ID   K0319_MOUSE             Reviewed;        1081 AA.
AC   Q5SZV5; Q14BF3; Q80U39;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   24-JAN-2024, entry version 132.
DE   RecName: Full=Dyslexia-associated protein KIAA0319 homolog;
DE   Flags: Precursor;
GN   Name=Kiaa0319;
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].
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   [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].
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   [4]
RP   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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1009, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with AP2M1; required for clathrin-
CC       mediated endocytosis (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5VV43};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q5VV43}.
CC       Early endosome membrane {ECO:0000250|UniProtKB:Q5VV43}; Single-pass
CC       type I membrane protein {ECO:0000250|UniProtKB:Q5VV43}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the frontal neocortex, glanglionic
CC       eminence, mesencephalon and cerebellum at 13.5 dpc. More prominently
CC       expressed in the developing cerebral neocortex and mesencephalon at
CC       15.5 dpc and in the cortical plate and in the remnant of the
CC       ventricular zone at 18.5 dpc. {ECO:0000269|PubMed:16600991}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- PTM: O-glycosylated. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65528.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK122246; BAC65528.1; ALT_INIT; mRNA.
DR   EMBL; AL589699; CAI26085.1; -; Genomic_DNA.
DR   EMBL; BC115723; AAI15724.1; -; mRNA.
DR   EMBL; BC115940; AAI15941.1; -; mRNA.
DR   CCDS; CCDS36624.1; -.
DR   RefSeq; NP_001074520.1; NM_001081051.2.
DR   AlphaFoldDB; Q5SZV5; -.
DR   SMR; Q5SZV5; -.
DR   BioGRID; 229131; 1.
DR   IntAct; Q5SZV5; 1.
DR   STRING; 10090.ENSMUSP00000006893; -.
DR   GlyConnect; 2268; 2 N-Linked glycans (1 site).
DR   GlyCosmos; Q5SZV5; 10 sites, 2 glycans.
DR   GlyGen; Q5SZV5; 10 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; Q5SZV5; -.
DR   PhosphoSitePlus; Q5SZV5; -.
DR   MaxQB; Q5SZV5; -.
DR   PaxDb; 10090-ENSMUSP00000006893; -.
DR   ProteomicsDB; 269038; -.
DR   Antibodypedia; 2465; 135 antibodies from 27 providers.
DR   Ensembl; ENSMUST00000006893.9; ENSMUSP00000006893.9; ENSMUSG00000006711.16.
DR   GeneID; 210108; -.
DR   KEGG; mmu:210108; -.
DR   UCSC; uc007pwn.1; mouse.
DR   AGR; MGI:3036268; -.
DR   MGI; MGI:3036268; D130043K22Rik.
DR   VEuPathDB; HostDB:ENSMUSG00000006711; -.
DR   eggNOG; ENOG502QR8M; Eukaryota.
DR   GeneTree; ENSGT00940000161462; -.
DR   HOGENOM; CLU_009448_0_1_1; -.
DR   InParanoid; Q5SZV5; -.
DR   OMA; HPVDYQG; -.
DR   OrthoDB; 3021035at2759; -.
DR   PhylomeDB; Q5SZV5; -.
DR   TreeFam; TF323356; -.
DR   Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR   BioGRID-ORCS; 210108; 3 hits in 76 CRISPR screens.
DR   ChiTaRS; D130043K22Rik; mouse.
DR   PRO; PR:Q5SZV5; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q5SZV5; Protein.
DR   Bgee; ENSMUSG00000006711; Expressed in lumbar dorsal root ganglion and 118 other cell types or tissues.
DR   ExpressionAtlas; Q5SZV5; baseline and differential.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0033555; P:multicellular organismal response to stress; IMP:MGI.
DR   GO; GO:0030517; P:negative regulation of axon extension; ISO: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; ISS:UniProtKB.
DR   GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR   GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISO:MGI.
DR   GO; GO:0010996; P:response to auditory stimulus; IGI:MGI.
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; IPR011106; MANSC_N.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   PANTHER; PTHR46182:SF1; DYSLEXIA-ASSOCIATED PROTEIN KIAA0319; 1.
