NYAP1_MOUSE
ID NYAP1_MOUSE Reviewed; 833 AA.
AC Q6PFX7; E1CB66; Q3UF51; Q8BNR4; Q8CCL6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 1;
GN Name=Nyap1;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH ACOT9;
RP ARHGAP26; CYFIP1; NCKAP1 AND PIK3R2, SUBUNIT, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, PHOSPHORYLATION, AND MUTAGENESIS
RP OF TYR-212 AND TYR-257.
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J;
RC TISSUE=Corpora quadrigemina, Olfactory bulb, and Sympathetic ganglion;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Activates PI3K and concomitantly recruits the WAVE1 complex
CC to the close vicinity of PI3K and regulates neuronal morphogenesis.
CC {ECO:0000269|PubMed:21946561}.
CC -!- SUBUNIT: Interacts with ACOT9, ARHGAP26 and PIK3R2. Interacts with
CC components of the WAVE1 complex, CYFIP1 and NCKAP1; this interaction
CC mediates PI3K-WAVE1 association and actin cytoskeleton remodeling.
CC {ECO:0000269|PubMed:21946561}.
CC -!- INTERACTION:
CC Q6PFX7; P27986: PIK3R1; Xeno; NbExp=4; IntAct=EBI-7447489, EBI-79464;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6PFX7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PFX7-2; Sequence=VSP_031748;
CC Name=3;
CC IsoId=Q6PFX7-3; Sequence=VSP_031747, VSP_031748;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in brain where it is
CC present in the neurons, but not in astrocytes or oligodendrites.
CC {ECO:0000269|PubMed:21946561}.
CC -!- DEVELOPMENTAL STAGE: Expression first detected in the cortical plate as
CC early as 14 dpc, peaks in the middle neocortex at postnatal day 1 and
CC then gradually decreases. At postnatal day 1, also expressed in the
CC striatum, but not in the olfactory bulb. {ECO:0000269|PubMed:21946561}.
CC -!- PTM: Phosphorylated on tyrosine residues by FYN upon stimulation with
CC CNTN5. Phosphorylation begins at 14 dpc, reaches a peak during
CC perinatal days in brain, then gradually decreases.
CC {ECO:0000269|PubMed:21946561}.
CC -!- DISRUPTION PHENOTYPE: Triple knockout mice NYAP1/NYAP2/MYO16 are
CC fertile and appear healthy. However, compared to wild-type mice they
CC show a clear reduction in brain size, exhibiting a reduction in the
CC size of the cortex and striatum, but not the olfactory bulb or corpus
CC callosum. The total neurite length of neurons in these mice is also
CC significantly shorter. {ECO:0000269|PubMed:21946561}.
CC -!- SIMILARITY: Belongs to the NYAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC38036.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB429289; BAJ19138.1; -; mRNA.
DR EMBL; AK032567; BAC27928.1; -; mRNA.
DR EMBL; AK080821; BAC38036.1; ALT_FRAME; mRNA.
DR EMBL; AK148980; BAE28710.1; -; mRNA.
DR EMBL; CH466529; EDL19242.1; -; Genomic_DNA.
DR EMBL; BC057372; AAH57372.1; -; mRNA.
DR CCDS; CCDS19775.1; -. [Q6PFX7-1]
DR CCDS; CCDS84980.1; -. [Q6PFX7-2]
DR RefSeq; NP_001334434.1; NM_001347505.1. [Q6PFX7-2]
DR RefSeq; NP_780730.2; NM_175521.3. [Q6PFX7-1]
DR RefSeq; XP_006504639.1; XM_006504576.3. [Q6PFX7-2]
DR RefSeq; XP_006504640.1; XM_006504577.3. [Q6PFX7-2]
DR AlphaFoldDB; Q6PFX7; -.
DR BioGRID; 232498; 5.
DR IntAct; Q6PFX7; 8.
DR MINT; Q6PFX7; -.
DR STRING; 10090.ENSMUSP00000113397; -.
DR iPTMnet; Q6PFX7; -.
DR PhosphoSitePlus; Q6PFX7; -.
DR PaxDb; Q6PFX7; -.
DR PRIDE; Q6PFX7; -.
DR ProteomicsDB; 293793; -. [Q6PFX7-1]
DR ProteomicsDB; 293794; -. [Q6PFX7-2]
DR ProteomicsDB; 293795; -. [Q6PFX7-3]
DR Antibodypedia; 16487; 9 antibodies from 8 providers.
DR DNASU; 243300; -.
DR Ensembl; ENSMUST00000061789; ENSMUSP00000058217; ENSMUSG00000045348. [Q6PFX7-1]
DR Ensembl; ENSMUST00000118326; ENSMUSP00000113397; ENSMUSG00000045348. [Q6PFX7-1]
DR Ensembl; ENSMUST00000212152; ENSMUSP00000148318; ENSMUSG00000045348. [Q6PFX7-2]
DR GeneID; 243300; -.
