K319L_MOUSE
ID K319L_MOUSE Reviewed; 1048 AA.
AC Q8K135; A2A790; Q3TTA3; Q8BHR5; Q8BHU7; Q8BHZ3; Q8VBZ9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Dyslexia-associated protein KIAA0319-like protein {ECO:0000250|UniProtKB:Q8IZA0};
DE AltName: Full=Adeno-associated virus receptor {ECO:0000250|UniProtKB:Q8IZA0};
DE Short=AAVR {ECO:0000250|UniProtKB:Q8IZA0};
GN Name=Kiaa0319l {ECO:0000250|UniProtKB:Q8IZA0};
GN Synonyms=Aavr {ECO:0000303|PubMed:26814968};
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Brain, Cerebellum, Embryo, Embryonic heart, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney, and Liver;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1008, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Pancreas, and Testis;
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).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION (MICROBIAL INFECTION).
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).
CC -!- FUNCTION: Possible role in axon guidance through interaction with
CC RTN4R. {ECO:0000250|UniProtKB:Q8IZA0}.
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:0000305|PubMed:26814968}.
CC -!- SUBUNIT: Interacts with RTN4R. {ECO:0000250|UniProtKB:Q8IZA0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule membrane
CC {ECO:0000250|UniProtKB:Q8IZA0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8IZA0}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8IZA0}; Multi-pass membrane protein. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q8IZA0};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IZA0}. Cell
CC membrane {ECO:0000250|UniProtKB:Q8IZA0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8IZA0}. Note=Traffics from the plasma membrane
CC to the trans-Golgi network. {ECO:0000250|UniProtKB:Q8IZA0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K135-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K135-2; Sequence=VSP_032956;
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice Kiaa0319l are normal.
CC {ECO:0000269|PubMed:26814968}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22154.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AK043006; BAC31432.1; -; mRNA.
DR EMBL; AK049570; BAC33818.1; -; mRNA.
DR EMBL; AK084668; BAC39244.1; -; mRNA.
DR EMBL; AK147569; BAE27999.1; -; mRNA.
DR EMBL; AK161493; BAE36422.1; -; mRNA.
DR EMBL; AK170261; BAE41669.1; -; mRNA.
DR EMBL; AL606908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022154; AAH22154.1; ALT_SEQ; mRNA.
DR EMBL; BC028869; AAH28869.1; -; mRNA.
DR CCDS; CCDS18660.1; -. [Q8K135-2]
DR CCDS; CCDS18661.1; -. [Q8K135-1]
DR RefSeq; NP_001030602.1; NM_001035525.1.
DR RefSeq; NP_001030603.1; NM_001035526.1.
DR RefSeq; NP_598647.1; NM_133886.2. [Q8K135-1]
DR RefSeq; XP_017175383.1; XM_017319894.1. [Q8K135-1]
DR RefSeq; XP_017175384.1; XM_017319895.1. [Q8K135-1]
DR RefSeq; XP_017175385.1; XM_017319896.1. [Q8K135-1]
DR RefSeq; XP_017175386.1; XM_017319897.1. [Q8K135-1]
DR AlphaFoldDB; Q8K135; -.
DR SMR; Q8K135; -.
DR STRING; 10090.ENSMUSP00000099667; -.
DR GlyConnect; 2269; 3 N-Linked glycans (2 sites).
DR GlyConnect; 2422; 2 N-Linked glycans (1 site). [Q8K135-2]
DR GlyGen; Q8K135; 4 sites, 3 N-linked glycans (2 sites).
DR iPTMnet; Q8K135; -.
DR PhosphoSitePlus; Q8K135; -.
DR SwissPalm; Q8K135; -.
DR CPTAC; non-CPTAC-3586; -.
DR EPD; Q8K135; -.
DR MaxQB; Q8K135; -.
DR PaxDb; Q8K135; -.
DR PeptideAtlas; Q8K135; -.
DR PRIDE; Q8K135; -.
DR ProteomicsDB; 268947; -. [Q8K135-1]
DR ProteomicsDB; 268948; -. [Q8K135-2]
DR Antibodypedia; 2498; 94 antibodies from 19 providers.
DR DNASU; 100317; -.
DR Ensembl; ENSMUST00000047431; ENSMUSP00000037802; ENSMUSG00000028830. [Q8K135-1]
DR GeneID; 100317; -.
DR KEGG; mmu:100317; -.
DR UCSC; uc008utw.1; mouse. [Q8K135-1]
DR MGI; MGI:2140475; AU040320.
DR VEuPathDB; HostDB:ENSMUSG00000028830; -.
DR eggNOG; ENOG502QR8M; Eukaryota.
DR GeneTree; ENSGT00940000157613; -.
DR HOGENOM; CLU_009448_0_0_1; -.
