ID   GRIP1_MOUSE             Reviewed;        1127 AA.
AC   Q925T6; Q8BLQ3; Q8C0T3; Q925T5; Q925T7;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 173.
DE   RecName: Full=Glutamate receptor-interacting protein 1;
DE            Short=GRIP-1;
GN   Name=Grip1;
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 1; 2 AND 3), DEVELOPMENTAL STAGE,
RP   TISSUE SPECIFICITY, AND PALMITOYLATION OF ISOFORM 2.
RC   TISSUE=Brain;
RX   PubMed=11335060; DOI=10.1016/s0304-3940(01)01766-9;
RA   Yamazaki M., Fukaya M., Abe M., Ikeno K., Kakizaki T., Watanabe M.,
RA   Sakimura K.;
RT   "Differential palmitoylation of two mouse glutamate receptor interacting
RT   protein 1 forms with different N-terminal sequences.";
RL   Neurosci. Lett. 304:81-84(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   INTERACTION WITH EFNB1; EPHA7 AND EPHB2.
RX   PubMed=9883737; DOI=10.1016/s0896-6273(00)80663-7;
RA   Torres R., Firestein B.L., Dong H., Staudinger J., Olson E.N.,
RA   Huganir R.L., Bredt D.S., Gale N.W., Yancopoulos G.D.;
RT   "PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors
RT   and their ephrin ligands.";
RL   Neuron 21:1453-1463(1998).
RN   [4]
RP   INTERACTION WITH KIF5A; KIF5B AND KIF5C.
RX   PubMed=11986669; DOI=10.1038/nature743;
RA   Setou M., Seog D.-H., Tanaka Y., Kanai Y., Takei Y., Kawagishi M.,
RA   Hirokawa N.;
RT   "Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to
RT   dendrites.";
RL   Nature 417:83-87(2002).
RN   [5]
RP   INTERACTION WITH CSPG4 AND GRIA2, DOMAIN, AND TISSUE SPECIFICITY.
RX   PubMed=12458226; DOI=10.1074/jbc.m210010200;
RA   Stegmueller J., Werner H., Nave K.-A., Trotter J.;
RT   "The proteoglycan NG2 is complexed with alpha-amino-3-hydroxy-5-methyl-4-
RT   isoxazolepropionic acid (AMPA) receptors by the PDZ glutamate receptor
RT   interaction protein (GRIP) in glial progenitor cells. Implications for
RT   glial-neuronal signaling.";
RL   J. Biol. Chem. 278:3590-3598(2003).
RN   [6]
RP   INTERACTION WITH PLCD4.
RX   PubMed=16272139; DOI=10.1093/jb/mvi135;
RA   Irino Y., Ichinohe M., Nakamura Y., Nakahara M., Fukami K.;
RT   "Phospholipase Cdelta4 associates with glutamate receptor interacting
RT   protein 1 in testis.";
RL   J. Biochem. 138:451-456(2005).
RN   [7]
RP   INTERACTION WITH SLC30A9.
RX   PubMed=15988012; DOI=10.1128/mcb.25.14.5965-5972.2005;
RA   Chen Y.-H., Kim J.H., Stallcup M.R.;
RT   "GAC63, a GRIP1-dependent nuclear receptor coactivator.";
RL   Mol. Cell. Biol. 25:5965-5972(2005).
RN   [8]
RP   INTERACTION WITH ATAD1 AND GRIA2.
RX   PubMed=21496646; DOI=10.1016/j.cell.2011.03.016;
RA   Zhang J., Wang Y., Chi Z., Keuss M.J., Pai Y.M., Kang H.C., Shin J.H.,
RA   Bugayenko A., Wang H., Xiong Y., Pletnikov M.V., Mattson M.P., Dawson T.M.,
RA   Dawson V.L.;
RT   "The AAA+ ATPase Thorase regulates AMPA receptor-dependent synaptic
RT   plasticity and behavior.";
RL   Cell 145:284-299(2011).
RN   [9]
RP   STRUCTURE BY NMR OF 461-570.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the PDZ domain from mouse glutamate receptor
RT   interacting protein 1A-L (GRIP1) homolog.";
RL   Submitted (MAY-2004) to the PDB data bank.
