K0319_HUMAN
ID K0319_HUMAN Reviewed; 1072 AA.
AC Q5VV43; A7MD37; B2RTU7; B4DHA7; B4DK75; B7ZML3; F5H123; Q9UJC8; Q9Y4G7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Dyslexia-associated protein KIAA0319;
DE Flags: Precursor;
GN Name=KIAA0319;
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), AND VARIANT PRO-142.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANTS
RP PRO-142 AND THR-311.
RC TISSUE=Brain, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP PRO-142 AND THR-311.
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=12834540; DOI=10.1186/1471-2164-4-25;
RA Londin E.R., Meng H., Gruen J.R.;
RT "A transcription map of the 6p22.3 reading disability locus identifying
RT candidate genes.";
RL BMC Genomics 4:25-25(2003).
RN [7]
RP POSSIBLE INVOLVEMENT IN DYX2, AND DEVELOPMENTAL STAGE.
RX PubMed=16600991; DOI=10.1093/hmg/ddl089;
RA Paracchini S., Thomas A., Castro S., Lai C., Paramasivam M., Wang Y.,
RA Keating B.J., Taylor J.M., Hacking D.F., Scerri T., Francks C.,
RA Richardson A.J., Wade-Martins R., Stein J.F., Knight J.C., Copp A.J.,
RA Loturco J., Monaco A.P.;
RT "The chromosome 6p22 haplotype associated with dyslexia reduces the
RT expression of KIAA0319, a novel gene involved in neuronal migration.";
RL Hum. Mol. Genet. 15:1659-1666(2006).
RN [8]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=17846832; DOI=10.1007/s00335-007-9051-3;
RA Velayos-Baeza A., Toma C., da Roza S., Paracchini S., Monaco A.P.;
RT "Alternative splicing in the dyslexia-associated gene KIAA0319.";
RL Mamm. Genome 18:627-634(2007).
RN [9]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND SUBUNIT.
RX PubMed=18063668; DOI=10.1093/hmg/ddm358;
RA Velayos-Baeza A., Toma C., Paracchini S., Monaco A.P.;
RT "The dyslexia-associated gene KIAA0319 encodes highly N- and O-glycosylated
RT plasma membrane and secreted isoforms.";
RL Hum. Mol. Genet. 17:859-871(2008).
RN [10]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-995, ENDOCYTOSIS SIGNAL, AND
RP INTERACTION WITH AP2M1.
RX PubMed=19419997; DOI=10.1152/ajpcell.00630.2008;
RA Levecque C., Velayos-Baeza A., Holloway Z.G., Monaco A.P.;
RT "The dyslexia-associated protein KIAA0319 interacts with adaptor protein 2
RT and follows the classical clathrin-mediated endocytosis pathway.";
RL Am. J. Physiol. 297:C160-C168(2009).
RN [11]
RP FUNCTION.
RX PubMed=19679544; DOI=10.1093/cercor/bhp154;
RA Peschansky V.J., Burbridge T.J., Volz A.J., Fiondella C., Wissner-Gross Z.,
RA Galaburda A.M., Lo Turco J.J., Rosen G.D.;
RT "The effect of variation in expression of the candidate dyslexia
RT susceptibility gene homolog Kiaa0319 on neuronal migration and dendritic
RT morphology in the rat.";
RL Cereb. Cortex 20:884-897(2010).
RN [12]
RP PROTEOLYTIC PROCESSING.
RX PubMed=20943657; DOI=10.1074/jbc.m110.145961;
RA Velayos-Baeza A., Levecque C., Kobayashi K., Holloway Z.G., Monaco A.P.;
RT "The dyslexia-associated KIAA0319 protein undergoes proteolytic processing
RT with {gamma}-secretase-independent intramembrane cleavage.";
RL J. Biol. Chem. 285:40148-40162(2010).
RN [13]
RP STRUCTURE BY NMR OF 324-428.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PKD domain (329-428) from human KIAA0319.";
RL Submitted (JUL-2007) to the PDB data bank.
RN [14]
RP VARIANT THR-311.
RX PubMed=15717286; DOI=10.1086/429131;
RA Cope N., Harold D., Hill G., Moskvina V., Stevenson J., Holmans P.,
RA Owen M.J., O'Donovan M.C., Williams J.;
RT "Strong evidence that KIAA0319 on chromosome 6p is a susceptibility gene
RT for developmental dyslexia.";
RL Am. J. Hum. Genet. 76:581-591(2005).
CC -!- FUNCTION: Involved in neuronal migration during development of the
CC cerebral neocortex. May function in a cell autonomous and a non-cell
CC autonomous manner and play a role in appropriate adhesion between
CC migrating neurons and radial glial fibers. May also regulate growth and
CC differentiation of dendrites. {ECO:0000269|PubMed:19679544}.
