000312|EMBL:BAE27303.1}, Bone marrow macrophage,
RC Embryo {ECO:0000312|EMBL:BAE34191.1}, and
RC Skin {ECO:0000312|EMBL:BAC26130.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAD90235.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain {ECO:0000312|EMBL:BAD90235.1};
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 [5] {ECO:0000305, ECO:0000312|EMBL:AAH54429.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH52713.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH54429.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH52713.1},
RC Mammary gland {ECO:0000312|EMBL:AAH54429.1}, and Olfactory epithelium;
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 [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH FMR1, AND SUBCELLULAR LOCATION.
RX PubMed=11438699; DOI=10.1073/pnas.151231598;
RA Schenck A., Bardoni B., Moro A., Bagni C., Mandel J.-L.;
RT "A highly conserved protein family interacting with the fragile X mental
RT retardation protein (FMRP) and displaying selective interactions with FMRP-
RT related proteins FXR1P and FXR2P.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8844-8849(2001).
RN [7]
RP FUNCTION, INTERACTION WITH EIF4E AND FMR1, AND MUTAGENESIS OF ASP-724;
RP LYS-725; ARG-726 AND GLU-730.
RX PubMed=18805096; DOI=10.1016/j.cell.2008.07.031;
RA Napoli I., Mercaldo V., Boyl P.P., Eleuteri B., Zalfa F., De Rubeis S.,
RA Di Marino D., Mohr E., Massimi M., Falconi M., Witke W., Costa-Mattioli M.,
RA Sonenberg N., Achsel T., Bagni C.;
RT "The fragile X syndrome protein represses activity-dependent translation
RT through CYFIP1, a new 4E-BP.";
RL Cell 134:1042-1054(2008).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19524508; DOI=10.1016/j.cell.2009.04.013;
RA Silva J.M., Ezhkova E., Silva J., Heart S., Castillo M., Campos Y.,
RA Castro V., Bonilla F., Cordon-Cardo C., Muthuswamy S.K., Powers S.,
RA Fuchs E., Hannon G.J.;
RT "Cyfip1 is a putative invasion suppressor in epithelial cancers.";
RL Cell 137:1047-1061(2009).
RN [9]
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 [10]
RP INTERACTION WITH NYAP1; NYAP2 AND MYO16.
RX PubMed=21946561; DOI=10.1038/emboj.2011.348;
RA Yokoyama K., Tezuka T., Kotani M., Nakazawa T., Hoshina N., Shimoda Y.,
RA Kakuta S., Sudo K., Watanabe K., Iwakura Y., Yamamoto T.;
RT "NYAP: a phosphoprotein family that links PI3K to WAVE1 signalling in
RT neurons.";
RL EMBO J. 30:4739-4754(2011).
RN [11]
RP INTERACTION WITH TMEM108.
RX PubMed=27605705; DOI=10.1091/mbc.e16-05-0326;
RA Xu C., Fu X., Zhu S., Liu J.J.;
RT "Retrolinkin recruits the WAVE1 protein complex to facilitate BDNF-induced
RT TrkB endocytosis and dendrite outgrowth.";
RL Mol. Biol. Cell 27:3342-3356(2016).
CC -!- FUNCTION: Component of the CYFIP1-EIF4E-FMR1 complex which binds to the
CC mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-
CC FMR1 complex this subunit is an adapter between EIF4E and FMR1.
CC Promotes the translation repression activity of FMR1 in brain probably
CC by mediating its association with EIF4E and mRNA (By similarity).
CC Regulates formation of membrane ruffles and lamellipodia. Plays a role
CC in axon outgrowth. Binds to F-actin but not to RNA. Part of the WAVE
CC complex that regulates actin filament reorganization via its
CC interaction with the Arp2/3 complex. Actin remodeling activity is
CC regulated by RAC1. Regulator of epithelial morphogenesis. May act as an
CC invasion suppressor in cancers. As component of the WAVE1 complex,
CC required for BDNF-NTRK2 endocytic trafficking and signaling from early
CC endosomes (PubMed:27605705). {ECO:0000250|UniProtKB:Q7L576,
CC ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:14765121,
CC ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:19524508,
CC ECO:0000269|PubMed:27605705}.
CC -!- SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP1 or
CC CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterodimer
CC containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by
CC WAVE1, ABI2 and BRK1. Component of the CYFIP1-EIF4E-FMR1 complex which
CC is composed of CYFIP, EIF4E and FMR1. Interacts with FMR1 but does not
CC bind to related proteins FXR1 or FXR2. Interaction with EIF4E
CC stimulates FMR1 binding. Component of the WAVE2 complex composed of
CC ABI1, CYFIP1/SRA1, NCKAP1/NAP1 (NCKAP1L/HEM1 in hematopoietic cells)
CC and WASF2/WAVE2. Interacts with the active GTP-bound form of RAC1.
