CAPON_HUMAN
ID CAPON_HUMAN Reviewed; 506 AA.
AC O75052; B7ZLF5; O43564; Q3T551; Q5VU95;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 3.
DT 03-AUG-2022, entry version 160.
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|HGNC:HGNC:16859}; Synonyms=CAPON, KIAA0464;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RX PubMed=16146415; DOI=10.1371/journal.pmed.0020263;
RA Xu B., Wratten N., Charych E.I., Buyske S., Firestein B.L.,
RA Brzustowicz L.M.;
RT "Increased expression in dorsolateral prefrontal cortex of CAPON in
RT schizophrenia and bipolar disorder.";
RL PLoS Med. 2:E263-E263(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC 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 NUCLEOTIDE SEQUENCE [MRNA] OF 354-506 (ISOFORM 1), AND INTERACTION WITH
RP NOS1.
RX PubMed=9459447; DOI=10.1016/s0896-6273(00)80439-0;
RA Jaffrey S.R., Snowman A.M., Eliasson M.J.L., Cohen N.A., Snyder S.H.;
RT "CAPON: a protein associated with neuronal nitric oxide synthase that
RT regulates its interactions with PSD95.";
RL Neuron 20:115-124(1998).
RN [6]
RP INVOLVEMENT IN THE REGULATION OF QT INTERVALS, AND POLYMORPHISM.
RX PubMed=16648850; DOI=10.1038/ng1790;
RA Arking D.E., Pfeufer A., Post W., Kao W.H.L., Newton-Cheh C., Ikeda M.,
RA West K., Kashuk C., Akyol M., Perz S., Jalilzadeh S., Illig T., Gieger C.,
RA Guo C.-Y., Larson M.G., Wichmann H.E., Marban E., O'Donnell C.J.,
RA Hirschhorn J.N., Kaeaeb S., Spooner P.M., Meitinger T., Chakravarti A.;
RT "A common genetic variant in the NOS1 regulator NOS1AP modulates cardiac
RT repolarization.";
RL Nat. Genet. 38:644-651(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP VARIANT NPHS22 TYR-143, TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT
RP NPHS22 TYR-143, AND 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 RASD1.
CC Forms a ternary complex with NOS1 and SYN1.
CC {ECO:0000250|UniProtKB:O54960}.
CC -!- INTERACTION:
CC O75052; Q8N9E0: FAM133A; NbExp=3; IntAct=EBI-780467, EBI-10268158;
CC O75052; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-780467, EBI-3650647;
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=3;
CC Name=1;
CC IsoId=O75052-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75052-2; Sequence=VSP_042751, VSP_042752;
CC Name=3;
CC IsoId=O75052-3; Sequence=VSP_043350;
CC -!- TISSUE SPECIFICITY: Expressed in kidney glomeruli podocytes.
CC {ECO:0000269|PubMed:33523862}.
CC -!- POLYMORPHISM: Genetic variation in NOS1AP influences the
CC electrocardiographic QT interval [MIM:610141]. The QT interval is
CC defined as the time from the beginning of the Q wave to the end of the
CC T wave, representing the duration of ventricular electrical activity.
CC The QT interval, a measure of cardiac repolarization, is a genetically
CC influenced quantitative trait with considerable medical relevance: both
CC high and low values are associated with increased risk of
CC cardiovascular morbidity and mortality. {ECO:0000269|PubMed:16648850}.
CC -!- DISEASE: Nephrotic syndrome 22 (NPHS22) [MIM:619155]: A form of
CC nephrotic syndrome, a renal disease clinically characterized by severe
CC proteinuria, resulting in complications such as hypoalbuminemia,
CC hyperlipidemia and edema. Kidney biopsies show non-specific histologic
CC changes such as focal segmental glomerulosclerosis and diffuse
CC mesangial proliferation. Some affected individuals have an inherited
CC steroid-resistant form that progresses to end-stage renal failure.
CC NPHS22 is an autosomal recessive, steroid-resistant form characterized
CC by onset of progressive kidney dysfunction in infancy.