CC -!- SUBUNIT: Homodimer. Interacts with AP2M1; required for clathrin-
CC mediated endocytosis. {ECO:0000269|PubMed:18063668,
CC ECO:0000269|PubMed:19419997}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18063668,
CC ECO:0000269|PubMed:19419997}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:18063668}. Early endosome membrane
CC {ECO:0000269|PubMed:19419997}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:18063668}. Note=Low-abundance isoforms lacking the
CC transmembrane domain have been described; these are secreted.
CC {ECO:0000269|PubMed:18063668}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=A;
CC IsoId=Q5VV43-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VV43-2; Sequence=VSP_036235;
CC Name=3;
CC IsoId=Q5VV43-3; Sequence=VSP_036234;
CC Name=4;
CC IsoId=Q5VV43-4; Sequence=VSP_044971;
CC -!- TISSUE SPECIFICITY: Detected in adult brain cortex and fetal frontal
CC lobe (at protein level). Highly expressed in brain cortex, putamen,
CC amygdala, hippocampus and cerebellum. {ECO:0000269|PubMed:12834540,
CC ECO:0000269|PubMed:17846832}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing cerebral neocortex and
CC glanglionic eminence in 57 days post-fertilization fetal brain.
CC {ECO:0000269|PubMed:16600991}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:18063668}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:18063668}.
CC -!- PTM: Shedding of the extracellular domain and intramembrane cleavage
CC produce several proteolytic products. The intramembrane cleavage
CC releases a soluble cytoplasmic polypeptide that translocates to the
CC nucleolus. {ECO:0000269|PubMed:20943657}.
CC -!- DISEASE: Dyslexia 2 (DYX2) [MIM:600202]: A relatively common, complex
CC cognitive disorder characterized by an impairment of reading
CC performance despite adequate motivational, educational and intellectual
CC opportunities. It is a multifactorial trait, with evidence for familial
CC clustering and heritability. {ECO:0000269|PubMed:16600991}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20777.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The twisted way of things
CC - Issue 125 of January 2011;
CC URL="https://web.expasy.org/spotlight/back_issues/125";
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DR EMBL; AB002317; BAA20777.2; ALT_INIT; mRNA.
DR EMBL; AK295008; BAG58068.1; -; mRNA.
DR EMBL; AK296310; BAG59008.1; -; mRNA.
DR EMBL; AK296426; BAG59087.1; -; mRNA.
DR EMBL; AL512385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC140821; AAI40822.1; -; mRNA.
DR EMBL; BC144628; AAI44629.1; -; mRNA.
DR EMBL; BC152460; AAI52461.1; -; mRNA.
DR CCDS; CCDS34348.1; -. [Q5VV43-1]
DR CCDS; CCDS54969.1; -. [Q5VV43-3]
DR CCDS; CCDS54970.1; -. [Q5VV43-2]
DR CCDS; CCDS54971.1; -. [Q5VV43-4]
DR RefSeq; NP_001161846.1; NM_001168374.1. [Q5VV43-2]
DR RefSeq; NP_001161847.1; NM_001168375.1. [Q5VV43-1]
DR RefSeq; NP_001161848.1; NM_001168376.1. [Q5VV43-3]
DR RefSeq; NP_001161849.1; NM_001168377.1. [Q5VV43-4]
DR RefSeq; NP_055624.2; NM_014809.3. [Q5VV43-1]
DR RefSeq; XP_011513327.1; XM_011515025.2.
DR RefSeq; XP_011513328.1; XM_011515026.2. [Q5VV43-3]
DR RefSeq; XP_016867030.1; XM_017011541.1. [Q5VV43-2]
DR RefSeq; XP_016867034.1; XM_017011545.1.
DR PDB; 2E7M; NMR; -; A=329-428.
DR PDBsum; 2E7M; -.
DR AlphaFoldDB; Q5VV43; -.
DR SMR; Q5VV43; -.
DR BioGRID; 115190; 4.
DR IntAct; Q5VV43; 5.
DR STRING; 9606.ENSP00000367459; -.
DR GlyGen; Q5VV43; 10 sites.
DR iPTMnet; Q5VV43; -.
DR PhosphoSitePlus; Q5VV43; -.
DR BioMuta; KIAA0319; -.
DR DMDM; 74747200; -.
DR jPOST; Q5VV43; -.
DR MassIVE; Q5VV43; -.
DR MaxQB; Q5VV43; -.
DR PaxDb; Q5VV43; -.
DR PeptideAtlas; Q5VV43; -.
