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Cytoplasmic FMR1-interacting protein 2 (p53-inducible protein 121)

 CYFP2_MOUSE             Reviewed;        1253 AA.
Q5SQX6; Q3UH21; Q3UHS8; Q8BSW0; Q8CHA9; Q924D3; Q9R181;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 2.
23-MAY-2018, entry version 109.
RecName: Full=Cytoplasmic FMR1-interacting protein 2;
AltName: Full=p53-inducible protein 121;
Name=Cyfip2 {ECO:0000312|MGI:MGI:1924134};
Synonyms=Kiaa1168 {ECO:0000312|EMBL:BAC41472.2},
Pir121 {ECO:0000312|EMBL:AAD45803.1};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAK81821.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH FMR1; FXR1 AND
FXR2, AND SUBCELLULAR LOCATION.
PubMed=11438699; DOI=10.1073/pnas.151231598;
Schenck A., Bardoni B., Moro A., Bagni C., Mandel J.-L.;
"A highly conserved protein family interacting with the fragile X
mental retardation protein (FMRP) and displaying selective
interactions with FMRP-related proteins FXR1P and FXR2P.";
Proc. Natl. Acad. Sci. U.S.A. 98:8844-8849(2001).
[2] {ECO:0000312|EMBL:BAC41472.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain {ECO:0000312|EMBL:BAC41472.2};
PubMed=12465718; DOI=10.1093/dnares/9.5.179;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
I. The complete nucleotide sequences of 100 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 9:179-188(2002).
[3] {ECO:0000312|EMBL:BAE28010.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE28010.1};
TISSUE=Brain {ECO:0000312|EMBL:BAE28010.1},
Kidney {ECO:0000312|EMBL:BAE27779.1}, and
Pituitary {ECO:0000312|EMBL:BAC26942.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5] {ECO:0000305, ECO:0000312|EMBL:AAD45803.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 1-367.
PubMed=10449408; DOI=10.1093/emboj/18.16.4424;
Saller E., Tom E., Brunori M., Otter M., Estreicher A., Mack D.H.,
Iggo R.;
"Increased apoptosis induction by 121F mutant p53.";
EMBO J. 18:4424-4437(1999).
[6] {ECO:0000305}
RNA EDITING OF POSITION 320.
PubMed=15731336; DOI=10.1093/nar/gki239;
Levanon E.Y., Hallegger M., Kinar Y., Shemesh R., Djinovic-Carugo K.,
Rechavi G., Jantsch M.F., Eisenberg E.;
"Evolutionarily conserved human targets of adenosine to inosine RNA
editing.";
Nucleic Acids Res. 33:1162-1168(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, and
Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
INTERACTION WITH SHANK3, AND TISSUE SPECIFICITY.
PubMed=24153177; DOI=10.1038/nature12630;
Han K., Holder J.L. Jr., Schaaf C.P., Lu H., Chen H., Kang H.,
Tang J., Wu Z., Hao S., Cheung S.W., Yu P., Sun H., Breman A.M.,
Patel A., Lu H.C., Zoghbi H.Y.;
"SHANK3 overexpression causes manic-like behaviour with unique
pharmacogenetic properties.";
Nature 503:72-77(2013).
[9]
FUNCTION, AND INTERACTION WITH TMEM108.
PubMed=27605705; DOI=10.1091/mbc.E16-05-0326;
Xu C., Fu X., Zhu S., Liu J.J.;
"Retrolinkin recruits the WAVE1 protein complex to facilitate BDNF-
induced TrkB endocytosis and dendrite outgrowth.";
Mol. Biol. Cell 27:3342-3356(2016).
-!- FUNCTION: Part of the WAVE1 complex that regulates actin filament
reorganization via its interaction with the Arp2/3 complex (By
similarity). Involved in T-cell adhesion and p53-dependent
induction of apoptosis (By similarity). Does not bind RNA. As
component of the WAVE1 complex, required for BDNF-NTRK2 endocytic
trafficking and signaling from early endosomes (PubMed:27605705).
{ECO:0000250|UniProtKB:Q96F07, ECO:0000269|PubMed:11438699,
ECO:0000269|PubMed:27605705}.
-!- SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP1
or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Interacts with FMR1, FXR1
and FXR2 (PubMed:11438699). Interacts with FMR1; the interaction
occurs in a RNA-dependent manner (By similarity). Interacts with
RAC1 (activated form) which causes the complex to dissociate,
releasing activated WASF1 (By similarity). The complex can also be
activated by NCK1 (By similarity). Interacts with SHANK3; the
interaction mediates the association of SHANK3 with the WAVE1
complex (PubMed:24153177). Interacts with TMEM108 (via N-
terminus); the interaction associates TMEM108 with the WAVE1
complex (PubMed:27605705). {ECO:0000250|UniProtKB:Q96F07,
ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:24153177,
ECO:0000269|PubMed:27605705}.
-!- INTERACTION:
Q4ACU6:Shank3; NbExp=3; IntAct=EBI-773783, EBI-771450;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11438699}.
Nucleus {ECO:0000250|UniProtKB:Q96F07}. Cytoplasm, perinuclear
region {ECO:0000269|PubMed:11438699}. Cell junction, synapse,
synaptosome {ECO:0000269|PubMed:11438699}. Note=Highly expressed
in the perinuclear region and enriched in synaptosomes
(PubMed:11438699). {ECO:0000269|PubMed:11438699}.