DR KEGG; mmu:243300; -.
DR UCSC; uc009adq.1; mouse. [Q6PFX7-1]
DR UCSC; uc009adr.1; mouse. [Q6PFX7-2]
DR CTD; 222950; -.
DR MGI; MGI:2443880; Nyap1.
DR VEuPathDB; HostDB:ENSMUSG00000045348; -.
DR eggNOG; ENOG502QRSX; Eukaryota.
DR GeneTree; ENSGT00890000139453; -.
DR HOGENOM; CLU_012558_0_0_1; -.
DR InParanoid; Q6PFX7; -.
DR OMA; CHSKEPT; -.
DR OrthoDB; 620667at2759; -.
DR PhylomeDB; Q6PFX7; -.
DR BioGRID-ORCS; 243300; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Nyap1; mouse.
DR PRO; PR:Q6PFX7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6PFX7; protein.
DR Bgee; ENSMUSG00000045348; Expressed in cortical plate and 166 other tissues.
DR ExpressionAtlas; Q6PFX7; baseline and differential.
DR Genevisible; Q6PFX7; MM.
DR GO; GO:0048812; P:neuron projection morphogenesis; IDA:UniProtKB.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR InterPro; IPR026724; NYAP1.
DR InterPro; IPR026722; NYAP1/NYAP2.
DR InterPro; IPR029353; NYAP_C.
DR InterPro; IPR039482; NYAP_N.
DR PANTHER; PTHR22633; PTHR22633; 1.
DR PANTHER; PTHR22633:SF2; PTHR22633:SF2; 1.
DR Pfam; PF15452; NYAP_C; 1.
DR Pfam; PF15439; NYAP_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Phosphoprotein; Reference proteome.
FT CHAIN 1..833
FT /note="Neuronal tyrosine-phosphorylated phosphoinositide-3-
FT kinase adapter 1"
FT /id="PRO_0000320930"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..181
FT /note="Involved in CYFIP1- and NCKAP1-binding"
FT REGION 219..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..392
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..259
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031747"
FT VAR_SEQ 644..645
FT /note="TE -> K (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:21946561"
FT /id="VSP_031748"
FT MUTAGEN 212
FT /note="Y->F: Abolishes binding to PIK3R2. Slight reduction
FT of phosphorylation in HEK293T cells. Abolishes
FT phosphorylation in HEK293T cells and in neurons; when
FT associated with F-257."
FT /evidence="ECO:0000269|PubMed:21946561"
FT MUTAGEN 257
FT /note="Y->F: Reduced binding to PIK3R2. Slight reduction of
FT phosphorylation in HEK293T cells. Abolishes phosphorylation
FT in HEK293T cells and neurons; when associated with F-212."
FT /evidence="ECO:0000269|PubMed:21946561"
SQ SEQUENCE 833 AA; 87668 MW; 3BC67410155550AA CRC64;
MNLLYRKTKL EWRQHKEEEA KRSSSKEAAP TGPVGPGAVP GPGVRVRDIA SLRRSLRMGF
MTMPASQEHT PHPCRSTMAP RSLSCHSVGS MDSVGGGPGG GLTEDSSTRR PPAKPRRHPS
TKLSMAGPGA ETPPSKKAGS QKPAPECRES SRKVPPQKPR RSPNTQLSVS FDESCAPAPS
PRGANLPLQR LSRASRITGD LDAGAQEEEP VYIEMVGDVF RGGGRSGGGL AGPPLGSGGP
TPPAAADSDS EDSEAIYEEM KYPLPEEAGD GRANGPPPLT APSPPQQTHI LQPHPHPHRR
PASALPSRRD GTPTKTTPCE IPPPFPNLLQ HRPPLLAFPQ AKSASRAPGD GVSRLPVLCH
SKEPAGSTPA PQVPARERET PPLPPPPPAA NLLLLGPSGR ARSHSTPLPP QGSGQTRGER
ELPNSHSMIC PKAAGVPAAH PAPAALLPGP PKDKAVSYTM VYSAVKVTTH SVLPAGPPLG
VGEPKTEEIS VLHGMLCASS RPPVPGKSSP HSGAMGSAAG VLHHRSCLAS PHSLPDPTGG
SLTPLWTYPA TAAGLKRPPA YDSLKAGGVL NKGCGMGAPS PMVKIQLQEQ GTDGGAFASI
SCAHVIASAG TPEEEEEMGA AFGAGWALQR KVLYGGRKAK EVDTEEDGAR AWNGSTEGPG
KVEHEDRGPV PSGIPVRSQG AEGLLARIHH DRGGSRTALP VPCQTFPACH RNGDFTGGYR
LGRSASTSGV RQAALHTPRP CSQPRDALSQ THPVLPLPLP PQPARERDGK LLEVIERKRC
VCKEIKARHR PDRGLCKQES MPILPSWRRV PEPRKSGTPP CRRQHTVLWD TAI
