K319L_PONAB
ID K319L_PONAB Reviewed; 1049 AA.
AC Q5RFR6; Q5R745;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
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:0000250|UniProtKB:Q8IZA0};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Possible role in axon guidance through interaction with
CC RTN4R. {ECO:0000250|UniProtKB:Q8IZA0}.
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=Q5RFR6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RFR6-2; Sequence=VSP_032957;
CC -!- PTM: N-glycosylated. {ECO:0000250}.
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DR EMBL; CR857086; CAH89391.1; -; mRNA.
DR EMBL; CR860273; CAH92415.1; -; mRNA.
DR RefSeq; NP_001124549.1; NM_001131077.1. [Q5RFR6-1]
DR RefSeq; XP_009250745.1; XM_009252470.1.
DR AlphaFoldDB; Q5RFR6; -.
DR SMR; Q5RFR6; -.
DR STRING; 9601.ENSPPYP00000001797; -.
DR Ensembl; ENSPPYT00000001854; ENSPPYP00000001797; ENSPPYG00000001558. [Q5RFR6-1]
DR GeneID; 100127092; -.
DR KEGG; pon:100127092; -.
DR CTD; 79932; -.
DR eggNOG; ENOG502QR8M; Eukaryota.
DR GeneTree; ENSGT00940000157613; -.
DR HOGENOM; CLU_009448_0_0_1; -.
DR InParanoid; Q5RFR6; -.
DR OrthoDB; 476157at2759; -.
DR TreeFam; TF323356; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
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:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Glycoprotein; Golgi apparatus;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1049
FT /note="Dyslexia-associated protein KIAA0319-like protein"
FT /id="PRO_0000329066"
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 310..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 234..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 974
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZA0"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZA0"
FT MOD_RES 1009
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K135"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZA0"
FT MOD_RES 1037
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZA0"
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 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..358
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_032957"
FT CONFLICT 397
FT /note="T -> A (in Ref. 1; CAH92415)"
FT /evidence="ECO:0000305"
FT CONFLICT 995
FT /note="V -> A (in Ref. 1; CAH92415)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1049 AA; 115740 MW; 32F20C9AFF4D8A49 CRC64;
MEKRLGVKPN PASWILSGYY WQTSAKWLRT LYLFYTCFCF SVLWLSTDAS ESRCQQGKTQ
FGVGLRSGGE NHLWLLEGTP SLQSCWAACC QDSACHVFWW LEGMCIQADC SRPQSCRAFR
THSSNSMLMF LKKFQTADDL GFLPEDDVPH LLGLGWNWAS WRQSPPRAAL RPAVSSSDQQ
SLIRKLQKRG SPSEVVTPIV TQHSKVNDSN ELGGLTTSGS AEVHKAITIS SPLTTDLTAE
LPGGPKNVSA QPEIPEGLAT TPSTQQVKSS EKTQIAVPQP VAPSYSYGTP TPQASFQSTS
APYPVIKELV VSAGDSVQIT 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 SIATVTGLQV
GTYVFTLTVK DERNLQSQSS VNVIVKEEIN KPPIAKITGN VVITLPTSTA ELDGSKSSDD
KGIVSYLWTR DEGSPAAGEV LNHSDHHPIL FLSNLVEGTY TFHLKVTDAK GESDTDRTTV
EVKPDPRKNN LVEIILDINV SQLTERLKGM FIRQIGVLLG VLDSDIIVQK IQPYTEQSTK
MVFFVQNEPP HQIFKGHEVA AMLKSELRKQ KADFLIFRAL EINTVTCQLN CSDHGHCDSF
TKRCICDPFW MENFIKVQLR DGESNCEWSV LYVIIATFVI VVALGILSWT VICCCKRQKG
KPKRKSKYKI LDATDQESLE LKPTSRTGIK QKGLVLSSSL MHSESELDSD DAIFTWPDRE
KGKLLHGQNG SVPNGQTPLK ARSPREEIL
