ID K319L_HUMAN Reviewed; 1049 AA. AC Q8IZA0; B1AN13; D3DPR8; O95010; Q6PJJ7; Q7L1C9; Q8N2B3; Q8NDA0; Q8WY39; AC Q8WYZ5; Q96IC3; Q96JJ0; Q9BUW6; Q9H7V0; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 2. DT 27-MAR-2024, entry version 157. DE RecName: Full=Dyslexia-associated protein KIAA0319-like protein {ECO:0000305|PubMed:20697954}; DE AltName: Full=Adeno-associated virus receptor {ECO:0000303|PubMed:26814968}; DE Short=AAVR {ECO:0000303|PubMed:26814968}; GN Name=KIAA0319L {ECO:0000312|HGNC:HGNC:30071}; GN Synonyms=AAVR {ECO:0000303|PubMed:26814968}, KIAA1837 GN {ECO:0000303|PubMed:11347906}; GN ORFNames=PP791 {ECO:0000303|PubMed:15498874}; 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 [MRNA] (ISOFORM 1). RA Hao D., Hooi S.; RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). 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 GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney, Lung, Muscle, and Placenta; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 304-1049 (ISOFORM 1). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 328-1049 (ISOFORM 1), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Amygdala; 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 359-1049 (ISOFORM 2). RC TISSUE=Brain; RX PubMed=11347906; DOI=10.1093/dnares/8.2.85; RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XX. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 8:85-95(2001). RN [9] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-472 AND ASN-525. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1037, 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 [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP FUNCTION, INTERACTION WITH RTN4R, GLYCOSYLATION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=20697954; DOI=10.1007/s10571-010-9549-1; RA Poon M.W., Tsang W.H., Chan S.O., Li H.M., Ng H.K., Waye M.M.; RT "Dyslexia-associated kiaa0319-like protein interacts with axon guidance RT receptor nogo receptor 1."; RL Cell. Mol. Neurobiol. 31:27-35(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-974; SER-978 AND SER-1031, RP AND IDENTIFICATION BY 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 [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [16] RP INTERACTION WITH AAV-2 VP1, FUNCTION (MICROBIAL INFECTION), AND SUBCELLULAR RP LOCATION. RX PubMed=26814968; DOI=10.1038/nature16465; RA Pillay S., Meyer N.L., Puschnik A.S., Davulcu O., Diep J., Ishikawa Y., RA Jae L.T., Wosen J.E., Nagamine C.M., Chapman M.S., Carette J.E.; RT "An essential receptor for adeno-associated virus infection."; RL Nature 530:108-112(2016). RN [17] RP STRUCTURE BY NMR OF 600-688. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the PKD domain from KIAA1837 protein."; RL Submitted (OCT-2007) to the PDB data bank. CC -!- FUNCTION: Possible role in axon guidance through interaction with CC RTN4R. {ECO:0000269|PubMed:20697954}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for adeno-associated CC virus and is involved in adeno-associated virus infection through CC endocytosis system. {ECO:0000269|PubMed:26814968}. CC -!- SUBUNIT: Interacts with RTN4R. {ECO:0000269|PubMed:20697954}. CC -!- SUBUNIT: (Microbial infection) Interacts with AAV-2 VP1. CC {ECO:0000269|PubMed:26814968}. CC -!