CC   -!- FUNCTION: May play a role as a localized scaffold for the assembly of a
CC       multiprotein signaling complex and as mediator of the trafficking of
CC       its binding partners at specific subcellular location in neurons (By
CC       similarity). Through complex formation with NSG1, GRIA2 and STX12
CC       controls the intracellular fate of AMPAR and the endosomal sorting of
CC       the GRIA2 subunit toward recycling and membrane targeting (By
CC       similarity). {ECO:0000250, ECO:0000250|UniProtKB:P97879}.
CC   -!- SUBUNIT: Interacts with EFNB3, GRIA2, GRIA3, GRIPAP1/GRASP1, PPFIA1,
CC       PPFIA4, FRAS1, PTPRF, liprins-alpha and the C-terminal tail of PRLHR.
CC       Can form homomultimers or heteromultimers with GRIP2 (By similarity).
CC       Interacts with EFNB1, EPHA7, EPHB2, KIF5A, KIF5B and KIF5C. Forms a
CC       ternary complex with GRIA2 and CSPG4. Interacts with ATAD1 in an ATP-
CC       dependent manner. ATAD1-catalyzed ATP hydrolysis disrupts binding to
CC       ATAD1 and to GRIA2 and leads to AMPAR complex disassembly. Interacts
CC       with SLC30A9 and PLCD4. Interacts with BUD23 (By similarity). Forms a
CC       complex with NSG1, GRIA2 and STX12; controls the intracellular fate of
CC       AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling
CC       and membrane targeting. Interacts with NSG1 (By similarity).
CC       {ECO:0000250, ECO:0000250|UniProtKB:P97879}.
CC   -!- INTERACTION:
CC       Q925T6; Q8VHY0: Cspg4; NbExp=7; IntAct=EBI-537752, EBI-8327479;
CC       Q925T6; P54763: Ephb2; NbExp=2; IntAct=EBI-537752, EBI-537711;
CC       Q925T6; P23819: Gria2; NbExp=5; IntAct=EBI-537752, EBI-77538;
CC       Q925T6; Q3UZ39: Lrrfip1; NbExp=2; IntAct=EBI-537752, EBI-2270972;
CC       Q925T6; P48281: Vdr; NbExp=2; IntAct=EBI-537752, EBI-346797;
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Membrane; Lipid-anchor.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC       {ECO:0000250|UniProtKB:Q9Y3R0}. Perikaryon
CC       {ECO:0000250|UniProtKB:P97879}. Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:P97879}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P97879}. Endomembrane system
CC       {ECO:0000250|UniProtKB:P97879}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P97879}. Postsynaptic cell membrane
CC       {ECO:0000250|UniProtKB:P97879}. Postsynaptic density
CC       {ECO:0000250|UniProtKB:P97879}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9Y3R0}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P97879}. Note=Membrane-associated with vesicles,
CC       peri-Golgi complexes and endoplasmic reticulum. Enriched in
CC       postsynaptic plasma membrane and postsynaptic densities.
CC       {ECO:0000250|UniProtKB:P97879}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=GRIP1a-L;
CC         IsoId=Q925T6-1; Sequence=Displayed;
CC       Name=2; Synonyms=GRIP1b, GRIP1b-S;
CC         IsoId=Q925T6-2; Sequence=VSP_009744, VSP_009747, VSP_009750;
CC       Name=3; Synonyms=GRIP1a-S;
CC         IsoId=Q925T6-3; Sequence=VSP_009746, VSP_009747, VSP_009750;
CC       Name=4;
CC         IsoId=Q925T6-4; Sequence=VSP_009745, VSP_009748, VSP_009749,
CC                                  VSP_009750;
CC   -!- TISSUE SPECIFICITY: Expressed in brain. Isoform 2 is the major isoform
CC       in brain. Expressed in oligodendrocyte lineage cells.
CC       {ECO:0000269|PubMed:11335060, ECO:0000269|PubMed:12458226}.
CC   -!- DEVELOPMENTAL STAGE: Detected in early development between postnatal
CC       days 3 (P3) and P8 and decreased from P14 in forebrain and cerebellum.
CC       {ECO:0000269|PubMed:11335060}.
CC   -!- DOMAIN: PDZ 6 mediates interaction with the PDZ recognition motif of
CC       EFNB1 and EPHB2 and with the C-terminus of PPFIA1 and PPFIA4. PDZ 4 and
CC       PDZ 5 mediate interaction with the C-terminus of GRIA2 and GRIA3. PDZ
CC       4, PDZ 5 and PDZ 6 mediate homomultimers. PDZ 7 mediates interaction
CC       with PDZ domain of GRASP1. PDZ 6 mediates interaction with the C-
CC       terminal of liprins-alpha. PDZ 1, PDZ 2 and PDZ 3 mediate interaction
CC       with the PDZ-binding motif of FRAS1. PDZ 4 and PDZ 5 mediate
CC       interaction with PRLHR (By similarity). PDZ 7 domain binds CSPG4.
