PALS1_CANLF
ID PALS1_CANLF Reviewed; 675 AA.
AC E2QY99;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protein PALS1 {ECO:0000305};
DE AltName: Full=MAGUK p55 subfamily member 5 {ECO:0000305};
DE AltName: Full=Protein associated with Lin-7 1;
GN Name=PALS1 {ECO:0000303|PubMed:17182851}; Synonyms=MPP5;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615 {ECO:0000312|Proteomes:UP000002254};
RN [1] {ECO:0000312|Proteomes:UP000002254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer {ECO:0000312|Proteomes:UP000002254};
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP IDENTIFICATION IN A COMPLEX WITH PATJ AND CRB3, AND INTERACTION WITH CRB3.
RX PubMed=12527193; DOI=10.1016/s0378111902010843;
RA Makarova O., Roh M.H., Liu C.-J., Laurinec S., Margolis B.;
RT "Mammalian Crumbs3 is a small transmembrane protein linked to protein
RT associated with Lin-7 (Pals1).";
RL Gene 302:21-29(2003).
RN [3] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17182851; DOI=10.1091/mbc.e06-07-0651;
RA Wang Q., Chen X.W., Margolis B.;
RT "PALS1 regulates E-cadherin trafficking in mammalian epithelial cells.";
RL Mol. Biol. Cell 18:874-885(2007).
CC -!- FUNCTION: Plays a role in tight junction biogenesis and in the
CC establishment of cell polarity in epithelial cells (PubMed:17182851).
CC Also involved in adherens junction biogenesis by ensuring correct
CC localization of the exocyst complex protein EXOC4/SEC8 which allows
CC trafficking of adherens junction structural component CDH1 to the cell
CC surface (PubMed:17182851). Plays a role through its interaction with
CC CDH5 in vascular lumen formation and endothelial membrane polarity (By
CC similarity). Required during embryonic and postnatal retinal
CC development (By similarity). Required for the maintenance of cerebellar
CC progenitor cells in an undifferentiated proliferative state, preventing
CC premature differentiation, and is required for cerebellar histogenesis,
CC fissure formation, cerebellar layer organization and cortical
CC development (By similarity). Plays a role in neuronal progenitor cell
CC survival, potentially via promotion of mTOR signaling (By similarity).
CC Plays a role in the radial and longitudinal extension of the myelin
CC sheath in Schwann cells (By similarity). May modulate SC6A1/GAT1-
CC mediated GABA uptake by stabilizing the transporter (By similarity).
CC May play a role in the T-cell receptor-mediated activation of NF-kappa-
CC B (By similarity). Required for localization of EZR to the apical
CC membrane of parietal cells and may play a role in the dynamic
CC remodeling of the apical cytoskeleton (By similarity). Required for the
CC normal polarized localization of the vesicular marker STX4 (By
CC similarity). Required for the correct trafficking of the myelin
CC proteins PMP22 and MAG (By similarity). Involved in promoting
CC phosphorylation and cytoplasmic retention of transcriptional
CC coactivators YAP1 and WWTR1/TAZ which leads to suppression of TGFB1-
CC dependent transcription of target genes such as CCN2/CTGF,
CC SERPINE1/PAI1, SNAI1/SNAIL1 and SMAD7 (By similarity).
CC {ECO:0000250|UniProtKB:B4F7E7, ECO:0000250|UniProtKB:Q8N3R9,
CC ECO:0000250|UniProtKB:Q9JLB2, ECO:0000269|PubMed:17182851}.
CC -!- SUBUNIT: Heterodimer with MPP1 (By similarity). Forms a heterotrimeric
CC complex composed of PALS1, LIN7B and PATJ; the N-terminal L27 domain of
CC PALS1 interacts with the L27 domain of PATJ and the C-terminal L27
CC domain of PALS1 interacts with the L27 domain of LIN7B (By similarity).