CC Interacts through its C-terminus with the C-terminus of DPYSL2/CRMP2
CC which is necessary for DPYSL2-induced axon outgrowth. Interacts with
CC NYAP1, NYAP2 and MYO16. Interacts with TMEM108 (via N-terminus); the
CC interaction associates TMEM108 with the WAVE1 complex
CC (PubMed:27605705). {ECO:0000250|UniProtKB:Q7L576,
CC ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:18805096,
CC ECO:0000269|PubMed:21946561, ECO:0000269|PubMed:27605705}.
CC -!- INTERACTION:
CC Q7TMB8; P63073: Eif4e; NbExp=5; IntAct=EBI-772928, EBI-2000006;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11438699,
CC ECO:0000269|PubMed:14765121}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:11438699}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:14765121}. Cell projection, ruffle
CC {ECO:0000269|PubMed:14765121}. Synapse, synaptosome
CC {ECO:0000269|PubMed:11438699}. Note=Highly expressed in the perinuclear
CC region (PubMed:11438699). Enriched in synaptosomes (PubMed:11438699).
CC Also enriched in membrane ruffles and at the tips of lamellipodia
CC (PubMed:14765121). {ECO:0000269|PubMed:11438699,
CC ECO:0000269|PubMed:14765121}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15489334};
CC IsoId=Q7TMB8-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q7TMB8-2; Sequence=VSP_052348;
CC -!- TISSUE SPECIFICITY: Highly expressed in embryonic and adult developing
CC nervous system. {ECO:0000269|PubMed:9756361}.
CC -!- DISRUPTION PHENOTYPE: Mice display greatly reduced lamellipodium
CC formation in response to growth factor stimulation or aluminum fluoride
CC treatment. Abnormal epithelial morphogenesis in vitro, and cooperation
CC with oncogenic Ras to produce invasive carcinomas in vivo.
CC {ECO:0000269|PubMed:14765121, ECO:0000269|PubMed:19524508}.
CC -!- SIMILARITY: Belongs to the CYFIP family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90235.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF072697; AAC25773.1; -; mRNA.
DR EMBL; AJ567911; CAD99196.1; -; mRNA.
DR EMBL; AK028811; BAC26130.1; -; mRNA.
DR EMBL; AK146613; BAE27303.1; -; mRNA.
DR EMBL; AK152558; BAE31312.1; -; mRNA.
DR EMBL; AK157773; BAE34191.1; -; mRNA.
DR EMBL; AK220320; BAD90235.1; ALT_INIT; mRNA.
DR EMBL; BC002174; AAH02174.1; -; mRNA.
DR EMBL; BC047135; AAH47135.2; -; mRNA.
DR EMBL; BC052713; AAH52713.1; -; mRNA.
DR EMBL; BC054429; AAH54429.1; -; mRNA.
DR CCDS; CCDS21315.1; -. [Q7TMB8-1]
DR CCDS; CCDS52262.1; -. [Q7TMB8-2]
DR PIR; T14349; T14349.
DR RefSeq; NP_001158133.1; NM_001164661.1. [Q7TMB8-1]
DR RefSeq; NP_001158134.1; NM_001164662.1.
DR RefSeq; NP_035500.2; NM_011370.3. [Q7TMB8-1]
DR RefSeq; XP_006540792.1; XM_006540729.2. [Q7TMB8-1]
DR AlphaFoldDB; Q7TMB8; -.
DR SMR; Q7TMB8; -.
DR BioGRID; 203226; 136.
DR CORUM; Q7TMB8; -.
DR IntAct; Q7TMB8; 125.
DR MINT; Q7TMB8; -.
DR STRING; 10090.ENSMUSP00000032629; -.
DR iPTMnet; Q7TMB8; -.
DR PhosphoSitePlus; Q7TMB8; -.
DR SwissPalm; Q7TMB8; -.
DR EPD; Q7TMB8; -.
DR jPOST; Q7TMB8; -.
DR MaxQB; Q7TMB8; -.
DR PaxDb; Q7TMB8; -.
DR PeptideAtlas; Q7TMB8; -.
DR PRIDE; Q7TMB8; -.
DR ProteomicsDB; 277934; -. [Q7TMB8-1]
DR ProteomicsDB; 277935; -. [Q7TMB8-2]
DR Antibodypedia; 72407; 117 antibodies from 26 providers.
DR DNASU; 20430; -.
