HOME1_MOUSE
ID HOME1_MOUSE Reviewed; 366 AA.
AC Q9Z2Y3; Q8K3E1; Q8K4M8; Q9Z0E9; Q9Z216;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Homer protein homolog 1 {ECO:0000305};
DE Short=Homer-1;
DE AltName: Full=VASP/Ena-related gene up-regulated during seizure and LTP 1;
DE Short=Vesl-1 {ECO:0000303|Ref.4};
GN Name=Homer1 {ECO:0000312|MGI:MGI:1347345}; Synonyms=Vesl1;
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 3 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Forebrain;
RX PubMed=9808458; DOI=10.1016/s0896-6273(00)80588-7;
RA Xiao B., Tu J.C., Petralia R.S., Yuan J.P., Doan A., Breder C.D.,
RA Ruggiero A., Lanahan A.A., Wenthold R.J., Worley P.F.;
RT "Homer regulates the association of group 1 metabotropic glutamate
RT receptors with multivalent complexes of homer-related, synaptic proteins.";
RL Neuron 21:707-716(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=BALB/cJ; TISSUE=Heart;
RX PubMed=12176012; DOI=10.1016/s0006-291x(02)00899-9;
RA Saito H., Kimura M., Inanobe A., Ohe T., Kurachi Y.;
RT "An N-terminal sequence specific for a novel Homer1 isoform controls
RT trafficking of group I metabotropic glutamate receptor in mammalian
RT cells.";
RL Biochem. Biophys. Res. Commun. 296:523-529(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5).
RC STRAIN=C57BL/6N; TISSUE=Brain cortex;
RA Inokuchi K., Hayashi F.;
RT "Mouse Vesl family of EVH-protein that interacts with group I mGluRs.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC STRAIN=129/SvJ; TISSUE=Hippocampus;
RA Hayashi F., Hirai K., Inokuchi K.;
RT "Genomic structure of mouse vesl-1 gene.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH GRM1; GRM5; DYN3 AND ITPR1.
RX PubMed=9808459; DOI=10.1016/s0896-6273(00)80589-9;
RA Tu J.C., Xiao B., Yuan J.P., Lanahan A.A., Leoffert K., Li M., Linden D.J.,
RA Worley P.F.;
RT "Homer binds a novel proline-rich motif and links group 1 metabotropic
RT glutamate receptors with IP3 receptors.";
RL Neuron 21:717-726(1998).
RN [6]
RP REVIEW.
RX PubMed=10851183; DOI=10.1016/s0959-4388(00)00087-8;
RA Xiao B., Tu J.C., Worley P.F.;
RT "Homer: a link between neural activity and glutamate receptor function.";
RL Curr. Opin. Neurobiol. 10:370-374(2000).
RN [7]
RP TISSUE SPECIFICITY, AND INTERACTION WITH ITPR1.
RX PubMed=12379179; DOI=10.1016/s0143416002001549;
RA Salanova M., Priori G., Barone V., Intravaia E., Flucher B., Ciruela F.,
RA McIlhinney R.A.J., Parys J.B., Mikoshiba K., Sorrentino V.;
RT "Homer proteins and InsP(3) receptors co-localise in the longitudinal
RT sarcoplasmic reticulum of skeletal muscle fibres.";
RL Cell Calcium 32:193-200(2002).
RN [8]
RP INTERACTION WITH IFT57.
RX PubMed=17107665; DOI=10.1016/j.bbrc.2006.10.167;
RA Sakamoto K., Yoshida S., Ikegami K., Minakami R., Kato A., Udo H.,
RA Sugiyama H.;
RT "Homer1c interacts with Hippi and protects striatal neurons from
RT apoptosis.";
RL Biochem. Biophys. Res. Commun. 352:1-5(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [10]
RP INTERACTION WITH SHANK3.
