CAPON_MOUSE
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 03-AUG-2022, entry version 132.
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;
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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 CORUM; Q9D3A8; -.
DR STRING; 10090.ENSMUSP00000125251; -.
DR iPTMnet; Q9D3A8; -.
DR PhosphoSitePlus; Q9D3A8; -.
DR MaxQB; Q9D3A8; -.
DR PaxDb; Q9D3A8; -.
DR PeptideAtlas; Q9D3A8; -.
DR PRIDE; Q9D3A8; -.
DR ProteomicsDB; 265433; -. [Q9D3A8-1]
DR ProteomicsDB; 265434; -. [Q9D3A8-2]
DR Antibodypedia; 4346; 246 antibodies from 29 providers.
DR DNASU; 70729; -.
DR Ensembl; ENSMUST00000160456; ENSMUSP00000125251; ENSMUSG00000038473. [Q9D3A8-1]
DR GeneID; 70729; -.
DR KEGG; mmu:70729; -.
DR UCSC; uc011wvt.1; mouse. [Q9D3A8-1]
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; KLECYRF; -.
DR OrthoDB; 1185572at2759; -.
DR PhylomeDB; Q9D3A8; -.
DR TreeFam; TF317226; -.
DR BioGRID-ORCS; 70729; 3 hits in 72 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 163 other tissues.
DR ExpressionAtlas; Q9D3A8; baseline and differential.
DR Genevisible; Q9D3A8; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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:0031965; C:nuclear membrane; ISO:MGI.
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: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:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:2000170; P:positive regulation of peptidyl-cysteine S-nitrosylation; ISO:MGI.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; ISO:MGI.
DR GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISO:MGI.
DR GO; GO:0003062; P:regulation of heart rate by chemical signal; ISO:MGI.
DR GO; GO:1901841; P:regulation of high voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISO:MGI.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR Pfam; PF00640; PID; 1.
DR SMART; SM00462; PTB; 1.
DR PROSITE; PS01179; PID; 1.
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
