CYFP2_MOUSE
ID CYFP2_MOUSE Reviewed; 1253 AA.
AC Q5SQX6; Q3UH21; Q3UHS8; Q8BSW0; Q8CHA9; Q924D3; Q9R181;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cytoplasmic FMR1-interacting protein 2;
DE AltName: Full=p53-inducible protein 121;
GN Name=Cyfip2 {ECO:0000312|MGI:MGI:1924134};
GN Synonyms=Kiaa1168 {ECO:0000312|EMBL:BAC41472.2},
GN Pir121 {ECO:0000312|EMBL:AAD45803.1};
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:AAK81821.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH FMR1; FXR1 AND FXR2,
RP 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 [2] {ECO:0000312|EMBL:BAC41472.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:BAC41472.2};
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [3] {ECO:0000312|EMBL:BAE28010.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE28010.1};
RC TISSUE=Brain {ECO:0000312|EMBL:BAE28010.1},
RC Kidney {ECO:0000312|EMBL:BAE27779.1}, and
RC Pituitary {ECO:0000312|EMBL:BAC26942.1};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAD45803.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-367.
RX PubMed=10449408; DOI=10.1093/emboj/18.16.4424;
RA Saller E., Tom E., Brunori M., Otter M., Estreicher A., Mack D.H., Iggo R.;
RT "Increased apoptosis induction by 121F mutant p53.";
RL EMBO J. 18:4424-4437(1999).
RN [6] {ECO:0000305}
RP RNA EDITING OF POSITION 320.
RX PubMed=15731336; DOI=10.1093/nar/gki239;
RA Levanon E.Y., Hallegger M., Kinar Y., Shemesh R., Djinovic-Carugo K.,
RA Rechavi G., Jantsch M.F., Eisenberg E.;
RT "Evolutionarily conserved human targets of adenosine to inosine RNA
RT editing.";
RL Nucleic Acids Res. 33:1162-1168(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, and Spleen;
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 [8]
RP INTERACTION WITH SHANK3, AND TISSUE SPECIFICITY.
RX PubMed=24153177; DOI=10.1038/nature12630;
RA Han K., Holder J.L. Jr., Schaaf C.P., Lu H., Chen H., Kang H., Tang J.,
RA Wu Z., Hao S., Cheung S.W., Yu P., Sun H., Breman A.M., Patel A., Lu H.C.,
RA Zoghbi H.Y.;
RT "SHANK3 overexpression causes manic-like behaviour with unique
RT pharmacogenetic properties.";
RL Nature 503:72-77(2013).
RN [9]
RP FUNCTION, AND 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: Part of the WAVE1 complex that regulates actin filament
CC reorganization via its interaction with the Arp2/3 complex (By
CC similarity). Involved in T-cell adhesion and p53-dependent induction of
CC apoptosis (By similarity). Does not bind RNA. As component of the WAVE1
CC complex, required for BDNF-NTRK2 endocytic trafficking and signaling
CC from early endosomes (PubMed:27605705). {ECO:0000250|UniProtKB:Q96F07,
CC ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:27605705}.
CC -!- SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP1 or
CC CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Interacts with FMR1, FXR1 and
CC FXR2 (PubMed:11438699). Interacts with FMR1; the interaction occurs in
CC a RNA-dependent manner (By similarity). Interacts with RAC1 (activated
CC form) which causes the complex to dissociate, releasing activated WASF1
CC (By similarity). The complex can also be activated by NCK1 (By
CC similarity). Interacts with SHANK3; the interaction mediates the
CC association of SHANK3 with the WAVE1 complex (PubMed:24153177).
CC Interacts with TMEM108 (via N-terminus); the interaction associates
CC TMEM108 with the WAVE1 complex (PubMed:27605705).
CC {ECO:0000250|UniProtKB:Q96F07, ECO:0000269|PubMed:11438699,
CC ECO:0000269|PubMed:24153177, ECO:0000269|PubMed:27605705}.