DR PRIDE; Q5VV43; -.
DR ProteomicsDB; 25518; -.
DR ProteomicsDB; 65441; -. [Q5VV43-1]
DR ProteomicsDB; 65442; -. [Q5VV43-2]
DR ProteomicsDB; 65443; -. [Q5VV43-3]
DR Antibodypedia; 2465; 125 antibodies from 26 providers.
DR DNASU; 9856; -.
DR Ensembl; ENST00000378214.8; ENSP00000367459.3; ENSG00000137261.15. [Q5VV43-1]
DR Ensembl; ENST00000430948.6; ENSP00000401086.2; ENSG00000137261.15. [Q5VV43-3]
DR Ensembl; ENST00000535378.5; ENSP00000442403.1; ENSG00000137261.15. [Q5VV43-2]
DR Ensembl; ENST00000537886.5; ENSP00000439700.1; ENSG00000137261.15. [Q5VV43-4]
DR GeneID; 9856; -.
DR KEGG; hsa:9856; -.
DR MANE-Select; ENST00000378214.8; ENSP00000367459.3; NM_014809.4; NP_055624.2.
DR UCSC; uc003neh.2; human. [Q5VV43-1]
DR CTD; 9856; -.
DR DisGeNET; 9856; -.
DR GeneCards; KIAA0319; -.
DR HGNC; HGNC:21580; KIAA0319.
DR HPA; ENSG00000137261; Group enriched (brain, pituitary gland).
DR MalaCards; KIAA0319; -.
DR MIM; 600202; phenotype.
DR MIM; 609269; gene.
DR neXtProt; NX_Q5VV43; -.
DR OpenTargets; ENSG00000137261; -.
DR PharmGKB; PA134936721; -.
DR VEuPathDB; HostDB:ENSG00000137261; -.
DR eggNOG; ENOG502QR8M; Eukaryota.
DR GeneTree; ENSGT00940000161462; -.
DR HOGENOM; CLU_009448_0_1_1; -.
DR InParanoid; Q5VV43; -.
DR OMA; TSYNYEW; -.
DR OrthoDB; 476157at2759; -.
DR PhylomeDB; Q5VV43; -.
DR TreeFam; TF323356; -.
DR PathwayCommons; Q5VV43; -.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q5VV43; -.
DR BioGRID-ORCS; 9856; 11 hits in 1062 CRISPR screens.
DR ChiTaRS; KIAA0319; human.
DR EvolutionaryTrace; Q5VV43; -.
DR GeneWiki; KIAA0319; -.
DR GenomeRNAi; 9856; -.
DR Pharos; Q5VV43; Tbio.
DR PRO; PR:Q5VV43; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5VV43; protein.
DR Bgee; ENSG00000137261; Expressed in cortical plate and 113 other tissues.
DR ExpressionAtlas; Q5VV43; baseline and differential.
DR Genevisible; Q5VV43; HS.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0033555; P:multicellular organismal response to stress; IEA:Ensembl.
DR GO; GO:0030517; P:negative regulation of axon extension; IMP:MGI.
DR GO; GO:0048692; P:negative regulation of axon extension involved in regeneration; IMP:MGI.
DR GO; GO:2000171; P:negative regulation of dendrite development; IGI:UniProtKB.
DR GO; GO:0001764; P:neuron migration; IGI:UniProtKB.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IMP:MGI.
DR GO; GO:0010996; P:response to auditory stimulus; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029865; KIAA0319-like.
DR InterPro; IPR013980; MANSC_dom.
DR InterPro; IPR011106; MANSC_N.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR002859; PKD/REJ-like.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR46182; PTHR46182; 1.
DR Pfam; PF02010; REJ; 1.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00765; MANEC; 1.
DR SMART; SM00089; PKD; 5.
DR SUPFAM; SSF49299; SSF49299; 4.
DR PROSITE; PS50986; MANSC; 1.
