PALS2_MOUSE
ID PALS2_MOUSE Reviewed; 553 AA.
AC Q9JLB0; Q9JLB1; Q9WV37;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Protein PALS2 {ECO:0000305};
DE AltName: Full=Dlgh4 protein;
DE AltName: Full=MAGUK p55 subfamily member 6;
DE AltName: Full=P55T protein;
DE AltName: Full=Protein associated with Lin-7 2 {ECO:0000303|PubMed:10753959};
GN Name=Pals2 {ECO:0000303|PubMed:10753959, ECO:0000312|MGI:MGI:1927340};
GN Synonyms=Dlgh4, Mpp6 {ECO:0000312|MGI:MGI:1927340};
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 [MRNA] (ISOFORMS ALPHA AND BETA).
RX PubMed=10753959; DOI=10.1074/jbc.275.15.11425;
RA Kamberov E., Makarova O., Roh M., Liu A., Karnak D., Straight S.,
RA Margolis B.;
RT "Molecular cloning and characterization of Pals, proteins associated with
RT mLin-7.";
RL J. Biol. Chem. 275:11425-11431(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RA Lin L., Chishti A.H.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH CADM1.
RX PubMed=12826663; DOI=10.1074/jbc.m305387200;
RA Shingai T., Ikeda W., Kakunaga S., Morimoto K., Takekuni K., Itoh S.,
RA Satoh K., Takeuchi M., Imai T., Monden M., Takai Y.;
RT "Implications of nectin-like molecule-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in
RT cell-cell adhesion and transmembrane protein localization in epithelial
RT cells.";
RL J. Biol. Chem. 278:35421-35427(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Spleen, and
RC 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).
CC -!- SUBUNIT: Interacts with CADM1. Interacts with the LIN7 proteins.
CC {ECO:0000269|PubMed:12826663}.
CC -!- INTERACTION:
CC Q9JLB0; O70318: Epb41l2; NbExp=3; IntAct=EBI-771456, EBI-643339;
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Beta;
CC IsoId=Q9JLB0-1; Sequence=Displayed;
CC Name=Alpha;
CC IsoId=Q9JLB0-2; Sequence=VSP_003161;
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; AF199009; AAF63790.1; -; mRNA.
DR EMBL; AF199010; AAF63791.1; -; mRNA.
DR EMBL; AF161181; AAD45009.1; -; mRNA.
DR CCDS; CCDS20128.1; -. [Q9JLB0-2]
DR CCDS; CCDS51770.1; -. [Q9JLB0-1]
DR RefSeq; NP_001158205.1; NM_001164733.1. [Q9JLB0-1]
DR RefSeq; NP_001158206.1; NM_001164734.1. [Q9JLB0-1]
DR RefSeq; NP_064323.2; NM_019939.2. [Q9JLB0-2]
DR AlphaFoldDB; Q9JLB0; -.
DR SMR; Q9JLB0; -.
DR BioGRID; 208035; 22.
DR IntAct; Q9JLB0; 8.
DR MINT; Q9JLB0; -.
DR STRING; 10090.ENSMUSP00000125880; -.
DR iPTMnet; Q9JLB0; -.
DR PhosphoSitePlus; Q9JLB0; -.
DR SwissPalm; Q9JLB0; -.
DR EPD; Q9JLB0; -.
DR jPOST; Q9JLB0; -.
DR MaxQB; Q9JLB0; -.
DR PaxDb; Q9JLB0; -.
DR PRIDE; Q9JLB0; -.
DR ProteomicsDB; 291490; -. [Q9JLB0-1]
DR ProteomicsDB; 291491; -. [Q9JLB0-2]
DR Antibodypedia; 12204; 252 antibodies from 35 providers.
DR DNASU; 56524; -.
DR Ensembl; ENSMUST00000036225; ENSMUSP00000038772; ENSMUSG00000038388. [Q9JLB0-1]
DR Ensembl; ENSMUST00000036236; ENSMUSP00000039314; ENSMUSG00000038388. [Q9JLB0-2]
DR Ensembl; ENSMUST00000166318; ENSMUSP00000125880; ENSMUSG00000038388. [Q9JLB0-1]
DR Ensembl; ENSMUST00000204545; ENSMUSP00000144737; ENSMUSG00000038388. [Q9JLB0-2]
DR GeneID; 56524; -.
DR KEGG; mmu:56524; -.
DR UCSC; uc009bwv.2; mouse. [Q9JLB0-1]
DR CTD; 51678; -.
DR MGI; MGI:1927340; Pals2.
DR VEuPathDB; HostDB:ENSMUSG00000038388; -.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000158500; -.
DR HOGENOM; CLU_001715_5_1_1; -.
DR InParanoid; Q9JLB0; -.
DR OMA; NPTTPHK; -.
DR PhylomeDB; Q9JLB0; -.
DR TreeFam; TF314263; -.
DR BioGRID-ORCS; 56524; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Mpp6; mouse.
DR PRO; PR:Q9JLB0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9JLB0; protein.
DR Bgee; ENSMUSG00000038388; Expressed in ureteric bud tip and 250 other tissues.
DR ExpressionAtlas; Q9JLB0; baseline and differential.
DR Genevisible; Q9JLB0; MM.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISS:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0004385; F:guanylate kinase activity; ISS:MGI.
DR CDD; cd12038; SH3_MPP6; 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; IPR035603; MPP6_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; 2.
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; 1.
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 Alternative splicing; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW SH3 domain.
FT CHAIN 1..553
FT /note="Protein PALS2"
FT /id="PRO_0000094585"
FT DOMAIN 1..48
FT /note="L27 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 49..107
FT /note="L27 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 129..208
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 228..297
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 351..538
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT MOD_RES 513
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZW5"
FT VAR_SEQ 217..230
FT /note="Missing (in isoform Alpha)"
FT /evidence="ECO:0000303|PubMed:10753959, ECO:0000303|Ref.2"
FT /id="VSP_003161"
FT CONFLICT 393..394
FT /note="DE -> EQ (in Ref. 2; AAD45009)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 62631 MW; 26F3BE2445ABEDC2 CRC64;
MQQVLENLTE LPSSTGAEEI DLIFLKGIME NPIVKSLAKA HERLEDSKLE AVSDNNLELV
NEILEDITPL ISVDENVAEL VGILKEPHFQ SLLEAHDIVA SKCYDSPPSS PEMNIPSLNN
QLPVDAIRIL GIHKKAGEPL GVTFRVENND LVIARILHGG MIDRQGLLHV GDIIKEVNGH
EVGNNPKELQ ELLKNISGSV TLKILPSYRD TITPQQSYVN MERHPAHVRQ VFVKCHFDYN
PFNDNLIPCK EAGLKFSKGE ILQIVNREDP NWWQASHVKE GGSAGLIPSQ FLEEKRKAFV
RRDWDNSGPF CGTISNKKKK KMMYLTTRNA EFDRHEIQIY EEVAKMPPFQ RKTLVLIGAQ
GVGRRSLKNR FIVLNPARFG TTVPFTSRKP REDEKDGQAY KFVSRSEMEA DIKAGKYLEH
GEYEGNLYGT KIDSILEVVQ TGRTCILDVN PQALKVLRTS EFMPYVVFIA APELETLRAM
HKAVVDAGIT TKLLTDSDLK KTVDESARIQ RAYNHYFDLI IVNDNLDKAF EKLQTAIEKL
RMEPQWVPIS WVY
