ID CAPON_MOUSE Reviewed; 503 AA. AC Q9D3A8; E9Q7B9; Q80TZ6; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 24-JAN-2024, entry version 140. DE RecName: Full=Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein {ECO:0000305}; DE AltName: Full=C-terminal PDZ ligand of neuronal nitric oxide synthase protein; DE AltName: Full=Nitric oxide synthase 1 adaptor protein; GN Name=Nos1ap {ECO:0000312|MGI:MGI:1917979}; Synonyms=Capon, Kiaa0464; 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 [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata; 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 [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 195-503 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=12693553; DOI=10.1093/dnares/10.1.35; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., RA Nakajima D., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II. RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL DNA Res. 10:35-48(2003). RN [4] RP INTERACTION WITH RASD1 AND NOS1. RX PubMed=11086993; DOI=10.1016/s0896-6273(00)00095-7; RA Fang M., Jaffrey S.R., Sawa A., Ye K., Luo X., Snyder S.H.; RT "Dexras1: a G protein specifically coupled to neuronal nitric oxide RT synthase via CAPON."; RL Neuron 28:183-193(2000). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-187; SER-190 AND RP SER-370, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-187; SER-190; RP SER-367; SER-370; SER-397 AND SER-413, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Heart, Kidney, Liver, Lung, 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 [7] RP FUNCTION. RX PubMed=33523862; DOI=10.1126/sciadv.abe1386; RA Majmundar A.J., Buerger F., Forbes T.A., Klaembt V., Schneider R., RA Deutsch K., Kitzler T.M., Howden S.E., Scurr M., Tan K.S., Krzeminski M., RA Widmeier E., Braun D.A., Lai E., Ullah I., Amar A., Kolb A., Eddy K., RA Chen C.H., Salmanullah D., Dai R., Nakayama M., Ottlewski I., RA Kolvenbach C.M., Onuchic-Whitford A.C., Mao Y., Mann N., Nabhan M.M., RA Rosen S., Forman-Kay J.D., Soliman N.A., Heilos A., Kain R., Aufricht C., RA Mane S., Lifton R.P., Shril S., Little M.H., Hildebrandt F.; RT "Recessive NOS1AP variants impair actin remodeling and cause glomerulopathy RT in humans and mice."; RL Sci. Adv. 7:0-0(2021). CC -!- FUNCTION: Adapter protein involved in neuronal nitric-oxide (NO) CC synthesis regulation via its association with nNOS/NOS1. The complex CC formed with NOS1 and synapsins is necessary for specific NO and CC synapsin functions at a presynaptic level. Mediates an indirect CC interaction between NOS1 and RASD1 leading to enhance the ability of CC NOS1 to activate RASD1. Competes with DLG4 for interaction with NOS1, CC possibly affecting NOS1 activity by regulating the interaction between CC NOS1 and DLG4 (By similarity). In kidney podocytes, plays a role in CC podosomes and filopodia formation through CDC42 activation CC (PubMed:33523862). {ECO:0000250|UniProtKB:O54960, CC ECO:0000269|PubMed:33523862}. CC -!- SUBUNIT: Interacts with the PDZ domain of NOS1 or the second PDZ domain CC of DLG4 through its C-terminus. Interacts with RASD1 and SYN1, SYN2 and CC SYN3 via its PID domain. Forms a ternary complex with NOS1 and SYN1 (By CC similarity). Forms a ternary complex with NOS1 and RASD1. {ECO:0000250, CC ECO:0000269|PubMed:11086993}. CC -!- SUBCELLULAR LOCATION: Cell projection, filopodium CC {ECO:0000250|UniProtKB:O54960}. Cell projection, podosome CC {ECO:0000250|UniProtKB:O54960}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9D3A8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9D3A8-2; Sequence=VSP_012462, VSP_012463; 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; AK018149; BAB31095.1; -; mRNA. DR EMBL; AC119431; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC123650; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC125017; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC125021; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK122290; BAC65572.3; -; Transcribed_RNA. DR CCDS; CCDS48438.1; -. [Q9D3A8-1] DR RefSeq; NP_001103455.1; NM_001109985.1. [Q9D3A8-1] DR AlphaFoldDB; Q9D3A8; -. DR SMR; Q9D3A8; -. DR BioGRID; 214224; 2. DR CORUM; Q9D3A8; -. DR STRING; 10090.ENSMUSP00000125251; -. DR iPTMnet; Q9D3A8; -. DR PhosphoSitePlus; Q9D3A8; -. DR MaxQB; Q9D3A8; -. DR PaxDb; 10090-ENSMUSP00000125251; -. DR PeptideAtlas; Q9D3A8; -. DR ProteomicsDB; 265433; -. [Q9D3A8-1] DR ProteomicsDB; 