PAL1A_DANRE
ID PAL1A_DANRE Reviewed; 677 AA.
AC Q8JHF4;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Protein PALS1;
DE AltName: Full=MAGUK family factor;
DE AltName: Full=MAGUK p55 subfamily member 5-A;
DE AltName: Full=Nagie oko protein {ECO:0000303|PubMed:11992120};
DE AltName: Full=Protein associated with Lin-7 1;
GN Name=pals1a; Synonyms=mpp5, mpp5a, nok;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, DOMAIN, FUNCTION, AND MUTAGENESIS OF ILE-303.
RC TISSUE=Embryo;
RX PubMed=11992120; DOI=10.1038/ng883;
RA Wei X., Malicki J.;
RT "nagie oko, encoding a MAGUK-family protein, is essential for cellular
RT patterning of the retina.";
RL Nat. Genet. 31:150-157(2002).
CC -!- FUNCTION: Plays a role in tight junction biogenesis and in the
CC establishment of cell polarity in epithelial cells (By similarity).
CC Also involved in adherens junction biogenesis (By similarity).
CC Functions in cellular patterning of the retina (PubMed:11992120).
CC {ECO:0000250|UniProtKB:Q8N3R9, ECO:0000250|UniProtKB:Q9JLB2,
CC ECO:0000269|PubMed:11992120}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:11992120}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11992120}. Cell junction, tight junction
CC {ECO:0000269|PubMed:11992120}. Note=Localizes to the apical region of
CC the cell membrane, in the vicinity of junctional complexes in the
CC neuroepithelium and the photoreceptor layer. Enriched in the areas
CC immediately apical to the adherens junctions-associated actin bundles.
CC -!- TISSUE SPECIFICITY: Expressed in the retina and in the neural tube.
CC {ECO:0000269|PubMed:11992120}.
CC -!- DEVELOPMENTAL STAGE: Expressed early in development.
CC {ECO:0000269|PubMed:11992120}.
CC -!- DOMAIN: The PDZ domain is required for apical location.
CC {ECO:0000269|PubMed:11992120}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM77880.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF510111; AAM77880.1; ALT_INIT; mRNA.
DR RefSeq; NP_919344.1; NM_194363.1.
DR AlphaFoldDB; Q8JHF4; -.
DR SMR; Q8JHF4; -.
DR STRING; 7955.ENSDARP00000078936; -.
DR PaxDb; Q8JHF4; -.
DR PRIDE; Q8JHF4; -.
DR GeneID; 252845; -.
DR KEGG; dre:252845; -.
DR CTD; 252845; -.
DR ZFIN; ZDB-GENE-020712-1; pals1a.
DR eggNOG; KOG0609; Eukaryota.
DR InParanoid; Q8JHF4; -.
DR OrthoDB; 531106at2759; -.
DR PRO; PR:Q8JHF4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0043296; C:apical junction complex; IDA:ZFIN.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:ZFIN.
DR GO; GO:0005634; C:nucleus; IDA:ZFIN.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:ZFIN.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045176; P:apical protein localization; IGI:ZFIN.
DR GO; GO:0007420; P:brain development; IMP:ZFIN.
DR GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IMP:ZFIN.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:ZFIN.
DR GO; GO:0021954; P:central nervous system neuron development; ISS:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR GO; GO:0021744; P:dorsal motor nucleus of vagus nerve development; IMP:ZFIN.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:ZFIN.
DR GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IMP:ZFIN.
DR GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; IMP:ZFIN.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IMP:ZFIN.
DR GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; IMP:ZFIN.
DR GO; GO:0048699; P:generation of neurons; IMP:ZFIN.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IMP:ZFIN.
DR GO; GO:0008078; P:mesodermal cell migration; IMP:ZFIN.
DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; IMP:ZFIN.
DR GO; GO:0001841; P:neural tube formation; IMP:ZFIN.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:ZFIN.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:ZFIN.
DR GO; GO:0021591; P:ventricular system development; IMP:ZFIN.
DR CDD; cd12036; SH3_MPP5; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR015145; L27_N.
DR InterPro; IPR035601; MPP5_SH3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF02828; L27; 1.
DR Pfam; PF09060; L27_N; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 2.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF101288; SSF101288; 2.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell junction; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; SH3 domain; Tight junction.
FT CHAIN 1..677
FT /note="Protein PALS1"
FT /id="PRO_0000094583"
FT DOMAIN 121..178
FT /note="L27 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 180..236
FT /note="L27 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 258..338
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 347..419
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 481..662
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 1..347
FT /note="Required for the correct localization of PALS1 and
FT PATJ at cell-cell contacts and the normal formation of
FT tight junctions and adherens junctions"
FT /evidence="ECO:0000250|UniProtKB:Q9JLB2"
FT REGION 39..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 488..495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT MUTAGEN 303
FT /note="I->D: In m227; recessive, larval lethal/Disrupts all
FT retinal layers."
FT /evidence="ECO:0000269|PubMed:11992120"
SQ SEQUENCE 677 AA; 76408 MW; 5599187B897E4C60 CRC64;
MTTSHMNGYV TESDGGGGTD IVEEGVQRHR EMAVDCPSEL GARTLPVRRS AQLEKIRQQQ
EDRRRREEEG RSRQELDLNS SMRLKKLSQN PKVGIDNPTF EQMEGPGGSA GGLQSLIAPP
ALLELEDLLM SLKQVQHSLN DSQSQEDVEL VLQLVQKPDF QKAFSIHNSV AHYMNRPSPP
YPLTDHAQTL AQEVEVMVQN SSHKEGLELS SLLSTSHMQA LMMAHDSVAE QEMQLEPLVP
SVNASETLTQ WGGETVKIVR IEKAKDIPLG ATVRNDMDSV VISRIVKGGA AERSGLLHEG
DEILEINGVE IRGKDVNEVF DILADMHGVL SFVLIPSAQI KSPPIKETVV HVKAHFDYDP
SDDPYVPCRE LGLCFQKGDI LHIISQDDPN WWQAYRDGDE DNQPLAGLVP GKSFQQQREA
MKQTIEEDKE PEKTGKLWCA KKTKKKRKKM QYNANKNDDF DNEEILTYEE MALYHQPANR
KRPIALIGPP NCGQNELRQR LLSTEPDRFA GPVPHTTRSR RDAEANGRDY HFVSRQAFEM
DSAAGKFIES GEFEKNFYGT STDSVRQVIN TGKICLLCVH TQSLKVLRSS DLKPYIIFIA
PPSQERLRAL LAKDNKNPKP EELRDIIEKA REMEQNYGHL FDAAIVNTDL DKSYQELLRL
INKLDTEPQW VPSSWLR