CC {ECO:0000269|PubMed:33523862}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA32309.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB007933; BAA32309.2; ALT_INIT; mRNA.
DR EMBL; AY841899; AAW57298.1; -; mRNA.
DR EMBL; AL590408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC112295; AAI12296.1; -; mRNA.
DR EMBL; BC143771; AAI43772.1; -; mRNA.
DR EMBL; AF037070; AAC39656.1; -; mRNA.
DR CCDS; CCDS1237.1; -. [O75052-1]
DR CCDS; CCDS44267.1; -. [O75052-2]
DR CCDS; CCDS53421.1; -. [O75052-3]
DR RefSeq; NP_001119532.2; NM_001126060.1. [O75052-2]
DR RefSeq; NP_001158229.1; NM_001164757.1. [O75052-3]
DR RefSeq; NP_055512.1; NM_014697.2. [O75052-1]
DR AlphaFoldDB; O75052; -.
DR SMR; O75052; -.
DR BioGRID; 115071; 171.
DR CORUM; O75052; -.
DR IntAct; O75052; 45.
DR MINT; O75052; -.
DR STRING; 9606.ENSP00000355133; -.
DR GlyGen; O75052; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75052; -.
DR PhosphoSitePlus; O75052; -.
DR BioMuta; NOS1AP; -.
DR EPD; O75052; -.
DR jPOST; O75052; -.
DR MassIVE; O75052; -.
DR MaxQB; O75052; -.
DR PaxDb; O75052; -.
DR PeptideAtlas; O75052; -.
DR PRIDE; O75052; -.
DR ProteomicsDB; 49725; -. [O75052-1]
DR ProteomicsDB; 49726; -. [O75052-2]
DR ProteomicsDB; 49727; -. [O75052-3]
DR Antibodypedia; 4346; 246 antibodies from 29 providers.
DR DNASU; 9722; -.
DR Ensembl; ENST00000361897.10; ENSP00000355133.5; ENSG00000198929.13. [O75052-1]
DR Ensembl; ENST00000493151.1; ENSP00000434988.1; ENSG00000198929.13. [O75052-2]
DR Ensembl; ENST00000530878.5; ENSP00000431586.1; ENSG00000198929.13. [O75052-3]
DR GeneID; 9722; -.
DR KEGG; hsa:9722; -.
DR MANE-Select; ENST00000361897.10; ENSP00000355133.5; NM_014697.3; NP_055512.1.
DR UCSC; uc001gbv.3; human. [O75052-1]
DR CTD; 9722; -.
DR DisGeNET; 9722; -.
DR GeneCards; NOS1AP; -.
DR HGNC; HGNC:16859; NOS1AP.
DR HPA; ENSG00000198929; Tissue enriched (brain).
DR MalaCards; NOS1AP; -.
DR MIM; 605551; gene.
DR MIM; 610141; phenotype.
DR MIM; 619155; phenotype.
DR neXtProt; NX_O75052; -.
DR OpenTargets; ENSG00000198929; -.
DR Orphanet; 101016; Romano-Ward syndrome.
DR PharmGKB; PA142671259; -.
DR VEuPathDB; HostDB:ENSG00000198929; -.
DR eggNOG; KOG4458; Eukaryota.
DR eggNOG; KOG4815; Eukaryota.
DR GeneTree; ENSGT00510000046975; -.
DR HOGENOM; CLU_040178_1_0_1; -.
DR InParanoid; O75052; -.
DR OMA; KLECYRF; -.
DR OrthoDB; 1185572at2759; -.
DR PhylomeDB; O75052; -.
DR TreeFam; TF317226; -.
DR PathwayCommons; O75052; -.
DR SignaLink; O75052; -.
DR BioGRID-ORCS; 9722; 211 hits in 1074 CRISPR screens.
DR ChiTaRS; NOS1AP; human.
DR GeneWiki; NOS1AP; -.
DR GenomeRNAi; 9722; -.
DR Pharos; O75052; Tbio.
DR PRO; PR:O75052; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75052; protein.