CC -!- INTERACTION:
CC Q5SQX6; Q4ACU6: Shank3; NbExp=3; IntAct=EBI-773783, EBI-771450;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11438699}. Nucleus
CC {ECO:0000250|UniProtKB:Q96F07}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:11438699}. Synapse, synaptosome
CC {ECO:0000269|PubMed:11438699}. Note=Highly expressed in the perinuclear
CC region and enriched in synaptosomes (PubMed:11438699).
CC {ECO:0000269|PubMed:11438699}.
CC -!- TISSUE SPECIFICITY: Expressed in hippocampus (at protein level).
CC {ECO:0000269|PubMed:24153177}.
CC -!- RNA EDITING: Modified_positions=320 {ECO:0000269|PubMed:15731336};
CC Note=Partially edited. Editing appears to be brain-specific.
CC {ECO:0000269|PubMed:15731336};
CC -!- SIMILARITY: Belongs to the CYFIP family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41472.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF334144; AAK81821.1; -; mRNA.
DR EMBL; AB093288; BAC41472.2; ALT_INIT; mRNA.
DR EMBL; AK030397; BAC26942.1; -; mRNA.
DR EMBL; AK147224; BAE27779.1; -; mRNA.
DR EMBL; AK147586; BAE28010.1; -; mRNA.
DR EMBL; AK147632; BAE28036.1; -; mRNA.
DR EMBL; AL662806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL713958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF162472; AAD45803.1; -; mRNA.
DR CCDS; CCDS24573.1; -.
DR RefSeq; NP_001239388.1; NM_001252459.1.
DR RefSeq; NP_001239389.1; NM_001252460.1.
DR RefSeq; NP_598530.2; NM_133769.3.
DR AlphaFoldDB; Q5SQX6; -.
DR SMR; Q5SQX6; -.
DR BioGRID; 218375; 56.
DR DIP; DIP-32111N; -.
DR IntAct; Q5SQX6; 62.
DR STRING; 10090.ENSMUSP00000090854; -.
DR GlyConnect; 2249; 1 N-Linked glycan (1 site).
DR GlyGen; Q5SQX6; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q5SQX6; -.
DR PhosphoSitePlus; Q5SQX6; -.
DR SwissPalm; Q5SQX6; -.
DR EPD; Q5SQX6; -.
DR jPOST; Q5SQX6; -.
DR MaxQB; Q5SQX6; -.
DR PaxDb; Q5SQX6; -.
DR PeptideAtlas; Q5SQX6; -.
DR PRIDE; Q5SQX6; -.
DR ProteomicsDB; 285439; -.
DR Antibodypedia; 28408; 150 antibodies from 27 providers.
DR DNASU; 76884; -.
DR Ensembl; ENSMUST00000093165; ENSMUSP00000090853; ENSMUSG00000020340.
DR Ensembl; ENSMUST00000093166; ENSMUSP00000090854; ENSMUSG00000020340.
DR Ensembl; ENSMUST00000165599; ENSMUSP00000127586; ENSMUSG00000020340.
DR GeneID; 76884; -.
DR KEGG; mmu:76884; -.
DR UCSC; uc007iob.2; mouse.
DR CTD; 26999; -.
DR MGI; MGI:1924134; Cyfip2.
DR VEuPathDB; HostDB:ENSMUSG00000020340; -.
DR eggNOG; KOG3534; Eukaryota.
DR GeneTree; ENSGT00500000044831; -.
DR HOGENOM; CLU_002688_2_1_1; -.
DR InParanoid; Q5SQX6; -.
DR OMA; MPKVCKL; -.
DR OrthoDB; 108507at2759; -.
DR PhylomeDB; Q5SQX6; -.
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-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 76884; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Cyfip2; mouse.
DR PRO; PR:Q5SQX6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SQX6; protein.
DR Bgee; ENSMUSG00000020340; Expressed in retrosplenial region and 251 other tissues.
DR ExpressionAtlas; Q5SQX6; baseline and differential.