RX PubMed=21558424; DOI=10.1093/hmg/ddr212;
RA Wang X., McCoy P.A., Rodriguiz R.M., Pan Y., Je H.S., Roberts A.C.,
RA Kim C.J., Berrios J., Colvin J.S., Bousquet-Moore D., Lorenzo I., Wu G.,
RA Weinberg R.J., Ehlers M.D., Philpot B.D., Beaudet A.L., Wetsel W.C.,
RA Jiang Y.H.;
RT "Synaptic dysfunction and abnormal behaviors in mice lacking major isoforms
RT of Shank3.";
RL Hum. Mol. Genet. 20:3093-3108(2011).
RN [11]
RP TISSUE SPECIFICITY, INTERACTION WITH SHANK3, AND SUBCELLULAR LOCATION.
RX PubMed=24153177; DOI=10.1038/nature12630;
RA Han K., Holder J.L. Jr., Schaaf C.P., Lu H., Chen H., Kang H., Tang J.,
RA Wu Z., Hao S., Cheung S.W., Yu P., Sun H., Breman A.M., Patel A., Lu H.C.,
RA Zoghbi H.Y.;
RT "SHANK3 overexpression causes manic-like behaviour with unique
RT pharmacogenetic properties.";
RL Nature 503:72-77(2013).
RN [12]
RP INTERACTION WITH SRGAP2.
RX PubMed=27373832; DOI=10.1016/j.neuron.2016.06.013;
RA Fossati M., Pizzarelli R., Schmidt E.R., Kupferman J.V., Stroebel D.,
RA Polleux F., Charrier C.;
RT "SRGAP2 and its human-specific paralog co-regulate the development of
RT excitatory and inhibitory synapses.";
RL Neuron 91:356-369(2016).
CC -!- FUNCTION: Postsynaptic density scaffolding protein. Binds and cross-
CC links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2,
CC SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-
CC associated ITPR1 receptors, it aids the coupling of surface receptors
CC to intracellular calcium release. May also couple GRM1 to PI3 kinase
CC through its interaction with AGAP2. Isoform 1 regulates the trafficking
CC and surface expression of GRM5. Differentially regulates the functions
CC of the calcium activated channel ryanodine receptors RYR1 and RYR2.
CC Isoform 1 decreases the activity of RYR2, and increases the activity of
CC RYR1, whereas isoform 5 counteracts the effects by competing for
CC binding sites. Isoform 3 regulates the trafficking and surface
CC expression of GRM5. Isoform 5 acts as a natural dominant negative, in
CC dynamic competition with constitutively expressed isoform 1, isoform 2
CC and isoform 3 to regulate synaptic metabotropic glutamate function.
CC Isoform 5, may be involved in the structural changes that occur at
CC synapses during long-lasting neuronal plasticity and development (By
CC similarity). Forms a high-order complex with SHANK1, which in turn is
CC necessary for the structural and functional integrity of dendritic
CC spines (By similarity). Negatively regulates T cell activation by
CC inhibiting the calcineurin-NFAT pathway. Acts by competing with
CC calcineurin/PPP3CA for NFAT protein binding, hence preventing NFAT
CC activation by PPP3CA (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q86YM7, ECO:0000250|UniProtKB:Q9Z214}.
CC -!- SUBUNIT: Tetramer; this tetrameric structure is critical for forming
CC the high-order complex with SHANK1, which in turn is necessary for the
CC structural and functional integrity of dendritic spines (By
CC similarity). Isoform 1, isoform 2 and isoform 3 encode a coiled-coil
CC structure that mediates homo- and heteromultimerization (By
CC similarity). Interacts with GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2 and
CC SHANK3 (PubMed:12379179, PubMed:21558424, PubMed:24153177). Interacts
CC with IFT57 and OPHN1 (PubMed:17107665). Interacts with SHANK1; forms
CC high-order polymerized complex with a mesh-like network structure, at
CC least composed of SHANK1, HOMER1 and DLGAP1; the complex formation is
CC SHANK1 multimerization dependent (By similarity). Interacts with NFATC4
CC (By similarity). Interacts with DAGLA (via PPXXF motif); this
CC interaction is required for the cell membrane localization of DAGLA (By
CC similarity). Interacts with SRGAP2 (PubMed:27373832).