CC       {ECO:0000250, ECO:0000269|PubMed:12458226}.
CC   -!- PTM: Palmitoylation of isoform 2. {ECO:0000269|PubMed:11335060}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Major isoform. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 3]: May be due to exons 2, 10 and 11 skipping.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB051560; BAB46929.1; -; mRNA.
DR   EMBL; AB051561; BAB46930.1; -; mRNA.
DR   EMBL; AB051562; BAB46931.1; -; mRNA.
DR   EMBL; AK029905; BAC26668.1; -; mRNA.
DR   EMBL; AK043821; BAC31662.2; -; mRNA.
DR   CCDS; CCDS24202.1; -. [Q925T6-1]
DR   CCDS; CCDS36071.1; -. [Q925T6-2]
DR   CCDS; CCDS36072.1; -. [Q925T6-3]
DR   CCDS; CCDS70114.1; -. [Q925T6-4]
DR   RefSeq; NP_001264221.1; NM_001277292.1.
DR   RefSeq; NP_001264223.1; NM_001277294.1.
DR   RefSeq; NP_001264224.1; NM_001277295.1. [Q925T6-4]
DR   RefSeq; NP_083012.1; NM_028736.2. [Q925T6-1]
DR   RefSeq; NP_570961.1; NM_130891.2. [Q925T6-3]
DR   RefSeq; NP_597699.1; NM_133442.2. [Q925T6-2]
DR   PDB; 1V5Q; NMR; -; A=461-569.
DR   PDBsum; 1V5Q; -.
DR   AlphaFoldDB; Q925T6; -.
DR   SMR; Q925T6; -.
DR   BioGRID; 216454; 16.
DR   CORUM; Q925T6; -.
DR   IntAct; Q925T6; 17.
DR   MINT; Q925T6; -.
DR   STRING; 10090.ENSMUSP00000123234; -.
DR   GlyGen; Q925T6; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q925T6; -.
DR   PhosphoSitePlus; Q925T6; -.
DR   SwissPalm; Q925T6; -.
DR   MaxQB; Q925T6; -.
DR   PaxDb; 10090-ENSMUSP00000123234; -.
DR   ProteomicsDB; 269633; -. [Q925T6-1]
DR   ProteomicsDB; 269634; -. [Q925T6-2]
DR   ProteomicsDB; 269635; -. [Q925T6-3]
DR   ProteomicsDB; 269636; -. [Q925T6-4]
DR   Antibodypedia; 8598; 272 antibodies from 36 providers.
DR   DNASU; 74053; -.
DR   Ensembl; ENSMUST00000077871.14; ENSMUSP00000077033.7; ENSMUSG00000034813.20. [Q925T6-2]
DR   Ensembl; ENSMUST00000105261.9; ENSMUSP00000100896.3; ENSMUSG00000034813.20. [Q925T6-4]
DR   Ensembl; ENSMUST00000138410.8; ENSMUSP00000123234.2; ENSMUSG00000034813.20. [Q925T6-1]
DR   Ensembl; ENSMUST00000144825.8; ENSMUSP00000121670.2; ENSMUSG00000034813.20. [Q925T6-3]
DR   GeneID; 74053; -.
DR   KEGG; mmu:74053; -.
DR   UCSC; uc007heg.2; mouse. [Q925T6-2]
DR   UCSC; uc007hek.2; mouse. [Q925T6-1]
DR   UCSC; uc007hel.2; mouse. [Q925T6-3]
DR   UCSC; uc007hep.2; mouse. [Q925T6-4]
DR   AGR; MGI:1921303; -.
DR   CTD; 23426; -.
DR   MGI; MGI:1921303; Grip1.
DR   VEuPathDB; HostDB:ENSMUSG00000034813; -.
DR   eggNOG; KOG3528; Eukaryota.
DR   GeneTree; ENSGT00940000158692; -.
DR   HOGENOM; CLU_004313_0_0_1; -.
DR   InParanoid; Q925T6; -.
DR   OMA; QGGIAAX; -.
DR   OrthoDB; 4199121at2759; -.