DR Ensembl; ENSMUST00000032629; ENSMUSP00000032629; ENSMUSG00000030447. [Q7TMB8-1]
DR Ensembl; ENSMUST00000163845; ENSMUSP00000127717; ENSMUSG00000030447. [Q7TMB8-1]
DR GeneID; 20430; -.
DR KEGG; mmu:20430; -.
DR UCSC; uc009hdk.2; mouse. [Q7TMB8-1]
DR UCSC; uc009hdn.2; mouse. [Q7TMB8-2]
DR CTD; 23191; -.
DR MGI; MGI:1338801; Cyfip1.
DR VEuPathDB; HostDB:ENSMUSG00000030447; -.
DR eggNOG; KOG3534; Eukaryota.
DR GeneTree; ENSGT00500000044831; -.
DR HOGENOM; CLU_002688_2_1_1; -.
DR InParanoid; Q7TMB8; -.
DR OMA; HKESFFY; -.
DR OrthoDB; 108507at2759; -.
DR PhylomeDB; Q7TMB8; -.
DR TreeFam; TF312925; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 20430; 15 hits in 75 CRISPR screens.
DR ChiTaRS; Cyfip1; mouse.
DR PRO; PR:Q7TMB8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q7TMB8; protein.
DR Bgee; ENSMUSG00000030447; Expressed in saccule of membranous labyrinth and 261 other tissues.
DR ExpressionAtlas; Q7TMB8; baseline and differential.
DR Genevisible; Q7TMB8; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044295; C:axonal growth cone; ISO:MGI.
DR GO; GO:0090724; C:central region of growth cone; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0044294; C:dendritic growth cone; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0060076; C:excitatory synapse; ISO:MGI.
DR GO; GO:0032433; C:filopodium tip; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0090725; C:peripheral region of growth cone; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0031209; C:SCAR complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0005522; F:profilin binding; TAS:MGI.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0045182; F:translation regulator activity; IDA:SynGO.
DR GO; GO:0048675; P:axon extension; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0097484; P:dendrite extension; IMP:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; IDA:MGI.
DR GO; GO:0099563; P:modification of synaptic structure; IMP:SynGO.
DR GO; GO:1903422; P:negative regulation of synaptic vesicle recycling; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; ISO:MGI.
DR GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI.
DR GO; GO:0050772; P:positive regulation of axonogenesis; ISO:MGI.
DR GO; GO:1900006; P:positive regulation of dendrite development; ISO:MGI.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:MGI.
DR GO; GO:0051388; P:positive regulation of neurotrophin TRK receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; ISO:MGI.
DR GO; GO:0016601; P:Rac protein signal transduction; ISO:MGI.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0031641; P:regulation of myelination; ISO:MGI.
DR GO; GO:0006417; P:regulation of translation; IMP:SynGO.
DR GO; GO:0099578; P:regulation of translation at postsynapse, modulating synaptic transmission; IDA:SynGO.
DR GO; GO:0051602; P:response to electrical stimulus; ISO:MGI.
DR GO; GO:0031529; P:ruffle organization; ISS:UniProtKB.
DR InterPro; IPR009828; CYRIA/CYRIB_Rac1-bd.
DR InterPro; IPR008081; Cytoplasmic_FMR1-int.
DR PANTHER; PTHR12195; PTHR12195; 1.
DR Pfam; PF07159; DUF1394; 1.
DR Pfam; PF05994; FragX_IP; 1.
DR PIRSF; PIRSF008153; FMR1_interacting; 1.
DR PRINTS; PR01698; CYTOFMRPINTP.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell projection; Cell shape;
KW Cytoplasm; Developmental protein; Differentiation; Neurogenesis;
KW Phosphoprotein; Reference proteome; Synapse; Synaptosome.
FT CHAIN 1..1253
FT /note="Cytoplasmic FMR1-interacting protein 1"
FT /id="PRO_0000279707"
FT REGION 724..732
FT /note="EIF4E-binding"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L576"
FT MOD_RES 1234
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7L576"
FT VAR_SEQ 570..609
FT /note="IADKSGSKKTLRSSLEGPTILDIEKFHRESFFYTHLINFS -> SSAELLRQ
FT LKSLGMERLLHVVNAFLRQSYTYPPLLTFG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052348"
FT MUTAGEN 724
FT /note="D->A: EIF4E-binding reduced by 20%; when associated
FT with A-726."
FT /evidence="ECO:0000269|PubMed:18805096"
FT MUTAGEN 724
FT /note="D->K: EIF4E-binding reduced by 60%; when associated
FT with E-725, E-726 and K-730."
FT /evidence="ECO:0000269|PubMed:18805096"
FT MUTAGEN 725
FT /note="K->E: EIF4E-binding reduced by 70%. EIF4E-binding
FT reduced by 60%; when associated with K-724, E-726 and K-
FT 730."
