GRIP1_MOUSE
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 03-AUG-2022, entry version 165.
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}.
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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; 14.
DR MINT; Q925T6; -.
DR STRING; 10090.ENSMUSP00000123234; -.
DR iPTMnet; Q925T6; -.
DR PhosphoSitePlus; Q925T6; -.
DR SwissPalm; Q925T6; -.
DR MaxQB; Q925T6; -.
DR PaxDb; Q925T6; -.
DR PRIDE; Q925T6; -.
DR ProteomicsDB; 269633; -. [Q925T6-1]
DR ProteomicsDB; 269634; -. [Q925T6-2]
DR ProteomicsDB; 269635; -. [Q925T6-3]
DR ProteomicsDB; 269636; -. [Q925T6-4]
DR Antibodypedia; 8598; 242 antibodies from 36 providers.
DR DNASU; 74053; -.
DR Ensembl; ENSMUST00000077871; ENSMUSP00000077033; ENSMUSG00000034813. [Q925T6-2]
DR Ensembl; ENSMUST00000105261; ENSMUSP00000100896; ENSMUSG00000034813. [Q925T6-4]
DR Ensembl; ENSMUST00000138410; ENSMUSP00000123234; ENSMUSG00000034813. [Q925T6-1]
DR Ensembl; ENSMUST00000144825; ENSMUSP00000121670; ENSMUSG00000034813. [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 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; QLYPGYE; -.
DR OrthoDB; 65191at2759; -.
DR PhylomeDB; Q925T6; -.
DR TreeFam; TF326909; -.
DR Reactome; R-MMU-416993; Trafficking of GluR2-containing AMPA receptors.
DR BioGRID-ORCS; 74053; 1 hit in 72 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 190 other tissues.
DR ExpressionAtlas; Q925T6; baseline and differential.
DR Genevisible; Q925T6; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0045121; C:membrane raft; IDA: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: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; IEA:UniProtKB-SubCell.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IEA:InterPro.
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:0150012; P:positive regulation of neuron projection arborization; ISO:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0015031; P:protein transport; ISO:MGI.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; IDA:SynGO.
DR Gene3D; 2.30.42.10; -; 7.
DR InterPro; IPR030026; GRIP1.
DR InterPro; IPR043545; GRIP1/2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR46227; PTHR46227; 1.
DR PANTHER; PTHR46227:SF3; PTHR46227:SF3; 1.
DR Pfam; PF00595; PDZ; 6.
DR Pfam; PF17820; PDZ_6; 1.
DR SMART; SM00228; PDZ; 7.
DR SUPFAM; SSF50156; SSF50156; 7.
DR PROSITE; PS50106; PDZ; 7.
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