DR   PhylomeDB; Q925T6; -.
DR   TreeFam; TF326909; -.
DR   Reactome; R-MMU-416993; Trafficking of GluR2-containing AMPA receptors.
DR   BioGRID-ORCS; 74053; 1 hit in 77 CRISPR screens.
DR   ChiTaRS; Grip1; mouse.
DR   EvolutionaryTrace; Q925T6; -.
DR   PRO; PR:Q925T6; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q925T6; Protein.
DR   Bgee; ENSMUSG00000034813; Expressed in rostral migratory stream and 192 other cell types or tissues.
DR   ExpressionAtlas; Q925T6; baseline and differential.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR   GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR   GO; GO:0044327; C:dendritic spine head; ISO:MGI.
DR   GO; GO:0044326; C:dendritic spine neck; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000145; C:exocyst; ISO:MGI.
DR   GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0005874; C:microtubule; ISO:MGI.
DR   GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0098794; C:postsynapse; ISO:MGI.
DR   GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR   GO; GO:0098793; C:presynapse; ISO:MGI.
DR   GO; GO:0048786; C:presynaptic active zone; ISO:MGI.
DR   GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR   GO; GO:1990635; C:proximal dendrite; ISO:MGI.
DR   GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR   GO; GO:0106033; C:spine synapse; ISO:MGI.
DR   GO; GO:0043083; C:synaptic cleft; ISO:MGI.
DR   GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR   GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR   GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR   GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR   GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; ISO:MGI.
DR   GO; GO:1904628; P:cellular response to phorbol 13-acetate 12-myristate; ISO:MGI.
DR   GO; GO:0140059; P:dendrite arborization; ISO:MGI.
DR   GO; GO:0007399; P:nervous system development; ISO:MGI.
DR   GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
DR   GO; GO:0150012; P:positive regulation of neuron projection arborization; ISO:MGI.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0150092; P:regulation of synaptic scaling; ISO:MGI.
DR   GO; GO:0099003; P:vesicle-mediated transport in synapse; IDA:SynGO.
DR   CDD; cd00992; PDZ_signaling; 7.
DR   Gene3D; 2.30.42.10; -; 7.
DR   InterPro; IPR043545; GRIP1/2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   PANTHER; PTHR46227:SF3; GLUTAMATE RECEPTOR-INTERACTING PROTEIN 1; 1.
DR   PANTHER; PTHR46227; GLUTAMATE RECEPTOR-INTERACTING PROTEIN GRIP; 1.
DR   Pfam; PF00595; PDZ; 6.
DR   Pfam; PF17820; PDZ_6; 1.
DR   SMART; SM00228; PDZ; 7.
DR   SUPFAM; SSF50156; PDZ domain-like; 7.
DR   PROSITE; PS50106; PDZ; 7.
DR   Genevisible; Q925T6; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW   Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; Lipoprotein;
KW   Membrane; Palmitate; Phosphoprotein; Postsynaptic cell membrane;
KW   Reference proteome; Repeat; Synapse.
FT   CHAIN           1..1127
FT                   /note="Glutamate receptor-interacting protein 1"
FT                   /id="PRO_0000083850"
FT   DOMAIN          53..136
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          150..238
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          252..336
FT                   /note="PDZ 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          471..560
FT                   /note="PDZ 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          572..657
FT                   /note="PDZ 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          672..754
FT                   /note="PDZ 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          1003..1085
FT                   /note="PDZ 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          752..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          840..865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          942..980