-!- TISSUE SPECIFICITY: Expressed in hippocampus (at protein level).
{ECO:0000269|PubMed:24153177}.
-!- RNA EDITING: Modified_positions=320 {ECO:0000269|PubMed:15731336};
Note=Partially edited. Editing appears to be brain-specific.
{ECO:0000269|PubMed:15731336};
-!- SIMILARITY: Belongs to the CYFIP family. {ECO:0000255}.
-!- SEQUENCE CAUTION:
Sequence=BAC41472.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF334144; AAK81821.1; -; mRNA.
EMBL; AB093288; BAC41472.2; ALT_INIT; mRNA.
EMBL; AK030397; BAC26942.1; -; mRNA.
EMBL; AK147224; BAE27779.1; -; mRNA.
EMBL; AK147586; BAE28010.1; -; mRNA.
EMBL; AK147632; BAE28036.1; -; mRNA.
EMBL; AL662806; CAI24844.2; -; Genomic_DNA.
EMBL; AL713958; CAI24844.2; JOINED; Genomic_DNA.
EMBL; AL713958; CAI25371.2; -; Genomic_DNA.
EMBL; AL662806; CAI25371.2; JOINED; Genomic_DNA.
EMBL; AF162472; AAD45803.1; -; mRNA.
CCDS; CCDS24573.1; -.
RefSeq; NP_001239388.1; NM_001252459.1.
RefSeq; NP_001239389.1; NM_001252460.1.
RefSeq; NP_598530.2; NM_133769.3.
UniGene; Mm.154358; -.
UniGene; Mm.454389; -.
ProteinModelPortal; Q5SQX6; -.
SMR; Q5SQX6; -.
BioGrid; 218375; 41.
DIP; DIP-32111N; -.
IntAct; Q5SQX6; 63.
STRING; 10090.ENSMUSP00000090853; -.
iPTMnet; Q5SQX6; -.
PhosphoSitePlus; Q5SQX6; -.
SwissPalm; Q5SQX6; -.
EPD; Q5SQX6; -.
MaxQB; Q5SQX6; -.
PaxDb; Q5SQX6; -.
PeptideAtlas; Q5SQX6; -.
PRIDE; Q5SQX6; -.
Ensembl; ENSMUST00000093165; ENSMUSP00000090853; ENSMUSG00000020340.
Ensembl; ENSMUST00000093166; ENSMUSP00000090854; ENSMUSG00000020340.
Ensembl; ENSMUST00000165599; ENSMUSP00000127586; ENSMUSG00000020340.
GeneID; 76884; -.
KEGG; mmu:76884; -.
UCSC; uc007iob.2; mouse.
CTD; 26999; -.
MGI; MGI:1924134; Cyfip2.
eggNOG; KOG3534; Eukaryota.
eggNOG; ENOG410XPKW; LUCA.
GeneTree; ENSGT00500000044831; -.
HOVERGEN; HBG053209; -.
InParanoid; Q5SQX6; -.
KO; K05749; -.
OMA; DHAISRF; -.
OrthoDB; EOG091G0105; -.
PhylomeDB; Q5SQX6; -.
TreeFam; TF312925; -.
Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
ChiTaRS; Cyfip2; mouse.
PRO; PR:Q5SQX6; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020340; -.
CleanEx; MM_CYFIP2; -.
ExpressionAtlas; Q5SQX6; baseline and differential.
Genevisible; Q5SQX6; MM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0045202; C:synapse; ISO:MGI.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; ISO:MGI.
GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
GO; GO:0097484; P:dendrite extension; IMP:UniProtKB.
GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
GO; GO:0051388; P:positive regulation of neurotrophin TRK receptor signaling pathway; IMP:UniProtKB.
GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
InterPro; IPR008081; Cytoplasmic_FMR1-int.
InterPro; IPR009828; DUF1394.
PANTHER; PTHR12195; PTHR12195; 1.
Pfam; PF07159; DUF1394; 1.
Pfam; PF05994; FragX_IP; 1.
PIRSF; PIRSF008153; FMR1_interacting; 1.
PRINTS; PR01698; CYTOFMRPINTP.
1: Evidence at protein level;
Acetylation; Apoptosis; Cell adhesion; Cell junction;
Complete proteome; Cytoplasm; Nucleus; Reference proteome;
RNA editing; Synapse; Synaptosome.
CHAIN 1 1253 Cytoplasmic FMR1-interacting protein 2.
/FTId=PRO_0000279710.
MOD_RES 1037 1037 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q96F07}.
VARIANT 320 320 K -> E (in RNA edited version).
{ECO:0000269|PubMed:15731336}.
CONFLICT 76 76 G -> V (in Ref. 3; BAC26942).
{ECO:0000305}.
CONFLICT 229 229 E -> G (in Ref. 3; BAE27779).
{ECO:0000305}.
CONFLICT 242 242 V -> A (in Ref. 3; BAE27779).
{ECO:0000305}.
CONFLICT 678 678 L -> P (in Ref. 3; BAC26942).
{ECO:0000305}.
CONFLICT 1080 1080 L -> P (in Ref. 3; BAC26942).
{ECO:0000305}.
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


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