DR InParanoid; Q8K135; -.
DR OrthoDB; 476157at2759; -.
DR PhylomeDB; Q8K135; -.
DR TreeFam; TF323356; -.
DR BioGRID-ORCS; 100317; 1 hit in 70 CRISPR screens.
DR ChiTaRS; AU040320; mouse.
DR PRO; PR:Q8K135; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8K135; protein.
DR Bgee; ENSMUSG00000028830; Expressed in seminal vesicle and 268 other tissues.
DR ExpressionAtlas; Q8K135; baseline and differential.
DR Genevisible; Q8K135; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR GO; GO:0001675; P:acrosome assembly; IMP:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0120211; P:proacrosomal vesicle fusion; IMP:MGI.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; IMP:MGI.
DR GO; GO:0010996; P:response to auditory stimulus; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP: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; 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 Alternative splicing; Cell membrane; Glycoprotein; Golgi apparatus;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1048
FT /note="Dyslexia-associated protein KIAA0319-like protein"
FT /id="PRO_0000329065"
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..928
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 929..949
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 950..1048
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 49..127
FT /note="MANSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00341"
FT DOMAIN 309..400
FT /note="PKD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 408..497
FT /note="PKD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 503..593
FT /note="PKD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 599..687
FT /note="PKD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 693..784
FT /note="PKD 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT REGION 198..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 973
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZA0"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZA0"
FT MOD_RES 1008
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1030
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZA0"
FT MOD_RES 1036
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZA0"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1025..1048
FT /note="YGQNGSVPNGQTPLKSRSAREEIL -> ALHWCRSQSLHHIGWWCRAPVCHE
FT TSSTNSTPGSDSGFCKGGKNLSSDYRTRTKSALVHGK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032956"
FT CONFLICT 4
FT /note="R -> G (in Ref. 1; BAC39244)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="Missing (in Ref. 1; BAE36422)"
FT /evidence="ECO:0000305"
FT CONFLICT 656
FT /note="G -> V (in Ref. 1; BAC33818)"
FT /evidence="ECO:0000305"
FT CONFLICT 684
FT /note="V -> A (in Ref. 1; BAC33818)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1048 AA; 115312 MW; F4D51DD6DE4C889D CRC64;
MEKRLGVKPS PASWVLPGYC WQTSVKLPRS LYLLYSFFCF SVLWLSTDAD ESRCQQGKTL
YGAGLRTEGE NHLRLLAGSL PFHACRAACC RDSACHALWW LEGMCFQADC SKPQSCQPFR
TDSSNSMLII FQKSQTTDDL GLLPEDDEPH LLRLGWGRTS WRRQSLLGAP LTLSVPSSHH
QSLLRDRQKR DLSVVPTHGA MQHSKVNHSE EAGALSPTSA EVRKTITVAG SFTSNHTTQT
PEWPKNVSIH PEPSEHSSPV SGTPQVKSTE HSPTDAPLPV APSYSYATPT PQASSQSTSA
PHPVVKELVV SAGKSVQITL PKNEVQLNAF VLPEAEPGET YTYDWQLITH PTDYSGEVER
KHSQSLQLSK LTPGLYEFKV TVDGQNAHGE GYVNVTVKPE PRKNRPPVAV VSPQFQEISL
PTTSTIIDGS QSTDDDKIVQ YHWEELKGPL REEKISEDTA ILKLSKLVPG NYTFSLTVVD
SDGATNSTTA SLTVNKAVDY PPVANAGPNQ VITLPQNSIT LFGNQSTDDH GITSYEWSLS
PSSKGKVVEM QGVRTPALQL SAMQEGDYTY QLTVTDTAGQ QATAQVTVIV QPENNKPPQA
DAGPDKELTL PVDSTTLDGS KSTDDQRVVS YLWEQSRGPD GVQLENANSS VATVTGLQVG
TYVFTLTVKD ERNLQSQSSV NVIVKEEINK PPVAKIAGNV VVTLPTSTAE LDGSRSSDDK
GIVSYLWTRD ETSPAAGEVL NHSDHHPVLF LSNLVEGTYT FHLKVTDAKG ESDTDRTTVE
VKPDPRKSNL VEIILDVNVS QLTERLKGML IRQIGVLLGV LDSDIIVQKI QPYTEQSTKM
LFFVQNDPPH QLFKGHEVAA MLKSELQKQK ADFLIFRALE ISTVTCQLNC SDHGHCDSFT
KRCVCDPFWM ENFIKVQLRD GDSNCEWSVL YVIIASFVIV VALGILSWTT ICCCKRQKGK
PKRKSRYKIL DATDQESLEL KPTSRAGSKQ KGPTLSSSLM HSESELDSDD AIFTWPDREK
GKLLYGQNGS VPNGQTPLKS RSAREEIL
