K0319_MOUSE
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 03-AUG-2022, entry version 124.
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 GlyGen; Q5SZV5; 10 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q5SZV5; -.
DR PhosphoSitePlus; Q5SZV5; -.
DR MaxQB; Q5SZV5; -.
DR PaxDb; Q5SZV5; -.
DR PRIDE; Q5SZV5; -.
DR ProteomicsDB; 269038; -.
DR Antibodypedia; 2465; 125 antibodies from 26 providers.
DR Ensembl; ENSMUST00000006893; ENSMUSP00000006893; ENSMUSG00000006711.
DR GeneID; 210108; -.
DR KEGG; mmu:210108; -.
DR UCSC; uc007pwn.1; mouse.
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; TSYNYEW; -.
DR OrthoDB; 476157at2759; -.
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 71 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 116 other tissues.
DR ExpressionAtlas; Q5SZV5; baseline and differential.
DR Genevisible; Q5SZV5; MM.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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 Gene3D; 2.60.40.10; -; 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; PTHR46182; 1.
DR SMART; SM00765; MANEC; 1.
DR SMART; SM00089; PKD; 5.
DR SUPFAM; SSF49299; SSF49299; 4.
DR PROSITE; PS50986; MANSC; 1.
DR PROSITE; PS50093; PKD; 2.
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
