K319L_HUMAN
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 03-AUG-2022, entry version 148.
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},
GN KIAA1837 {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};
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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. [Q8IZA0-1]
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. [Q8IZA0-1]
DR RefSeq; XP_016857865.1; XM_017002376.1.
DR RefSeq; XP_016857867.1; XM_017002378.1. [Q8IZA0-3]
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 PDBsum; 2YRL; -.
DR PDBsum; 6IHB; -.
DR PDBsum; 6JCQ; -.
DR PDBsum; 6JCS; -.
DR PDBsum; 6NZ0; -.
DR PDBsum; 7KPN; -.
DR AlphaFoldDB; Q8IZA0; -.
DR SMR; Q8IZA0; -.
DR BioGRID; 123007; 75.
DR IntAct; Q8IZA0; 30.
DR MINT; Q8IZA0; -.
DR STRING; 9606.ENSP00000318406; -.
DR GlyGen; Q8IZA0; 14 sites, 4 O-linked glycans (5 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; Q8IZA0; -.
DR PeptideAtlas; Q8IZA0; -.
DR PRIDE; Q8IZA0; -.
DR ProteomicsDB; 71307; -. [Q8IZA0-1]
DR ProteomicsDB; 71308; -. [Q8IZA0-2]
DR ProteomicsDB; 71309; -. [Q8IZA0-3]
DR Antibodypedia; 2498; 94 antibodies from 19 providers.
DR DNASU; 79932; -.
DR Ensembl; ENST00000325722.8; ENSP00000318406.3; ENSG00000142687.18. [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 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; CISNEAC; -.
DR OrthoDB; 476157at2759; -.
DR PhylomeDB; Q8IZA0; -.
DR TreeFam; TF323356; -.
DR PathwayCommons; Q8IZA0; -.
DR SignaLink; Q8IZA0; -.
DR BioGRID-ORCS; 79932; 13 hits in 1085 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 188 other tissues.
DR ExpressionAtlas; Q8IZA0; baseline and differential.
DR Genevisible; Q8IZA0; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 2.60.40.10; -; 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; PTHR46182; 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; 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
