LOCUS       NP_001152793            1203 aa            linear   ROD 01-JUN-2024
DEFINITION  delphilin isoform 1 [Mus musculus].
ACCESSION   NP_001152793
VERSION     NP_001152793.1
DBSOURCE    REFSEQ: accession NM_001159321.2
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 1203)
  AUTHORS   Boyle,M.P., Bernard,A., Thompson,C.L., Ng,L., Boe,A., Mortrud,M.,
            Hawrylycz,M.J., Jones,A.R., Hevner,R.F. and Lein,E.S.
  TITLE     Cell-type-specific consequences of Reelin deficiency in the mouse
            neocortex, hippocampus, and amygdala
  JOURNAL   J Comp Neurol 519 (11), 2061-2089 (2011)
   PUBMED   21491433
REFERENCE   2  (residues 1 to 1203)
  AUTHORS   Takeuchi,T., Ohtsuki,G., Yoshida,T., Fukaya,M., Wainai,T.,
            Yamashita,M., Yamazaki,Y., Mori,H., Sakimura,K., Kawamoto,S.,
            Watanabe,M., Hirano,T. and Mishina,M.
  TITLE     Enhancement of both long-term depression induction and optokinetic
            response adaptation in mice lacking delphilin
  JOURNAL   PLoS One 3 (5), e2297 (2008)
   PUBMED   18509461
  REMARK    GeneRIF: findings are compatible with the idea that LTD induction
            at PF-PC synapses is a crucial rate-limiting step in optokinetic
            resonse gain-increase adaptation, a simple form of motor learning
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1203)
  AUTHORS   Matsuda,K., Matsuda,S., Gladding,C.M. and Yuzaki,M.
  TITLE     Characterization of the delta2 glutamate receptor-binding protein
            delphilin: Splicing variants with differential palmitoylation and
            an additional PDZ domain
  JOURNAL   J Biol Chem 281 (35), 25577-25587 (2006)
   PUBMED   16835239
REFERENCE   4  (residues 1 to 1203)
  AUTHORS   Yamashita,T., Miyagi,Y., Ono,M., Ito,H., Watanabe,K., Sonoda,T.,
            Tsuzuki,K., Ozawa,S., Aoki,I., Okuda,K., Mishina,M. and Kawamoto,S.
  TITLE     Identification and characterization of a novel Delphilin variant
            with an alternative N-terminus
  JOURNAL   Brain Res Mol Brain Res 141 (1), 83-94 (2005)
   PUBMED   16168524
  REMARK    GeneRIF: Results show that the Delphilin protein exhibits diversity
            at its N-terminus by variable usage of the first several exons.
REFERENCE   5  (residues 1 to 1203)
  AUTHORS   Selimi,F., Lohof,A.M., Heitz,S., Lalouette,A., Jarvis,C.I.,
            Bailly,Y. and Mariani,J.
  TITLE     Lurcher GRID2-induced death and depolarization can be dissociated
            in cerebellar Purkinje cells
  JOURNAL   Neuron 37 (5), 813-819 (2003)
   PUBMED   12628171
  REMARK    GeneRIF: Absence of GRID2 receptors in heteroallelic mutants
            induces an early and massive Purkinje cell death that is correlated
            with early signs of autophagy and is independent of depolarization.
REFERENCE   6  (residues 1 to 1203)
  AUTHORS   Yue,Z., Horton,A., Bravin,M., DeJager,P.L., Selimi,F. and Heintz,N.
  TITLE     A novel protein complex linking the delta 2 glutamate receptor and
            autophagy: implications for neurodegeneration in lurcher mice
  JOURNAL   Neuron 35 (5), 921-933 (2002)
   PUBMED   12372286
  REMARK    GeneRIF: A direct link exists between GluR2delta receptor and
            stimulation of the autophagic pathway in dying Purkinje cells of
            lurcher mice.
REFERENCE   7  (residues 1 to 1203)
  AUTHORS   Miyagi,Y., Yamashita,T., Fukaya,M., Sonoda,T., Okuno,T., Yamada,K.,
            Watanabe,M., Nagashima,Y., Aoki,I., Okuda,K., Mishina,M. and
            Kawamoto,S.
  TITLE     Delphilin: a novel PDZ and formin homology domain-containing
            protein that synaptically colocalizes and interacts with glutamate
            receptor delta 2 subunit
  JOURNAL   J Neurosci 22 (3), 803-814 (2002)
   PUBMED   11826110
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC118226.7 and DQ193535.1.