- INTERACTION: CC Q8IZA0; Q9BZR6: RTN4R; NbExp=4; IntAct=EBI-5240269, EBI-5240240; CC Q8IZA0; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-5240269, EBI-747107; CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule membrane {ECO:0000305}; CC Multi-pass membrane protein {ECO:0000305}. Golgi apparatus membrane CC {ECO:0000269|PubMed:26814968}; Multi-pass membrane protein CC {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:26814968}; Multi-pass membrane protein CC {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:26814968}; Multi-pass CC membrane protein {ECO:0000305}. Note=Traffics from the plasma membrane CC to the trans-Golgi network. {ECO:0000269|PubMed:26814968}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8IZA0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8IZA0-2; Sequence=VSP_032955; CC Name=3; CC IsoId=Q8IZA0-3; Sequence=VSP_032953, VSP_032954; CC -!- TISSUE SPECIFICITY: Expressed in cortical neurons in the brain cortex CC (at protein level). {ECO:0000269|PubMed:20697954}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19159218, CC ECO:0000269|PubMed:20697954}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD05028.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=AAL55781.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB14874.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB47466.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305}; 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; AY163234; AAN61054.1; -; mRNA. DR EMBL; AF275679; AAG24389.2; -; mRNA. DR EMBL; AF289597; AAL55781.1; ALT_INIT; mRNA. DR EMBL; AC004865; AAD05028.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL356362; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL445211; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX07415.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07416.1; -; Genomic_DNA. DR EMBL; BC001858; AAH01858.2; -; mRNA. DR EMBL; BC007645; AAH07645.1; -; mRNA. DR EMBL; BC014530; AAH14530.1; -; mRNA. DR EMBL; BC031672; AAH31672.2; -; mRNA. DR EMBL; AL834315; CAD38985.1; -; mRNA. DR EMBL; AK024287; BAB14874.1; ALT_INIT; mRNA. DR EMBL; AK090878; BAC03536.1; -; mRNA. DR EMBL; AB058740; BAB47466.1; ALT_SEQ; mRNA. DR CCDS; CCDS390.1; -. [Q8IZA0-1] DR RefSeq; NP_079150.3; NM_024874.4. [Q8IZA0-1] DR RefSeq; XP_006710970.1; XM_006710907.1. DR RefSeq; XP_006710972.1; XM_006710909.1. [Q8IZA0-1] DR RefSeq; XP_006710973.1; XM_006710910.1. DR RefSeq; XP_011540481.1; XM_011542179.2. DR RefSeq; XP_016857865.1; XM_017002376.1. DR RefSeq; XP_016857867.1; XM_017002378.1. DR PDB; 2YRL; NMR; -; A=600-688. DR PDB; 6IHB; EM; 2.84 A; R=404-497. DR PDB; 6JCQ; EM; 3.30 A; R=407-497. DR PDB; 6JCS; EM; 3.18 A; R=305-401. DR PDB; 6NZ0; EM; 2.40 A; Z=311-597. DR PDB; 7KPN; EM; 1.90 A; Z=311-500. DR PDB; 7TI5; EM; 2.40 A; Z=311-597. DR PDB; 7WJX; EM; 3.23 A; R=403-497. DR PDB; 7WQP; EM; 3.76 A; R=405-496. DR PDBsum; 2YRL; -. DR PDBsum; 6IHB; -. DR PDBsum; 6JCQ; -. DR PDBsum; 6JCS; -. DR PDBsum; 6NZ0; -. DR PDBsum; 7KPN; -. DR PDBsum; 7TI5; -. DR PDBsum; 7WJX; -. DR PDBsum; 7WQP; -. DR AlphaFoldDB; Q8IZA0; -. DR EMDB; EMD-0553; -. DR EMDB; EMD-22988; -. DR EMDB; EMD-25910; -. DR EMDB; EMD-32551; -. DR EMDB; EMD-32712; -. DR EMDB; EMD-9672; -. DR EMDB; EMD-9794; -. DR EMDB; EMD-9796; -. DR SMR; Q8IZA0; -. DR BioGRID; 123007; 92. DR IntAct; Q8IZA0; 35. DR MINT; Q8IZA0; -. DR STRING; 9606.ENSP00000318406; -. DR GlyCosmos; Q8IZA0; 10 sites, 4 glycans. DR GlyGen; Q8IZA0; 23 sites, 5 O-linked glycans (14 sites). DR iPTMnet; Q8IZA0; -. DR PhosphoSitePlus; Q8IZA0; -. DR SwissPalm; Q8IZA0; -. DR BioMuta; KIAA0319L; -. DR DMDM; 187609609; -. DR EPD; Q8IZA0; -. DR jPOST; Q8IZA0; -. DR MassIVE; Q8IZA0; -. DR MaxQB; Q8IZA0; -. DR PaxDb; 9606-ENSP00000318406; -. DR PeptideAtlas; Q8IZA0; -. DR ProteomicsDB; 71307; -. [Q8IZA0-1] DR ProteomicsDB; 71308; -. [Q8IZA0-2] DR ProteomicsDB; 71309; -. [Q8IZA0-3] DR Pumba; Q8IZA0; -. DR Antibodypedia; 2498; 109 antibodies from 19 providers. DR DNASU; 79932; -. DR Ensembl; ENST00000325722.8; ENSP00000318406.3; ENSG00000142687.19. [Q8IZA0-1] DR