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1108..1127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        947..977
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97879"
FT   VAR_SEQ         1..415
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_009745"
FT   VAR_SEQ         1..45
FT                   /note="MIAVSFKCRCQILRRLTKDESPYTKSASQTKPPDGALAVRRQSIP -> MPG
FT                   WKKNIPICLQAEEQER (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11335060"
FT                   /id="VSP_009744"
FT   VAR_SEQ         19..45
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11335060"
FT                   /id="VSP_009746"
FT   VAR_SEQ         348..400
FT                   /note="VKIQRSDRQHPWDAWASNQCGVHTNHHHNTYHPDHCRVPALTFPKALPPNSP
FT                   P -> A (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11335060"
FT                   /id="VSP_009747"
FT   VAR_SEQ         416..451
FT                   /note="LSSLNMGTLPRSLYSTSPRGTMMRRRLKKKDFKSSL -> MTAKRAERKEMK
FT                   RPNSFHLPFRPSLRKGQKKNAAHV (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_009748"
FT   VAR_SEQ         756..820
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_009749"
FT   VAR_SEQ         911..925
FT                   /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11335060,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_009750"
FT   CONFLICT        1011
FT                   /note="G -> C (in Ref. 2; BAC26668)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1044
FT                   /note="L -> M (in Ref. 2; BAC31662)"
FT                   /evidence="ECO:0000305"
FT   STRAND          467..474
FT                   /evidence="ECO:0007829|PDB:1V5Q"
FT   STRAND          478..482
FT                   /evidence="ECO:0007829|PDB:1V5Q"
FT   STRAND          484..487
FT                   /evidence="ECO:0007829|PDB:1V5Q"
FT   STRAND          493..495
FT                   /evidence="ECO:0007829|PDB:1V5Q"
FT   STRAND          501..505
FT                   /evidence="ECO:0007829|PDB:1V5Q"
FT   HELIX           510..513
FT                   /evidence="ECO:0007829|PDB:1V5Q"
FT   STRAND          523..526
FT                   /evidence="ECO:0007829|PDB:1V5Q"
FT   STRAND          529..534
FT                   /evidence="ECO:0007829|PDB:1V5Q"
FT   HELIX           536..546
FT                   /evidence="ECO:0007829|PDB:1V5Q"
FT   TURN            547..550
FT                   /evidence="ECO:0007829|PDB:1V5Q"
FT   STRAND          552..559
FT                   /evidence="ECO:0007829|PDB:1V5Q"
FT   LIPID           Q925T6-2:11
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1127 AA;  122058 MW;  556DFCCE2CE6248A CRC64;
     MIAVSFKCRC QILRRLTKDE SPYTKSASQT KPPDGALAVR RQSIPEEFKG STVVELMKKE
     GTTLGLTVSG GIDKDGKPRV SNLRQGGIAA RSDQLDVGDY IKAVNGINLA KFRHDEIISL
     LKNVGERVVL EVEYELPPVS VQGSSVMFRT VEVTLHKEGN TFGFVIRGGA HDDRNKSRPV
     VITCVRPGGP ADREGTIKPG DRLLSVDGIR LLGTTHAEAM SILKQCGQEA TLLIEYDVSV
     MDSVATASGP LLVEVAKTPG ASLGVALTTS VCCNKQVIVI DKIKSASIAD RCGALHVGDH
     ILSIDGTSME YCTLAEATQF LANTTDQVKL EILPHHQTRL ALKGPDHVKI QRSDRQHPWD
     AWASNQCGVH TNHHHNTYHP DHCRVPALTF PKALPPNSPP AMVPSSSPTS MSAYSLSSLN
     MGTLPRSLYS TSPRGTMMRR RLKKKDFKSS LSLASSTVGL AGQVVHTETT EVVLTADPVT
     GFGIQLQGSV FATETLSSPP LISYIEADSP AERCGVLQIG DRVMAINGIP TEDSTFEEAN
     QLLRDSSITS KVTLEIEFDV AESVIPSSGT FHVKLPKKHS VELGITISSP SSRKPGDPLV
     ISDIKKGSVA HRTGTLELGD KLLAIDNIRL DNCSMEDAVQ ILQQCEDLVK LKIRKDEDNS
     DEQESSGAII YTVELKRYGG PLGITISGTE EPFDPIIISS LTKGGLAERT GAIHIGDRIL
     AINSSSLKGK PLSEAIHLLQ MAGETVTLKI KKQTDAQSAS SPKKFPIPGH SGDLGDGEED
     PSPIQKPGKL SDAYPSTVPS VDSAVDSWDG SGIDASYGSQ GSTFQTSGYN YNTYDWRSPK
     QRTSLSPVPK PRSQTYPDVG LSNEDWDRST ASGFVGASDS ADAEQEENFW SQALEDLETC
     GQSGILRELE EKADRRVSLR NMTLLATIMS GSTMSLNHEA PMARSQLGRQ ASFQERSSSR
     PHYSQTTRSN TLPSDVGRKS VTLRKMKQEI KEIMSPTPVE LHKVTLYKDS GMEDFGFSVA
     DGLLEKGVYV KNIRPAGPGD VGGLKPYDRL LQVNHVRTRD FDCCLVVPLI AESGNKLDLV
     ISRNPLASQK SIEQPALPSD WSEQNSAFFQ QPSHGGNLET REPTNTL
//