CC Component of a complex composed of PALS1, CRB1 and MPP4 (By
CC similarity). Component of a complex whose core is composed of ARHGAP17,
CC AMOT, PALS1, PATJ and PARD3/PAR3 (By similarity). Component of a
CC complex composed of PALS1, CRB1 and EPB41L5 (By similarity). Within the
CC complex, interacts (via HOOK domain) with EPB41L5 (via FERM domain),
CC and interacts with CRB1 (via intracellular domain) (By similarity).
CC Component of a complex composed of PALS1, MPP3 and CRB1; PALS1 acts as
CC a bridging protein between MPP3 (via guanylate kinase-like domain) and
CC CRB1 (By similarity). Component of a complex composed of CRB3, PALS1
CC and PATJ (PubMed:12527193). Interacts (via PDZ domain) with PATJ (via
CC N-terminus) (By similarity). Interacts with EZR (By similarity).
CC Interacts (via PDZ domain) with CRB1 (via C-terminal ERLI motif) (By
CC similarity). While the PDZ domain is sufficient for interaction with
CC CRB1, the adjacent SH3 and guanylate kinase-like domains are likely to
CC contribute to a high affinity interaction (By similarity). Interacts
CC with WWTR1/TAZ (via WW domain) (By similarity). Interacts with MPP7 (By
CC similarity). Interacts (via PDZ domain) with CRB3 (via C-terminus)
CC (PubMed:12527193). Interacts with LIN7C (By similarity). Interacts with
CC MPDZ (By similarity). Interacts with PARD6B (By similarity). Interacts
CC with SC6A1 (By similarity). Interacts with CDH5; the interaction
CC promotes PALS1 localization to cell junctions and is required for CDH5-
CC mediated vascular lumen formation and endothelial cell (By similarity).
CC Interacts with NPHP1 (via coiled coil and SH3 domains) (By similarity).
CC Interacts with NPHP4 (By similarity). Interacts with CRB2 (By
CC similarity). {ECO:0000250|UniProtKB:Q8N3R9,
CC ECO:0000250|UniProtKB:Q9JLB2, ECO:0000269|PubMed:12527193}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q8N3R9}.
CC Cell membrane {ECO:0000250|UniProtKB:Q9JLB2}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q9JLB2}. Endomembrane system
CC {ECO:0000250|UniProtKB:Q9JLB2}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9JLB2}. Cell junction, tight junction
CC {ECO:0000269|PubMed:17182851}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:17182851}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9JLB2}. Perikaryon
CC {ECO:0000250|UniProtKB:Q9JLB2}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q8N3R9}. Note=Localized to the tight junctions
CC of epithelial cells (By similarity). Localized to the Golgi apparatus
CC in T lymphocytes (By similarity). Localized to a subset of
CC intracellular vesicles (By similarity). Localized to the Purkinje cell
CC body and axon (By similarity). Localized to intercellular junctions in
CC vascular endothelial cells (By similarity). Localized to Schmidt-
CC Lanterman incisures, the adaxonal domain, and the inner part of
CC paranodal loops in myelinating Schwann cells of the sciatic nerve (By
CC similarity). Localized to apical membrane domains of the outer limiting
CC membrane (OLM) junctions in the retina (By similarity). Colocalizes
CC with CRB1 at the OLM, apical to the adherens junction (By similarity).
CC Colocalizes with MPP1 in the retina at the OLM (By similarity).
CC Colocalizes with MPP3 to the subapical region of adherens junctions in
CC the retina OLM (By similarity). {ECO:0000250|UniProtKB:Q8N3R9,
CC ECO:0000250|UniProtKB:Q9JLB2}.
CC -!- DOMAIN: The L27 domain 1 functions in targeting to the tight junctions
CC by binding to and stabilizing PATJ. {ECO:0000250|UniProtKB:Q9JLB2}.
CC -!- DOMAIN: The PDZ domain binds to the C-terminus of SC6A1.
CC {ECO:0000250|UniProtKB:Q9JLB2}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; AAEX03005795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005623574.1; XM_005623517.2.
DR RefSeq; XP_005623575.1; XM_005623518.2.
DR RefSeq; XP_005623576.1; XM_005623519.2.
DR RefSeq; XP_005623577.1; XM_005623520.2.