Ensembl; ENST00000426982.7; ENSP00000395883.3; ENSG00000142687.19. [Q8IZA0-1] DR Ensembl; ENST00000469892.6; ENSP00000419396.2; ENSG00000142687.19. [Q8IZA0-1] DR GeneID; 79932; -. DR KEGG; hsa:79932; -. DR MANE-Select; ENST00000325722.8; ENSP00000318406.3; NM_024874.5; NP_079150.3. DR UCSC; uc001byx.4; human. [Q8IZA0-1] DR AGR; HGNC:30071; -. DR CTD; 79932; -. DR DisGeNET; 79932; -. DR GeneCards; KIAA0319L; -. DR HGNC; HGNC:30071; KIAA0319L. DR HPA; ENSG00000142687; Low tissue specificity. DR MalaCards; KIAA0319L; -. DR MIM; 613535; gene. DR neXtProt; NX_Q8IZA0; -. DR OpenTargets; ENSG00000142687; -. DR Orphanet; 220402; Limited cutaneous systemic sclerosis. DR Orphanet; 536; Systemic lupus erythematosus. DR PharmGKB; PA142671625; -. DR VEuPathDB; HostDB:ENSG00000142687; -. DR eggNOG; ENOG502QR8M; Eukaryota. DR GeneTree; ENSGT00940000157613; -. DR InParanoid; Q8IZA0; -. DR OMA; AYVIPDE; -. DR OrthoDB; 3021035at2759; -. DR PhylomeDB; Q8IZA0; -. DR TreeFam; TF323356; -. DR PathwayCommons; Q8IZA0; -. DR SignaLink; Q8IZA0; -. DR BioGRID-ORCS; 79932; 14 hits in 1165 CRISPR screens. DR ChiTaRS; KIAA0319L; human. DR EvolutionaryTrace; Q8IZA0; -. DR GenomeRNAi; 79932; -. DR Pharos; Q8IZA0; Tbio. DR PRO; PR:Q8IZA0; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q8IZA0; Protein. DR Bgee; ENSG00000142687; Expressed in right uterine tube and 190 other cell types or tissues. DR ExpressionAtlas; Q8IZA0; baseline and differential. DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0001764; P:neuron migration; IBA:GO_Central. DR CDD; cd00146; PKD; 4. DR Gene3D; 2.60.40.10; Immunoglobulins; 5. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR029865; KIAA0319-like. DR InterPro; IPR013980; MANSC_dom. DR InterPro; IPR022409; PKD/Chitinase_dom. DR InterPro; IPR000601; PKD_dom. DR InterPro; IPR035986; PKD_dom_sf. DR PANTHER; PTHR46182:SF3; DYSLEXIA-ASSOCIATED PROTEIN KIAA0319-LIKE PROTEIN; 1. DR PANTHER; PTHR46182; FI19480P1; 1. DR Pfam; PF18911; PKD_4; 1. DR SMART; SM00089; PKD; 5. DR SUPFAM; SSF49299; PKD domain; 4. DR PROSITE; PS50986; MANSC; 1. DR PROSITE; PS50093; PKD; 1. DR Genevisible; Q8IZA0; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Glycoprotein; KW Golgi apparatus; Host-virus interaction; Membrane; Phosphoprotein; KW Reference proteome; Repeat; Transmembrane; Transmembrane helix. FT CHAIN 1..1049 FT /note="Dyslexia-associated protein KIAA0319-like protein" FT /id="PRO_0000329064" FT TOPO_DOM 1..29 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 30..50 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 51..932 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 933..953 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 954..1049 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 49..127 FT /note="MANSC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00341" FT DOMAIN 312..401 FT /note="PKD 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151" FT DOMAIN 409..498 FT /note="PKD 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151" FT DOMAIN 504..594 FT /note="PKD 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151" FT DOMAIN 600..688 FT /note="PKD 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151" FT DOMAIN 694..785 FT /note="PKD 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151" FT REGION 1022..1049 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 974 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 978 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1009 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8K135" FT MOD_RES 1031 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1037 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT CARBOHYD 247 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 