DR PROSITE; PS50093; PKD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Developmental protein;
KW Endosome; Glycoprotein; Membrane; Neurogenesis; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1072
FT /note="Dyslexia-associated protein KIAA0319"
FT /id="PRO_0000042946"
FT TOPO_DOM 21..955
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 956..976
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 977..1072
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..99
FT /note="MANSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00341"
FT DOMAIN 341..427
FT /note="PKD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 435..524
FT /note="PKD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 530..620
FT /note="PKD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 621..714
FT /note="PKD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 720..811
FT /note="PKD 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT REGION 168..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 995..998
FT /note="Endocytosis signal"
FT COMPBIAS 247..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..45
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036234"
FT VAR_SEQ 1..19
FT /note="MAPPTGVLSSLLLLVTIAG -> MTRLGWPSPC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_036235"
FT VAR_SEQ 953..1013
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_044971"
FT VARIANT 142
FT /note="T -> P (in dbSNP:rs4576240)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9205841"
FT /id="VAR_023837"
FT VARIANT 311
FT /note="A -> T (may be associated with susceptibility to
FT dyslexia; dbSNP:rs4504469)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15717286"
FT /id="VAR_023838"
FT VARIANT 567
FT /note="G -> S (in dbSNP:rs2744559)"
FT /id="VAR_049505"
FT VARIANT 773
FT /note="S -> G (in dbSNP:rs2744550)"
FT /id="VAR_049506"
FT VARIANT 774
FT /note="V -> A (in dbSNP:rs2817191)"
FT /id="VAR_049507"
FT VARIANT 919
FT /note="G -> A (in dbSNP:rs10946705)"
FT /id="VAR_034032"
FT VARIANT 1013
FT /note="Y -> C (in dbSNP:rs807534)"
FT /id="VAR_049508"
FT MUTAGEN 995
FT /note="Y->A: Loss of interaction with AP2M1 and impaired
FT endocytosis."
FT /evidence="ECO:0000269|PubMed:19419997"
FT CONFLICT 97
FT /note="R -> S (in Ref. 3; BAG58068)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="S -> A (in Ref. 1; BAA20777 and 5; AAI52461)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="L -> H (in Ref. 3; BAG59087)"
FT /evidence="ECO:0000305"
FT CONFLICT 926
FT /note="L -> I (in Ref. 5; AAI44629)"
FT /evidence="ECO:0000305"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:2E7M"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:2E7M"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:2E7M"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:2E7M"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:2E7M"
FT STRAND 389..395
FT /evidence="ECO:0007829|PDB:2E7M"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:2E7M"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:2E7M"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:2E7M"
FT STRAND 420..425
FT /evidence="ECO:0007829|PDB:2E7M"
SQ SEQUENCE 1072 AA; 117763 MW; 94F33B03E7FE8C0F CRC64;
MAPPTGVLSS LLLLVTIAGC ARKQCSEGRT YSNAVISPNL ETTRIMRVSH TFPVVDCTAA
CCDLSSCDLA WWFEGRCYLV SCPHKENCEP KKMGPIRSYL TFVLRPVQRP AQLLDYGDMM
LNRGSPSGIW GDSPEDIRKD LTFLGKDWGL EEMSEYSDDY RELEKDLLQP SGKQEPRGSA
EYTDWGLLPG SEGAFNSSVG DSPAVPAETQ QDPELHYLNE SASTPAPKLP ERSVLLPLPT
TPSSGEVLEK EKASQLQEQS SNSSGKEVLM PSHSLPPASL ELSSVTVEKS PVLTVTPGST
EHSIPTPPTS AAPSESTPSE LPISPTTAPR TVKELTVSAG DNLIITLPDN EVELKAFVAP
APPVETTYNY EWNLISHPTD YQGEIKQGHK QTLNLSQLSV GLYVFKVTVS SENAFGEGFV
NVTVKPARRV NLPPVAVVSP QLQELTLPLT SALIDGSQST DDTEIVSYHW EEINGPFIEE
KTSVDSPVLR LSNLDPGNYS FRLTVTDSDG ATNSTTAALI VNNAVDYPPV ANAGPNHTIT
LPQNSITLNG NQSSDDHQIV LYEWSLGPGS EGKHVVMQGV QTPYLHLSAM QEGDYTFQLK
VTDSSRQQST AVVTVIVQPE NNRPPVAVAG PDKELIFPVE SATLDGSSSS DDHGIVFYHW
EHVRGPSAVE MENIDKAIAT VTGLQVGTYH FRLTVKDQQG LSSTSTLTVA VKKENNSPPR
ARAGGRHVLV LPNNSITLDG SRSTDDQRIV SYLWIRDGQS PAAGDVIDGS DHSVALQLTN
LVEGVYTFHL RVTDSQGASD TDTATVEVQP DPRKSGLVEL TLQVGVGQLT EQRKDTLVRQ
LAVLLNVLDS DIKVQKIRAH SDLSTVIVFY VQSRPPFKVL KAAEVARNLH MRLSKEKADF
LLFKVLRVDT AGCLLKCSGH GHCDPLTKRC ICSHLWMENL IQRYIWDGES NCEWSIFYVT
VLAFTLIVLT GGFTWLCICC CKRQKRTKIR KKTKYTILDN MDEQERMELR PKYGIKHRST
EHNSSLMVSE SEFDSDQDTI FSREKMERGN PKVSMNGSIR NGASFSYCSK DR
