LOCUS       NP_001181960             429 aa            linear   ROD 04-JUN-2024
DEFINITION  phosphoprotein associated with glycosphingolipid-enriched
            microdomains 1 [Mus musculus].
ACCESSION   NP_001181960
VERSION     NP_001181960.1
DBSOURCE    REFSEQ: accession NM_001195031.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Lucas,R.M., Liu,L., Curson,J.E.B., Koh,Y.W.H., Tuladhar,N.,
            Condon,N.D., Das Gupta,K., Burgener,S.S., Schroder,K., Ingley,E.,
            Sweet,M.J., Stow,J.L. and Luo,L.
  TITLE     SCIMP is a spatiotemporal transmembrane scaffold for Erk1/2 to
            direct pro-inflammatory signaling in TLR-activated macrophages
  JOURNAL   Cell Rep 36 (10), 109662 (2021)
   PUBMED   34496234
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Tsuboi,Y., Oyama,M., Kozuka-Hata,H., Ito,A., Matsubara,D. and
            Murakami,Y.
  TITLE     CADM1 suppresses c-Src activation by binding with Cbp on membrane
            lipid rafts and intervenes colon carcinogenesis
  JOURNAL   Biochem Biophys Res Commun 529 (3), 854-860 (2020)
   PUBMED   32616310
  REMARK    GeneRIF: CADM1 suppresses c-Src activation by binding with Cbp on
            membrane lipid rafts and intervenes colon carcinogenesis.
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Ullah,M.A., Vicente,C.T., Collinson,N., Curren,B., Sikder,M.A.A.,
            Sebina,I., Simpson,J., Varelias,A., Lindquist,J.A., Ferreira,M.A.R.
            and Phipps,S.
  TITLE     PAG1 limits allergen-induced type 2 inflammation in the murine lung
  JOURNAL   Allergy 75 (2), 336-345 (2020)
   PUBMED   31321783
  REMARK    GeneRIF: PAG1 limits allergen-induced type 2 inflammation in the
            murine lung.
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Plani-Lam,J.H., Slavova-Azmanova,N.S., Kucera,N., Louw,A.,
            Satiaputra,J., Singer,P., Lam,K.P., Hibbs,M.L. and Ingley,E.
  TITLE     Csk-binding protein controls red blood cell development via
            regulation of Lyn tyrosine kinase activity
  JOURNAL   Exp Hematol 46, 70-82 (2017)
   PUBMED   27751872
  REMARK    GeneRIF: our findings illustrate that Cbp is an important regulator
            of Csk recruitment to the SFK Lyn in Eporesponsive erythroid cells.
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Davidson,D., Zhong,M.C., Pandolfi,P.P., Bolland,S., Xavier,R.J.,
            Seed,B., Li,X., Gu,H. and Veillette,A.
  TITLE     The Csk-Associated Adaptor PAG Inhibits Effector T Cell Activation
            in Cooperation with Phosphatase PTPN22 and Dok Adaptors
  JOURNAL   Cell Rep 17 (10), 2776-2788 (2016)
   PUBMED   27926878
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Van Laethem,F., Liang,X., Andris,F., Urbain,J., Vandenbranden,M.,
            Ruysschaert,J.M., Resh,M.D., Stulnig,T.M. and Leo,O.
  TITLE     Glucocorticoids alter the lipid and protein composition of membrane
            rafts of a murine T cell hybridoma
  JOURNAL   J Immunol 170 (6), 2932-2939 (2003)
   PUBMED   12626544
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Davidson,D., Bakinowski,M., Thomas,M.L., Horejsi,V. and
            Veillette,A.
  TITLE     Phosphorylation-dependent regulation of T-cell activation by
            PAG/Cbp, a lipid raft-associated transmembrane adaptor
  JOURNAL   Mol Cell Biol 23 (6), 2017-2028 (2003)
   PUBMED   12612075
  REMARK    GeneRIF: PAG is a bona fide negative regulator of T-cell activation
            as a result of its capacity to recruit Csk.
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Yasuda,K., Nagafuku,M., Shima,T., Okada,M., Yagi,T., Yamada,T.,
            Minaki,Y., Kato,A., Tani-Ichi,S., Hamaoka,T. and Kosugi,A.