CC {ECO:0000250|UniProtKB:Q86YM7, ECO:0000250|UniProtKB:Q9Z214,
CC ECO:0000269|PubMed:12379179, ECO:0000269|PubMed:17107665,
CC ECO:0000269|PubMed:21558424, ECO:0000269|PubMed:24153177,
CC ECO:0000269|PubMed:27373832, ECO:0000269|PubMed:9808459}.
CC -!- INTERACTION:
CC Q9Z2Y3; Q9D415: Dlgap1; NbExp=4; IntAct=EBI-396980, EBI-400152;
CC Q9Z2Y3; Q4ACU6: Shank3; NbExp=8; IntAct=EBI-396980, EBI-771450;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24153177}.
CC Postsynaptic density {ECO:0000269|PubMed:24153177}. Synapse
CC {ECO:0000269|PubMed:24153177}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q9Z214}. Note=Isoform 1 inhibits surface
CC expression of GRM5 causing it to be retained in the endoplasmic
CC reticulum. The N-terminal of isoform 2 may facilitate trafficking of
CC the complex with GRM5 from the endoplasmic reticulum (ER) to the plasma
CC membrane (PM).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Vesl-1L;
CC IsoId=Q9Z2Y3-1; Sequence=Displayed;
CC Name=2; Synonyms=1d;
CC IsoId=Q9Z2Y3-2; Sequence=VSP_009060, VSP_009061;
CC Name=3; Synonyms=1b;
CC IsoId=Q9Z2Y3-3; Sequence=VSP_009061;
CC Name=4; Synonyms=Vesl-1M;
CC IsoId=Q9Z2Y3-4; Sequence=VSP_009063, VSP_009065;
CC Name=5; Synonyms=Vesl-1S;
CC IsoId=Q9Z2Y3-5; Sequence=VSP_009062, VSP_009064;
CC -!- TISSUE SPECIFICITY: Isoform 1, isoform 3 and isoform 5 are expressed in
CC skeletal muscle at the level of the Z line, in heart, forebrain and
CC cerebellum. Isoform 2, is a minor isoform and is expressed in cardiac
CC and skeletal muscle. Isoform 5 is expressed in the postsynaptic region
CC of neurons. {ECO:0000269|PubMed:12379179, ECO:0000269|PubMed:24153177}.
CC -!- DOMAIN: The WH1 domain interacts with the PPXXF motif in GRM1, GRM5,
CC RYR1, RYR2, ITPR1, SHANK 1 and SHANK3. The coiled-Coil domain forms an
CC antiparallel tetrameric arrangement (By similarity).
CC {ECO:0000250|UniProtKB:Q9Z214}.
CC -!- SIMILARITY: Belongs to the Homer family. {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; AF093257; AAC71021.1; -; mRNA.
DR EMBL; AF093258; AAC71022.1; -; mRNA.
DR EMBL; AY137385; AAM95461.1; -; mRNA.
DR EMBL; AB019478; BAA34353.1; -; mRNA.
DR EMBL; AB019479; BAA34354.1; -; mRNA.
DR EMBL; AB089435; BAC07257.1; -; mRNA.
DR CCDS; CCDS26687.1; -. [Q9Z2Y3-5]
DR CCDS; CCDS36745.1; -. [Q9Z2Y3-1]
DR CCDS; CCDS36746.1; -. [Q9Z2Y3-2]
DR CCDS; CCDS70484.1; -. [Q9Z2Y3-3]
DR CCDS; CCDS84048.1; -. [Q9Z2Y3-4]
DR RefSeq; NP_001271118.1; NM_001284189.2. [Q9Z2Y3-3]
DR RefSeq; NP_001334527.1; NM_001347598.1. [Q9Z2Y3-4]
DR RefSeq; NP_036112.1; NM_011982.4. [Q9Z2Y3-5]
DR RefSeq; NP_671705.2; NM_147176.4. [Q9Z2Y3-1]
DR RefSeq; NP_687036.1; NM_152134.3. [Q9Z2Y3-2]
DR AlphaFoldDB; Q9Z2Y3; -.