FT /evidence="ECO:0000269|PubMed:18805096"
FT MUTAGEN 726
FT /note="R->A: EIF4E-binding reduced by 20%; when associated
FT with A-724."
FT /evidence="ECO:0000269|PubMed:18805096"
FT MUTAGEN 726
FT /note="R->E: EIF4E-binding reduced by 60%; when associated
FT with K-724, E-725 and K-730."
FT /evidence="ECO:0000269|PubMed:18805096"
FT MUTAGEN 730
FT /note="E->K: EIF4E-binding reduced by 60%; when associated
FT with K-724, E-725 and E-726."
FT /evidence="ECO:0000269|PubMed:18805096"
FT CONFLICT 169
FT /note="A -> G (in Ref. 1; AAC25773)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="Q -> H (in Ref. 5; AAH47135)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="V -> A (in Ref. 1; AAC25773)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="M -> L (in Ref. 5; AAH52713)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="L -> A (in Ref. 5; AAH52713)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="V -> A (in Ref. 1; AAC25773)"
FT /evidence="ECO:0000305"
FT CONFLICT 1079
FT /note="D -> H (in Ref. 1; AAC25773)"
FT /evidence="ECO:0000305"
FT CONFLICT 1222
FT /note="L -> Q (in Ref. 3; BAC26130)"
FT /evidence="ECO:0000305"
FT CONFLICT 1233
FT /note="S -> T (in Ref. 1; AAC25773)"
FT /evidence="ECO:0000305"
FT CONFLICT 1238
FT /note="H -> Y (in Ref. 3; BAE27303/BAE31312)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1253 AA; 145241 MW; 793986FB417CF19B CRC64;
MAAQVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSLLYQP NFNTNFEDRN AFVTGIARYI
EQATVHSSMN EMLEEGQEYA VMLYTWRSCS RAIPQVKCNE QPNRVEIYEK TVEVLEPEVT
KLMNFMYFQR NAIERFCGEV RRLCHAERRK DFVSEAYLIT LGKFINMFAV LDELKNMKCS
VKNDHSAYKR AAQFLRKMAD PQSIQESQNL SMFLANHNKI TQSLQQQLEV ISGYEELLAD
IVNLCVDYYE NRMYLTPSEK HMLLKVMGFG LYLMDGSVSN IYKLDAKKRI NLSKIDKYFK
QLQVVPLFGD MQIELARYIK TSAHYEENKS RWTCASSSSS PQYNICEQMI QIREDHMRFI
SELARYSNSE VVTGSGRQEA QKTDAEYRKL FDLALQGLQL LSQWSAHVME VYSWKLVHPT
DKYSNKDCPD NAEEYERATR YNYTTEEKFA LVEVIAMIKG LQVLMGRMES VFNHAIRHTV
YAALQDFSQV TLREPLRQAI KKKKNVIQSV LQAIRKTVCD WETGHEPFND PALRGEKDPK
SGFDIKVPRR AVGPSSTQLY MVRTMLESLI ADKSGSKKTL RSSLEGPTIL DIEKFHRESF
FYTHLINFSE TLQQCCDLSQ LWFREFFLEL TMGRRIQFPI EMSMPWILTD HILETKEASM
MEYVLYSLDL YNDSAHYALT KFNKQFLYDE IEAEVNLCFD QFVYKLADQI FAYYKVMAGS
LLLDKRLRSE CKNQGATIHL PPSNRYETLL KQRHVQLLGR SIDLNRLITQ RVSAAMYKSL
ELAIGRFESE DLTSVVELDG LLEINRMTHK LLSRYLTLDS FDAMFREANH NVSAPYGRIT
LHVFWELNYD FLPNYCYNGS TNRFVRTVLP FSQEFQRDKQ PNAQPQYLHG SKALNLAYSS
IYGSYRNFVG PPHFQVICRL LGYQGIAVVM EELLKVVKSL LQGTILQYVK TLMEVMPKIC
RLPRHEYGSP GILEFFHHQL KDIVEYAELK TVCFQNLREV GNAVLFCLLI EQSLSLEEVC
DLLHAAPFQN ILPRIHVKEG ERVDAKMKRL ESKYAPLHLV PLIERLGTPQ QIAIAREGDL
LTKERLCCGL SMFEVILTRI RTFLDDPIWR GPLPSNGVMH VDECVEFHRL WSAMQFVYCI
PVGTHEFTVE QCFGDGLHWA GCMIIVLLGQ QRRFAVLDFC YHLLKVQKHD GKDEIIKNVP
LKKMVERIRK FQILNDEIIT ILDKYLKSGD GESTPVEHVR CFQPPIHQSL ASS