265434; -. [Q9D3A8-2] DR Antibodypedia; 4346; 257 antibodies from 29 providers. DR DNASU; 70729; -. DR Ensembl; ENSMUST00000160456.8; ENSMUSP00000125251.2; ENSMUSG00000038473.15. [Q9D3A8-1] DR GeneID; 70729; -. DR KEGG; mmu:70729; -. DR UCSC; uc011wvt.1; mouse. [Q9D3A8-1] DR AGR; MGI:1917979; -. DR CTD; 9722; -. DR MGI; MGI:1917979; Nos1ap. DR VEuPathDB; HostDB:ENSMUSG00000038473; -. DR eggNOG; KOG4458; Eukaryota. DR eggNOG; KOG4815; Eukaryota. DR GeneTree; ENSGT00510000046975; -. DR HOGENOM; CLU_040178_1_0_1; -. DR InParanoid; Q9D3A8; -. DR OMA; QNTMGSQ; -. DR OrthoDB; 2917768at2759; -. DR PhylomeDB; Q9D3A8; -. DR TreeFam; TF317226; -. DR BioGRID-ORCS; 70729; 3 hits in 77 CRISPR screens. DR ChiTaRS; Nos1ap; mouse. DR PRO; PR:Q9D3A8; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; Q9D3A8; Protein. DR Bgee; ENSMUSG00000038473; Expressed in primary motor cortex and 165 other cell types or tissues. DR ExpressionAtlas; Q9D3A8; baseline and differential. DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell. DR GO; GO:0098794; C:postsynapse; ISO:MGI. DR GO; GO:0098793; C:presynapse; ISO:MGI. DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:BHF-UCL. DR GO; GO:0030018; C:Z disc; IDA:BHF-UCL. DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; ISO:MGI. DR GO; GO:0050998; F:nitric-oxide synthase binding; IPI:BHF-UCL. DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI. DR GO; GO:0002020; F:protease binding; ISO:MGI. DR GO; GO:0035591; F:signaling adaptor activity; ISO:MGI. DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; ISO:MGI. DR GO; GO:0003062; P:regulation of heart rate by chemical signal; ISO:MGI. DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISO:MGI. DR CDD; cd01270; PTB_CAPON-like; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR006020; PTB/PI_dom. DR PANTHER; PTHR11232:SF76; CARBOXYL-TERMINAL PDZ LIGAND OF NEURONAL NITRIC OXIDE SYNTHASE PROTEIN; 1. DR PANTHER; PTHR11232; PHOSPHOTYROSINE INTERACTION DOMAIN-CONTAINING FAMILY MEMBER; 1. DR Pfam; PF00640; PID; 1. DR SMART; SM00462; PTB; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS01179; PID; 1. DR Genevisible; Q9D3A8; MM. PE 1: Evidence at protein level; KW Alternative splicing; Cell junction; Cell projection; Coiled coil; KW Phosphoprotein; Reference proteome. FT CHAIN 1..503 FT /note="Carboxyl-terminal PDZ ligand of neuronal nitric FT oxide synthase protein" FT /id="PRO_0000089317" FT DOMAIN 26..191 FT /note="PID" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148" FT REGION 170..212 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 491..503 FT /note="Interaction with NOS1" FT /evidence="ECO:0000250" FT COILED 318..359 FT /evidence="ECO:0000255" FT MOTIF 501..503 FT /note="PDZ-binding" FT /evidence="ECO:0000250" FT MOD_RES 183 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 187 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 190 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 262 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O75052" FT MOD_RES 367 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 370 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 397 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 413 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT VAR_SEQ 313..325 FT /note="LKDQLAAEAAARL -> SLLPSSQAPLSWA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_012462" FT VAR_SEQ 326..503 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_012463" FT CONFLICT 25 FT /note="A -> S (in Ref. 1; BAB31095)" FT /evidence="ECO:0000305" FT CONFLICT 110 FT /note="R -> K (in Ref. 1; BAB31095)" FT /evidence="ECO:0000305" FT CONFLICT 157 FT /note="G -> A (in Ref. 1; BAB31095)" FT /evidence="ECO:0000305" FT CONFLICT 311 FT /note="H -> L (in Ref. 1; BAB31095 and 3; BAC65572)" FT /evidence="ECO:0000305" SQ SEQUENCE 503 AA; 55873 MW; 1BD365C67437C8A5 CRC64; MPSKTKYNLV DDGHDLRIPL HNEDAFQHGI SFEAKYVGSL DVPRPNSRVE IVAAMRRIRY EFKAKNIKKK KVSIMVSVDG VKVILKKKKK KKEWTWDESK MLVMQDPIYR IFYVSHDSQD LKIFSYIARD GASNIFRCNV FKSKKKSQAM RIVRTVGQAF EVCHKLSLQH TQQNADGQED GESERNSDGS GDPGRQLTGA ERVSTAAAEE TDIDAVEVPL PGNDILEFSR GVTDLDAVGK DGGSHIDSTV SPHPQEPMLT ASPRMLLPSS SSKPPGLGTG TPLSTHHQMQ LLQQLLQQQQ QQTQVAVAQV HLLKDQLAAE AAARLEAQAR VHQLLLQNKD MLQHISLLVK QVQELELKLS GQNTMGSQDS LLEITFRSGA LPVLCESTTP KPEDLHSPLL GAGLADFAHP AGSPLGRHDC LVKLECFRFL PPEDTQPMMA QGEPLLGGLE LIKFRESGIA SEYESNTDES EERDSWSQEE LPRLLNVLQR QELGDSLDDE IAV //