DR Genevisible; Q5SQX6; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0031209; C:SCAR complex; IDA:ARUK-UCL.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0097484; P:dendrite extension; IMP:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0051388; P:positive regulation of neurotrophin TRK receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
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 Acetylation; Apoptosis; Cell adhesion; Cytoplasm; Nucleus;
KW Reference proteome; RNA editing; Synapse; Synaptosome.
FT CHAIN 1..1253
FT /note="Cytoplasmic FMR1-interacting protein 2"
FT /id="PRO_0000279710"
FT MOD_RES 1037
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96F07"
FT VARIANT 320
FT /note="K -> E (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:15731336"
FT CONFLICT 76
FT /note="G -> V (in Ref. 3; BAC26942)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="E -> G (in Ref. 3; BAE27779)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="V -> A (in Ref. 3; BAE27779)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="L -> P (in Ref. 3; BAC26942)"
FT /evidence="ECO:0000305"
FT CONFLICT 1080
FT /note="L -> P (in Ref. 3; BAC26942)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1253 AA; 145659 MW; 321011BF830F424E CRC64;
MTTHVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSIMYQA NFDTNFEDRN AFVTGIARYI
EQATVHSSMN EMLEEGHDYA VMLYTWRSCS RAIPQVKCNE QPNRVEIYEK TVEVLEPEVT
KLMKFMYFQR KAIERFCSEV KRLCHAERRK DFVSEAYLLT LGKFINMFAV LDELKNMKCS
VKNDHSAYKR AAQFLRKMAD PQSIQESQNL SMFLANHNRI TQCLHQQLEV IPGYEELLAD
IVNICVDYYE NKMYLTPSEK HMLLKVMGFG LYLMDGNVSN IYKLDAKKRI NLSKIDKFFK
QLQVVPLFGD MQIELARYIK TSAHYEENKS KWTCTQSSIS PQYNICEQMV QIRDDHIRFI
SELARYSNSE VVTGSGLDSQ KSDEEYRELF DLALRGLQLL SKWSAHVMEV YSWKLVHPTD
KFCNKDCPGT AEEYERATRY NYTSEEKFAF VEVIAMIKGL QVLMGRMESV FNQAIRNTIY
AALQDFAQVT LREPLRQAVR KKKNVLISVL QAIRKTICDW EGGREPPNDP CLRGEKDPKG
GFDIKVPRRA VGPSSTQLYM VRTMLESLIA DKSGSKKTLR SSLDGPIVLA IEDFHKQSFF
FTHLLNISEA LQQCCDLSQL WFREFFLELT MGRRIQFPIE MSMPWILTDH ILETKEPSMM
EYVLYPLDLY NDSAYYALTK FKKQFLYDEI EAEVNLCFDQ FVYKLADQIF AYYKAMAGSV
LLDKRFRAEC KNYGVIIPYP PSNRYETLLK QRHVQLLGRS IDLNRLITQR ISAAMYKSLD
QAISRFESED LTSIVELEWL LEINRLTHRL LCKHMTLDSF DAMFREANHN VSAPYGRITL
HVFWELNFDF LPNYCYNGST NRFVRTAIPF TQEPQRDKPA NVQPYYLYGS KPLNIAYSHI
YSSYRNFVGP PHFKTICRLL GYQGIAVVME ELLKIVKSLL QGTILQYVKT LIEVMPKICR
LPRHEYGSPG ILEFFHHQLK DIIEYAELKT DVFQSLREVG NAILFCLLIE QALSQEEVCD
LLHAAPFQNI LPRVYIKEGE RLEVRMKRLE AKYAPLHLVP LIERLGTPQQ IAIAREGDLL
TKERLCCGLS MFEVILTRIR SYLQDPIWRG PPPTNGVMHV DECVEFHRLW SAMQFVYCIP
VGTNEFTAEQ CFGDGLNWAG CSIIVLLGQQ RRFDLFDFCY HLLKVQRQDG KDEIIKNVPL
KKMADRIRKY QILNNEVFAI LNKYMKSVET DSSTVEHVRC FQPPIHQSLA TTC