DR BMRB; Q9Z2Y3; -.
DR SMR; Q9Z2Y3; -.
DR BioGRID; 205014; 64.
DR CORUM; Q9Z2Y3; -.
DR IntAct; Q9Z2Y3; 51.
DR MINT; Q9Z2Y3; -.
DR STRING; 10090.ENSMUSP00000078093; -.
DR TCDB; 8.A.29.1.1; the homer1 (homer1) family of excitation-contraction coupling proteins.
DR iPTMnet; Q9Z2Y3; -.
DR PhosphoSitePlus; Q9Z2Y3; -.
DR SwissPalm; Q9Z2Y3; -.
DR EPD; Q9Z2Y3; -.
DR MaxQB; Q9Z2Y3; -.
DR PaxDb; Q9Z2Y3; -.
DR PeptideAtlas; Q9Z2Y3; -.
DR PRIDE; Q9Z2Y3; -.
DR ProteomicsDB; 273121; -. [Q9Z2Y3-1]
DR ProteomicsDB; 273122; -. [Q9Z2Y3-2]
DR ProteomicsDB; 273123; -. [Q9Z2Y3-3]
DR ProteomicsDB; 273124; -. [Q9Z2Y3-4]
DR ProteomicsDB; 273125; -. [Q9Z2Y3-5]
DR ABCD; Q9Z2Y3; 12 sequenced antibodies.
DR Antibodypedia; 3836; 365 antibodies from 38 providers.
DR DNASU; 26556; -.
DR Ensembl; ENSMUST00000060490; ENSMUSP00000050471; ENSMUSG00000007617. [Q9Z2Y3-3]
DR Ensembl; ENSMUST00000079086; ENSMUSP00000078093; ENSMUSG00000007617. [Q9Z2Y3-2]
DR Ensembl; ENSMUST00000080127; ENSMUSP00000079026; ENSMUSG00000007617. [Q9Z2Y3-1]
DR Ensembl; ENSMUST00000102752; ENSMUSP00000099813; ENSMUSG00000007617. [Q9Z2Y3-5]
DR Ensembl; ENSMUST00000109492; ENSMUSP00000105118; ENSMUSG00000007617. [Q9Z2Y3-4]
DR GeneID; 26556; -.
DR KEGG; mmu:26556; -.
DR UCSC; uc007rlc.3; mouse. [Q9Z2Y3-1]
DR UCSC; uc007rld.3; mouse. [Q9Z2Y3-3]
DR UCSC; uc007rle.3; mouse. [Q9Z2Y3-2]
DR CTD; 9456; -.
DR MGI; MGI:1347345; Homer1.
DR VEuPathDB; HostDB:ENSMUSG00000007617; -.
DR eggNOG; ENOG502QR3K; Eukaryota.
DR GeneTree; ENSGT00940000156354; -.
DR HOGENOM; CLU_103795_0_0_1; -.
DR InParanoid; Q9Z2Y3; -.
DR OMA; GKMGEQP; -.
DR OrthoDB; 1251658at2759; -.
DR PhylomeDB; Q9Z2Y3; -.
DR TreeFam; TF325627; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 26556; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Homer1; mouse.
DR PRO; PR:Q9Z2Y3; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9Z2Y3; protein.
DR Bgee; ENSMUSG00000007617; Expressed in dorsal striatum and 246 other tissues.
DR ExpressionAtlas; Q9Z2Y3; baseline and differential.