DR RefSeq; XP_547862.2; XM_547862.5.
DR AlphaFoldDB; E2QY99; -.
DR SMR; E2QY99; -.
DR CORUM; E2QY99; -.
DR STRING; 9615.ENSCAFP00000024081; -.
DR PaxDb; E2QY99; -.
DR Ensembl; ENSCAFT00030031469; ENSCAFP00030027451; ENSCAFG00030017049.
DR Ensembl; ENSCAFT00030031577; ENSCAFP00030027534; ENSCAFG00030017049.
DR Ensembl; ENSCAFT00040019323; ENSCAFP00040016768; ENSCAFG00040010408.
DR GeneID; 490740; -.
DR KEGG; cfa:490740; -.
DR CTD; 64398; -.
DR eggNOG; KOG0609; Eukaryota.
DR HOGENOM; CLU_001715_5_4_1; -.
DR InParanoid; E2QY99; -.
DR OMA; LKHIQHV; -.
DR OrthoDB; 531106at2759; -.
DR TreeFam; TF314263; -.
DR Proteomes; UP000002254; Unplaced.
DR Bgee; ENSCAFG00000016353; Expressed in renal medulla and 46 other tissues.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; 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:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043219; C:lateral loop; IEA:Ensembl.
DR GO; GO:0035749; C:myelin sheath adaxonal region; IEA:Ensembl.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
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:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; IBA:GO_Central.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0048699; P:generation of neurons; IBA:GO_Central.
DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; IBA:GO_Central.
DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; IEA:Ensembl.
DR GO; GO:0035750; P:protein localization to myelin sheath abaxonal region; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
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; Cell projection;
KW Golgi apparatus; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Tight junction.
FT CHAIN 1..675
FT /note="Protein PALS1"
FT /id="PRO_0000447573"
FT DOMAIN 120..177
FT /note="L27 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 179..235
FT /note="L27 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 256..336
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 345..417
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 479..660
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 1..345
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 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 21..140
FT /note="Interaction with PARD6B"
FT /evidence="ECO:0000250|UniProtKB:Q9JLB2"
FT REGION 181..243
FT /note="Interaction with LIN7C"
FT /evidence="ECO:0000250|UniProtKB:Q9JLB2"
FT COMPBIAS 10..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 486..493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3R9"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLB2"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3R9"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3R9"
SQ SEQUENCE 675 AA; 77232 MW; 765259AA78501EE9 CRC64;
MTTSHMNGHV TEESDNEVKN VDLASPEEHQ KHREMAVDCP GDLGTRMMPV RRSAQLERIR
QQQEDMRRRR EEEGKKQELD LNSSMRLKKL AQIPPKTGID NPIFDTEEGI VLESPHYAVK
ILEVEDLFSS LKHIQHTLVD SQSQEDISLL LQLVQNKDFQ NAFKIHNAVT VHMNKASPPF
PLISNAQDLA QEVQTVLKPV HHKEGQELTA LLSAPHVQAL LLAHDKVAEQ EMQLEPFTDE
RVYESIGQYG GETVKIVRIE KARDIPLGAT VRNEMDSVII SRIVKGGAAE KSGLLHEGDE
VLEINGIEIR GKDVNEVFDL LSDMHGTLTF VLIPSQQIKP PPAKETVIHV KAHFDYDPSD
DPYVPCRELG LSFQKGDILH IISQEDPNWW QAYREGDEDN QPLAGLVPGK SFQQQREAMK
QTIEEDKEPE KSGKLWCAKK NKKKRKKVLY NANKNDDYDN EEILTYEEMS LYHQPANRKR
PIILIGPQNC GQNELRQRLM NKEKDRFASA VPHTTRSRRD HEVAGRDYHF VSRQAFEADI
AAGKFIEHGE FEKNLYGTSI DSVRQVINSG KICLLSLRTQ SLKTLRNSDL KPYIIFIAPP
SQERLRALLA KEGKNPKPEE LREIIEKTRE MEQNNGHYFD TAIVNSDLDK AYQELLRLIN
KLDTEPQWVP SSWLR