            
            Transcript Variant: This variant (1) encodes the larger isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ193535.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164136, SAMN01164137
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1203
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="5"
                     /map="5 82.1 cM"
     Protein         1..1203
                     /product="delphilin isoform 1"
                     /note="L-delphilin; glutamate receptor, ionotropic, delta
                     2-interacting protein 1; GluR-delta2 philic-protein"
                     /calculated_mol_wt=131890
     Region          2..77
                     /region_name="PDZ1_L-delphilin-like"
                     /note="PDZ domain 1 of delphilin (L-delphilin isoform),
                     and related domains; cd06743"
                     /db_xref="CDD:467225"
     Site            order(11..17,25,28,57,61,64..65)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467225"
     Region          122..201
                     /region_name="HN_L-delphilin-R1_like"
                     /note="first harmonin_N_like domain (repeat 1) of
                     L-delphilin, and related domains; cd07354"
                     /db_xref="CDD:259820"
     Site            order(123,126,130,145,148,151..152,155)
                     /site_type="other"
                     /note="putative protein binding site [polypeptide
                     binding]"
                     /db_xref="CDD:259820"
     Region          215..270
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0QWG9.1)"
     Region          269..342
                     /region_name="PDZ2_L-delphilin-like"
                     /note="PDZ domain 2 of delphilin (L-delphilin isoform),
                     and related domains; cd06744"
                     /db_xref="CDD:467226"
     Site            order(277..283,291,294,323,327,330..331)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467226"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q0QWG9.1)"
     Region          378..457
                     /region_name="HN_L-delphilin-R2_like"
                     /note="second harmonin_N_like domain (repeat 2) of
                     L-delphilin, and related domains; cd07355"
                     /db_xref="CDD:259821"
     Site            order(379,382,386,399,402,405..406,409)
                     /site_type="other"
                     /note="putative protein binding site [polypeptide
                     binding]"
                     /db_xref="CDD:259821"
     Region          466..541
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0QWG9.1)"
     Region          563..586
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0QWG9.1)"
     Site            572
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q0QWG9.1)"
     Region          611..656
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0QWG9.1)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q0QWG9.1)"
     Site            644
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q0QWG9.1)"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q0QWG9.1)"
     Region          710..821
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0QWG9.1)"
     Region          812..1180
                     /region_name="FH2"
                     /note="Formin Homology 2 Domain; pfam02181"
                     /db_xref="CDD:396655"
     CDS             1..1203
                     /gene="Grid2ip"
                     /coded_by="NM_001159321.2:222..3833"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS51689.1"
                     /db_xref="GeneID:170935"
                     /db_xref="MGI:MGI:2176213"
ORIGIN      
        1 mpatnqgwpe dfgfqlggsg pcfvievaeg ssahagglrp gdqilevegl avgglsreri
       61 vrlarrcprv ppslgvlpgp eggptaltaa wltrrfgrsl plsrellrla ggprpdavhr
      121 errrkaqefs cqvddilgdr ltakeqvfta lkqfaaeqrv delvwtltlv lpseaqgpvl
      181 dnlrifipkk hrarfdevvs qgllgklcra rraqgaqrlr rsrseerper llvstrasaa
      241 prrpdepppr katsllggrt gpggprrtvr vykgnksfgf tlrghgpvwi esvlpgspae
      301 naslksgdri lflngldmrn cshdkvvsml qgsgamptlv veegpvpfas dsdsldsptr
      361 asaltslqwv adilpssirv qgrtfsqqld hlltpperyg vcralerffq hrnidtlivd
      421 vypvldtpak qvlwqflyql ltyeeqelcq ekiacflgyt amtepessld lepestpept
      481 pepqprsslr assmcrrslr sqgletslsc gpgdcpempl plipgerqag dgtslpetpn
      541 pkmmsavyae lesrlnssfk gkigtmsksr asppvpslvg tsgprtlsgv swpsdrllps
      601 pcydplcsgg laspsssesh pyasldssra pspqpglgsi hadsppspdp irppsrrklf
      661 afsrpvrsrd tdrfldalse qlgprlsivd dfltpendye emsfhddqgs fvtnerssas
      721 ecvssseegs sltyssisdh ipppplsppp ppplpfhdpk pssrtsdgpr gppqsltkpl
      781 tqinhpvppp pppplpppvp cappmlsrgv ghrrsetshm svkrlrweqv ensegtiwgq
      841 lgedsdydkl sdmvkyldle lhfgtqkppk pvpgpepfrk kevveilshk kayntsilla
      901 hlkltpgelr qvlmsmeprr lepahlaqll lfapdadeeq ryqafreapg rlsepdqfvl
      961 qmlsvpeykt rlrslhfqat lqekteeirg sleclrqasl elknsrklak ilefvlamgn
     1021 ylndgqpktn kttgfkinfl telnstktvd gkstflhila kslsqhfpel lgfaqdlptv
     1081 plaakvnqra ltgdladlhd tvseiqvacq smapssedrf avvmasflet aqpalraldg
     1141 lqreameelg kalaffgeds kattseaffg ifsefmskfe ralsdlqagd gprssgmvsp
     1201 law
//