DR Genevisible; Q9Z2Y3; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0043034; C:costamere; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
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:0060076; C:excitatory synapse; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR GO; GO:0044309; C:neuron spine; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:MGI.
DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0035256; F:G protein-coupled glutamate receptor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0099186; F:structural constituent of postsynapse; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0048148; P:behavioral response to cocaine; IMP:MGI.
DR GO; GO:0048875; P:chemical homeostasis within a tissue; IMP:MGI.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; ISO:MGI.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IMP:MGI.
DR GO; GO:0035418; P:protein localization to synapse; ISO:MGI.
DR GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB.
DR GO; GO:0090279; P:regulation of calcium ion import; IMP:BHF-UCL.
DR GO; GO:2001257; P:regulation of cation channel activity; IMP:BHF-UCL.
DR GO; GO:1902950; P:regulation of dendritic spine maintenance; ISS:UniProtKB.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IDA:SynGO.
DR GO; GO:2001256; P:regulation of store-operated calcium entry; IMP:BHF-UCL.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISS:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR GO; GO:0003009; P:skeletal muscle contraction; IMP:MGI.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
DR CDD; cd01206; EVH1_Homer_Vesl; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR045027; Homer.
DR InterPro; IPR044100; Homer_EVH1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR PANTHER; PTHR10918; PTHR10918; 1.
DR Pfam; PF00568; WH1; 1.
DR SMART; SM00461; WH1; 1.
DR PROSITE; PS50229; WH1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Phosphoprotein; Reference proteome; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q86YM7"
FT CHAIN 2..366
FT /note="Homer protein homolog 1"
FT /id="PRO_0000191006"
FT DOMAIN 1..110
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT REGION 114..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..366
FT /note="Required for tetramerization"
FT /evidence="ECO:0000250|UniProtKB:Q9Z214"
FT COILED 193..364
FT /evidence="ECO:0000255"
FT COMPBIAS 122..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q86YM7"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..2
FT /note="MG -> MLIHHHNRRALCKGSPTT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12176012"
FT /id="VSP_009060"
FT VAR_SEQ 176..187
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12176012,
FT ECO:0000303|PubMed:9808458"
FT /id="VSP_009061"
FT VAR_SEQ 176..186
FT /note="SAGDRTQALSH -> RYTFNSAIMIK (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9808458, ECO:0000303|Ref.3"
FT /id="VSP_009062"
FT VAR_SEQ 177..203
FT /note="AGDRTQALSHASSAISKHWEAELATLK -> SSRWIFFPYCEDSQLSLLESS
FT SGLGYF (in isoform 4)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_009063"
FT VAR_SEQ 187..366
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9808458, ECO:0000303|Ref.3"
FT /id="VSP_009064"
FT VAR_SEQ 204..366
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_009065"
FT CONFLICT 193
FT /note="K -> N (in Ref. 3; BAA34354)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="A -> V (in Ref. 3; BAA34354)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="N -> T (in Ref. 3; BAA34354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 41413 MW; 6A4CBCE5B8A91A3F CRC64;
MGEQPIFSTR AHVFQIDPNT KKNWVPTSKH AVTVSYFYDS TRNVYRIISL DGSKAIINST
ITPNMTFTKT SQKFGQWADS RANTVYGLGF SSEHHLSKFA EKFQEFKEAA RLAKEKSQEK
MELTSTPSQE SAGGDLQSPL TPESINGTDD ERTPDVTQNS EPRAEPTQNA LPFPHSAGDR
TQALSHASSA ISKHWEAELA TLKGNNAKLT AALLESTANV KQWKQQLAAY QEEAERLHKR
VTELECVSSQ ANAVHSHKTE LNQTVQELEE TLKVKEEEIE RLKQEIDNAR ELQEQRDSLT
QKLQEVEIRN KDLEGQLSDL EQRLEKSQNE QEAFRSNLKT LLEILDGKIF ELTELRDNLA
KLLECS