DR Bgee; ENSG00000198929; Expressed in CA1 field of hippocampus and 155 other tissues.
DR ExpressionAtlas; O75052; baseline and differential.
DR Genevisible; O75052; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005901; C:caveola; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005739; C:mitochondrion; ISS:BHF-UCL.
DR GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; ISS:BHF-UCL.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:BHF-UCL.
DR GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
DR GO; GO:0050998; F:nitric-oxide synthase binding; ISS:UniProtKB.
DR GO; GO:1902261; P:positive regulation of delayed rectifier potassium channel activity; ISS:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:BHF-UCL.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0010750; P:positive regulation of nitric oxide mediated signal transduction; ISS:BHF-UCL.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISS:BHF-UCL.
DR GO; GO:2000170; P:positive regulation of peptidyl-cysteine S-nitrosylation; ISS:BHF-UCL.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISS:BHF-UCL.
DR GO; GO:1903762; P:positive regulation of voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; ISS:BHF-UCL.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IDA:SynGO.
DR GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISS:BHF-UCL.
DR GO; GO:0098901; P:regulation of cardiac muscle cell action potential; ISS:BHF-UCL.
DR GO; GO:0003062; P:regulation of heart rate by chemical signal; IMP:BHF-UCL.
DR GO; GO:1901841; P:regulation of high voltage-gated calcium channel activity; ISS:BHF-UCL.
DR GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; NAS:DFLAT.
DR GO; GO:0050999; P:regulation of nitric-oxide synthase activity; NAS:DFLAT.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
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 Disease variant; Phosphoprotein; Reference proteome.
FT CHAIN 1..506
FT /note="Carboxyl-terminal PDZ ligand of neuronal nitric
FT oxide synthase protein"
FT /id="PRO_0000089316"
FT DOMAIN 26..196
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 175..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..506
FT /note="Interaction with NOS1"
FT /evidence="ECO:0000250"
FT COILED 322..363
FT /evidence="ECO:0000255"
FT MOTIF 504..506
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 192..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D3A8"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D3A8"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D3A8"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D3A8"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D3A8"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D3A8"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D3A8"
FT VAR_SEQ 1..17
FT /note="MPSKTKYNLVDDGHDLR -> MSLSSLCPVFSAAASSL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16146415"
FT /id="VSP_042751"
FT VAR_SEQ 18..312
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16146415"
FT /id="VSP_042752"
FT VAR_SEQ 91..95
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043350"
FT VARIANT 143
FT /note="C -> Y (in NPHS22; loss of promotion of filipodia
FT and podosome formation and migration)"
FT /evidence="ECO:0000269|PubMed:33523862"
FT /id="VAR_085238"
SQ SEQUENCE 506 AA; 56150 MW; D969C65E87684A7C CRC64;
MPSKTKYNLV DDGHDLRIPL HNEDAFQHGI CFEAKYVGSL DVPRPNSRVE IVAAMRRIRY
EFKAKNIKKK KVSIMVSVDG VKVILKKKKK LLLLQKKEWT WDESKMLVMQ DPIYRIFYVS
HDSQDLKIFS YIARDGASNI FRCNVFKSKK KSQAMRIVRT VGQAFEVCHK LSLQHTQQNA
DGQEDGESER NSNSSGDPGR QLTGAERAST ATAEETDIDA VEVPLPGNDV LEFSRGVTDL
DAVGKEGGSH TGSKVSHPQE PMLTASPRML LPSSSSKPPG LGTETPLSTH HQMQLLQQLL
QQQQQQTQVA VAQVHLLKDQ LAAEAAARLE AQARVHQLLL QNKDMLQHIS LLVKQVQELE
LKLSGQNAMG SQDSLLEITF RSGALPVLCD PTTPKPEDLH SPPLGAGLAD FAHPAGSPLG
RRDCLVKLEC FRFLPPEDTP PPAQGEALLG GLELIKFRES GIASEYESNT DESEERDSWS
QEELPRLLNV LQRQELGDGL DDEIAV