  TITLE     Cutting edge: Fyn is essential for tyrosine phosphorylation of
            Csk-binding protein/phosphoprotein associated with
            glycolipid-enriched microdomains in lipid rafts in resting T cells
  JOURNAL   J Immunol 169 (6), 2813-2817 (2002)
   PUBMED   12218089
REFERENCE   9  (residues 1 to 429)
  AUTHORS   Itoh,K., Sakakibara,M., Yamasaki,S., Takeuchi,A., Arase,H.,
            Miyazaki,M., Nakajima,N., Okada,M. and Saito,T.
  TITLE     Cutting edge: negative regulation of immune synapse formation by
            anchoring lipid raft to cytoskeleton through Cbp-EBP50-ERM assembly
  JOURNAL   J Immunol 168 (2), 541-544 (2002)
   PUBMED   11777944
REFERENCE   10 (residues 1 to 429)
  AUTHORS   Brdicka,T., Pavlistova,D., Leo,A., Bruyns,E., Korinek,V.,
            Angelisova,P., Scherer,J., Shevchenko,A., Hilgert,I., Cerny,J.,
            Drbal,K., Kuramitsu,Y., Kornacker,B., Horejsi,V. and Schraven,B.
  TITLE     Phosphoprotein associated with glycosphingolipid-enriched
            microdomains (PAG), a novel ubiquitously expressed transmembrane
            adaptor protein, binds the protein tyrosine kinase csk and is
            involved in regulation of T cell activation
  JOURNAL   J Exp Med 191 (9), 1591-1604 (2000)
   PUBMED   10790433
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC156996.7, AK040230.1 and AC129945.10.
            
            Transcript Variant: This variant (A) represents the longer
            transcript. Both variants A and B encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK156000.1, AK172106.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="3"
                     /map="3 2.47 cM"
     Protein         1..429
                     /product="phosphoprotein associated with
                     glycosphingolipid-enriched microdomains 1"
                     /note="phosphoprotein transmembrane adaptor 1;
                     phosphoprotein-associated with GEMs; Csk-binding protein;
                     transmembrane phosphoprotein Cbp"
                     /calculated_mol_wt=46419
     Region          1..429
                     /region_name="PAG"
                     /note="Phosphoprotein associated with
                     glycosphingolipid-enriched; pfam15347"
                     /db_xref="CDD:434654"
     Site            18..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Region          46..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JM80; propagated from
                     UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JM80; propagated from
                     UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by LYN.
                     /evidence=ECO:0000250|UniProtKB:Q9JM80; propagated from
                     UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Region          113..134
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19144319; propagated from
                     UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19144319; propagated from
                     UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:17947660,
                     ECO:0007744|PubMed:19144319; propagated from
                     UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NWQ8; propagated from
                     UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Region          263..350
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Region          314..317
                     /region_name="Interaction with CSK"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by FYN.
                     /evidence=ECO:0000269|PubMed:12218089,
                     ECO:0000269|PubMed:12612075, ECO:0000269|PubMed:14967142;
                     propagated from UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9NWQ8; propagated from
                     UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Region          364..429
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19144319,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9NWQ8; propagated from
                     UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9NWQ8; propagated from
                     UniProtKB/Swiss-Prot (Q3U1F9.2)"
     Region          427..429
                     /region_name="Interaction with NHERF1.
                     /evidence=ECO:0000269|PubMed:11777944"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3U1F9.2)"
     CDS             1..429
                     /gene="Pag1"
                     /gene_synonym="Cbp; F730007C19Rik; Pag"
                     /coded_by="NM_001195031.1:679..1968"
                     /db_xref="CCDS:CCDS17235.1"
                     /db_xref="GeneID:94212"
                     /db_xref="MGI:MGI:2443160"
ORIGIN      
        1 mgpagsvlss gqmqmqmvlw gslaavamff litflvllcs tcdrekkprq hsgdhenlmn
       61 vpsdkdmfsh satslttdal asseqngvlt ngdilsedst ltcmqhyeev qtsasdllds
      121 qdstgkakch qsrelpripp enavdeilta raadtelgpg vegpyevlkd sssqenmved
      181 clyetvkeik evadkgqggk skstsalkel qgapmegkad faeyasvdrn kkcrhsanae
      241 silgtcsdld eespppvpvk lldenanlpq egggqaeeqa aegtgghskr fsslsyksre
      301 edptlteeei samyssvnkp gqsahkpgpc mkgpesachs mkglpqrsss scndlyatvk
      361 dfektpnsis tlpparrpse epepdyeaiq tlnredekvp letnghhvpk esdyesigdl
      421 qqcrdvtrl
//
