K0319_RAT
ID K0319_RAT Reviewed; 1081 AA.
AC P0CI71;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Dyslexia-associated protein KIAA0319 homolog;
DE Flags: Precursor;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP FUNCTION.
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 [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
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).
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:16600991,
CC ECO:0000269|PubMed:19679544}.
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 -!- TISSUE SPECIFICITY: Highly expressed during development in ventricular
CC zone, intermediate zone, cortical plate, striatum, hippocampus, and
CC brain stem.
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}.
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DR EMBL; AABR03104707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001183952.1; NM_001197023.1.
DR RefSeq; XP_017456093.1; XM_017600604.1.
DR AlphaFoldDB; P0CI71; -.
DR SMR; P0CI71; -.
DR STRING; 10116.ENSRNOP00000024536; -.
DR GlyGen; P0CI71; 2 sites.
DR PaxDb; P0CI71; -.
DR Ensembl; ENSRNOT00000024536; ENSRNOP00000024536; ENSRNOG00000018141.
DR GeneID; 361244; -.
DR KEGG; rno:361244; -.
DR UCSC; RGD:1307443; rat.
DR CTD; 361244; -.
DR RGD; 1307443; RGD1307443.
DR eggNOG; ENOG502QR8M; Eukaryota.
DR GeneTree; ENSGT00940000161462; -.
DR HOGENOM; CLU_009448_0_1_1; -.
DR InParanoid; P0CI71; -.
DR OMA; TSYNYEW; -.
DR OrthoDB; 476157at2759; -.
DR PhylomeDB; P0CI71; -.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P0CI71; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000018141; Expressed in frontal cortex and 8 other tissues.
DR Genevisible; P0CI71; RN.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
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:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0033555; P:multicellular organismal response to stress; ISO:RGD.
DR GO; GO:0030517; P:negative regulation of axon extension; ISO:RGD.
DR GO; GO:0048692; P:negative regulation of axon extension involved in regeneration; ISO:RGD.
DR GO; GO:2000171; P:negative regulation of dendrite development; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISO:RGD.
DR GO; GO:0010996; P:response to auditory stimulus; ISO:RGD.
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; 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.
PE 2: Evidence at transcript level;
KW Cell membrane; Developmental protein; Endosome; Glycoprotein; Membrane;
KW Neurogenesis; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1081
FT /note="Dyslexia-associated protein KIAA0319 homolog"
FT /id="PRO_0000403479"
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 DOMAIN 444..533
FT /note="PKD 2"
FT DOMAIN 539..629
FT /note="PKD 3"
FT DOMAIN 630..723
FT /note="PKD 4"
FT DOMAIN 729..820
FT /note="PKD 5"
FT REGION 141..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1004..1007
FT /note="Endocytosis signal"
FT COMPBIAS 191..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1081 AA; 118013 MW; 799EC97AC8303F79 CRC64;
MVSPPGVLSS LLLLAAMAGG SSQQCSEGRT YSDAIISPNL ESIRIMRVSH TFSVGDCTAA
CCDLPSCDLA WWFEGSCYLV NCMRPENCEP RTTGPIRSYL TFVRRPVQRS GQLLDYGDMM
LGRGSPSGAW GDSLEDLRKD LPFLGKDGGP EETAEYSDDY KELERGLLQP SNQQDPRGSA
EYPDWSLLPS SDGDFNASAT GDNSAASTEK LQDLTPYPLD QEQLQSLNES TWSPTPRHSE
MSSMWPSSVT ASPTEEGLEG EETLQLQEQP NNSSGKKVPM PSHNPSPASL ESSPTTVEKS
SIFTVTPWSR DPGTPTFPAS TVLPGLISPS WPLSPTTSRT VKALAVSAGD NLVLTLPNGE
AELKASVEPA PPADTAYTYE WSLMSHPVDF QGKIKQENKP TLHLSQLSVG LYAFRVAVSG
ENAFGEGYVN VTVMPAARIN QPPVAIVSPQ IQELSLPLTS ALIDGSQSTD DAEIVSYHWE
EVDGPFLGEA FLDDSPLLRL SNLDPGNYTF RLTITDSDGA TNSTTAALII RGSLDYPPVA
NAGPNQTITL PQNTIILNGN QSSDDHQIVL YEWFPDPGGE SKEMVMQGAQ TPYLHLSELQ
EGEYTFQLMV TDSSGQQSTA LVTLTVQAEN NQAPVAVAGP DKELVFPVQS AMLDGSRSSD
DHGIVCYRWE HIRGPSAVEM ENVDKAIATV TGLQVGTYHF RLTVRDQQGL SSTSTLTVAV
KKENNSPPRA QAGGRHVLML PNNSITLDGS RSTDDRGIVS YLWIRDGQSP AAGDIIGSSD
NGAALQLTNL VEGVYTFHLL VTDSQGASDS DTAIVEVLPD PKKDGMVELI LQVGVEQLTE
QQKETLVRQL AVLLNVLDSD VKVLKIQAHT DVSTVIVFYV QSGSPFKVLR AADVARNLHK
RLSKEKGAFL LFKVLRIDTA GCLLKCSGHG HCDPITKRCI CSQLWMENLL QRYMWDGESN
CEWSVFYVAA LALTLTVLTG AVTWVCICCC RRRKRTKIRK KTKYTILDNM DEQERMELRP
KYGIKHRSTE HNSSLMVSES EFESDQDTLF SQERMERGVL KGSLNGSARS GVSFGYYSKD
R