395 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 472 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 487 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 525 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT VAR_SEQ 1..563 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_032953" FT VAR_SEQ 638 FT /note="Q -> HFFFCR (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_032954" FT VAR_SEQ 989..1049 FT /note="IKQKGLLLSSSLMHSESELDSDDAIFTWPDREKGKLLHGQNGSVPNGQTPLK FT ARSPREEIL -> RGPGCQSF (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11347906" FT /id="VSP_032955" FT VARIANT 243 FT /note="G -> D (in dbSNP:rs1635712)" FT /id="VAR_042644" FT VARIANT 837 FT /note="Q -> H (in dbSNP:rs1361040)" FT /id="VAR_042645" FT CONFLICT 37 FT /note="C -> Y (in Ref. 1; AAN61054 and 2; AAG24389)" FT /evidence="ECO:0000305" FT CONFLICT 86 FT /note="W -> L (in Ref. 5; AAH14530)" FT /evidence="ECO:0000305" FT CONFLICT 203 FT /note="H -> Y (in Ref. 2; AAG24389)" FT /evidence="ECO:0000305" FT CONFLICT 520 FT /note="I -> T (in Ref. 2; AAG24389)" FT /evidence="ECO:0000305" FT STRAND 315..319 FT /evidence="ECO:0007829|PDB:7KPN" FT STRAND 326..328 FT /evidence="ECO:0007829|PDB:7KPN" FT STRAND 332..334 FT /evidence="ECO:0007829|PDB:6JCS" FT STRAND 348..350 FT /evidence="ECO:0007829|PDB:7KPN" FT STRAND 358..360 FT /evidence="ECO:0007829|PDB:7KPN" FT STRAND 362..365 FT /evidence="ECO:0007829|PDB:7KPN" FT STRAND 367..371 FT /evidence="ECO:0007829|PDB:7KPN" FT STRAND 374..382 FT /evidence="ECO:0007829|PDB:7KPN" FT STRAND 391..398 FT /evidence="ECO:0007829|PDB:7KPN" FT STRAND 415..420 FT /evidence="ECO:0007829|PDB:6NZ0" FT STRAND 426..429 FT /evidence="ECO:0007829|PDB:6NZ0" FT STRAND 434..437 FT /evidence="ECO:0007829|PDB:6NZ0" FT STRAND 441..448 FT /evidence="ECO:0007829|PDB:6NZ0" FT STRAND 461..465 FT /evidence="ECO:0007829|PDB:6NZ0" FT STRAND 470..480 FT /evidence="ECO:0007829|PDB:6NZ0" FT STRAND 482..484 FT /evidence="ECO:0007829|PDB:6NZ0" FT STRAND 486..496 FT /evidence="ECO:0007829|PDB:6NZ0" FT STRAND 607..610 FT /evidence="ECO:0007829|PDB:2YRL" FT STRAND 615..619 FT /evidence="ECO:0007829|PDB:2YRL" FT STRAND 625..627 FT /evidence="ECO:0007829|PDB:2YRL" FT STRAND 634..639 FT /evidence="ECO:0007829|PDB:2YRL" FT STRAND 644..647 FT /evidence="ECO:0007829|PDB:2YRL" FT STRAND 650..657 FT /evidence="ECO:0007829|PDB:2YRL" FT STRAND 660..671 FT /evidence="ECO:0007829|PDB:2YRL" FT STRAND 676..686 FT /evidence="ECO:0007829|PDB:2YRL" SQ SEQUENCE 1049 AA; 115658 MW; FD81BFCA3D38D106 CRC64; MEKRLGVKPN PASWILSGYY WQTSAKWLRS LYLFYTCFCF SVLWLSTDAS ESRCQQGKTQ FGVGLRSGGE NHLWLLEGTP SLQSCWAACC QDSACHVFWW LEGMCIQADC SRPQSCRAFR THSSNSMLVF LKKFQTADDL GFLPEDDVPH LLGLGWNWAS WRQSPPRAAL RPAVSSSDQQ SLIRKLQKRG SPSDVVTPIV TQHSKVNDSN ELGGLTTSGS AEVHKAITIS SPLTTDLTAE LSGGPKNVSV QPEISEGLAT TPSTQQVKSS EKTQIAVPQP VAPSYSYATP TPQASFQSTS APYPVIKELV VSAGESVQIT LPKNEVQLNA YVLQEPPKGE TYTYDWQLIT HPRDYSGEME GKHSQILKLS KLTPGLYEFK VIVEGQNAHG EGYVNVTVKP EPRKNRPPIA IVSPQFQEIS LPTTSTVIDG SQSTDDDKIV QYHWEELKGP LREEKISEDT AILKLSKLVP GNYTFSLTVV DSDGATNSTT ANLTVNKAVD YPPVANAGPN QVITLPQNSI TLFGNQSTDD HGITSYEWSL SPSSKGKVVE MQGVRTPTLQ LSAMQEGDYT YQLTVTDTIG QQATAQVTVI VQPENNKPPQ ADAGPDKELT LPVDSTTLDG SKSSDDQKII SYLWEKTQGP DGVQLENANS SVATVTGLQV GTYVFTLTVK DERNLQSQSS VNVIVKEEIN KPPIAKITGN VVITLPTSTA ELDGSKSSDD KGIVSYLWTR DEGSPAAGEV LNHSDHHPIL FLSNLVEGTY TFHLKVTDAK GESDTDRTTV EVKPDPRKNN LVEIILDINV SQLTERLKGM FIRQIGVLLG VLDSDIIVQK IQPYTEQSTK MVFFVQNEPP HQIFKGHEVA AMLKSELRKQ KADFLIFRAL EVNTVTCQLN CSDHGHCDSF TKRCICDPFW MENFIKVQLR DGDSNCEWSV LYVIIATFVI VVALGILSWT VICCCKRQKG KPKRKSKYKI LDATDQESLE LKPTSRAGIK QKGLLLSSSL MHSESELDSD DAIFTWPDRE KGKLLHGQNG SVPNGQTPLK ARSPREEIL //