DR   PANTHER; PTHR46182; FI19480P1; 1.
DR   SMART; SM00765; MANEC; 1.
DR   SMART; SM00089; PKD; 5.
DR   SUPFAM; SSF49299; PKD domain; 4.
DR   PROSITE; PS50986; MANSC; 1.
DR   PROSITE; PS50093; PKD; 2.
DR   Genevisible; Q5SZV5; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Developmental protein; Endosome; Glycoprotein; Membrane;
KW   Neurogenesis; Phosphoprotein; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..1081
FT                   /note="Dyslexia-associated protein KIAA0319 homolog"
FT                   /id="PRO_0000042947"
FT   TOPO_DOM        23..964
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        965..985
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        986..1081
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          23..99
FT                   /note="MANSC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00341"
FT   DOMAIN          345..436
FT                   /note="PKD 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT   DOMAIN          444..533
FT                   /note="PKD 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT   DOMAIN          539..629
FT                   /note="PKD 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT   DOMAIN          630..723
FT                   /note="PKD 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT   DOMAIN          729..820
FT                   /note="PKD 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT   REGION          168..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1004..1007
FT                   /note="Endocytosis signal"
FT   COMPBIAS        191..210
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1009
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        430
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        507
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        522
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        545
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        560
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        742
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1081 AA;  117988 MW;  C142C9746D9AF4DA CRC64;
     MVSPPGVLSS LLLLAAMAGG SSQQCSEGRT YSDAIISPNP ETIRIMRVSQ TFSVGDCTAA
     CCDLLTCDLA WWFEGSCYLV KCMRSENCEP RTTGPIRSYL TFVRRPVQRP GQLLDYGDMM
     LSRGSPSGAW GDSLEDLRKD LPFLGKDGGP EETTEYSDEY KDLERGLLQP SNQQDPRGSA
     EYPDWSLLPS NEGGFNATAT GDNSAASMEK LQDPTPHPLD QEQLQALNES TWSPTPGHSS
     ISSVWPSSAS PLPTEEGLEG EETLQLQEQP SNSSGKEVPM PSHNPSPASL ESSPATTEKN
     SNFTVTPRSR KHSTPTFPTS TVLTGLTPPP WPLSPTASRT VKALAVSAGD NLVLTLPDRE
     AELKASVEPA PPADTTYSYE WSLMSHPVDF QGKIKQENKP TLHLSQLSVG LYAFRVAVSS
     ENAFGEGYVN VTVMPAARVN QPPVAVVSPQ TQELSVPLTS ALIDGSQSTD DTEIVSYHWE
     EVDGPFLGEE FPADTPILRL SNLVPGNYTF RLTITDSDGA TNSTTASLVI RDAVDYPPVA
     NAGPNQTITL PQNTIILNGN QSSDDHQIVL YEWFAGPGGE SKEMVMQGAQ TPYLHLSELQ
     EGEYTFQLMV TDSSGQQSTA LVAVTVQAEN NQAPVAVAGP DKELVFPVQS ATLDGSRSSD
     DHGIVCYHWE HIRGPSAVEM ENVDKAIATV TGLQVGIYHF RLTVRDQQGL SSTSTLTVAV
     KKENNSPPRA QAGGRHVLIL PNNSITLDGS RSTDDRGIVS YLWIRDGQSP AAGDVIGGSD
     HRAALQLTNL VEGVYTFHLL VTDSQGASDS DAATVEVLPD PKKDGLVELI LQVGVEQLTE
     QQKETLVRQL AVLLNVLDSD VKVLKIQAHT DVSTVIVFYV QSGSPFKVLR AAAVARNLHK
     RLSKEKEAFL LFKVLRVDTA GCLLKCSGHG HCDPITKRCI CSQLWMENLI QRYMWDGESN
     CEWSVFYVAA LALTLTLLTG AVSWLCICCC RRRKRTKIRK KTKYTILDSM DEQERMELRP
     KYGIKHRSTE HNSSLMVSES EFESDQDTLF SRERMERGVL KGSLNGCARN GVSFGYYSKD
     R
//