GRM5_MOUSE
ID GRM5_MOUSE Reviewed; 1203 AA.
AC Q3UVX5;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Metabotropic glutamate receptor 5;
DE Short=mGluR5;
DE Flags: Precursor;
GN Name=Grm5; Synonyms=Gprc1e, Mglur5;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1014 AND SER-1016, AND
RP IDENTIFICATION BY 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 [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-868 AND ARG-924, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: G-protein coupled receptor for glutamate. Ligand binding
CC causes a conformation change that triggers signaling via guanine
CC nucleotide-binding proteins (G proteins) and modulates the activity of
CC down-stream effectors. Signaling activates a phosphatidylinositol-
CC calcium second messenger system and generates a calcium-activated
CC chloride current. Plays an important role in the regulation of synaptic
CC plasticity and the modulation of the neural network activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: The PPXXF motif binds HOMER1, HOMER2 and HOMER3. Interacts
CC with RYR1, RYR2, ITPR1, SHANK1 and SHANK3 (By similarity). Interacts
CC with SIAH1 and TAMALIN. Interacts with NCDN. Interacts with NECAB2 (By
CC similarity). Interacts with CAMK2A (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P31424, ECO:0000250|UniProtKB:P41594}.
CC -!- INTERACTION:
CC Q3UVX5; P16056: Met; NbExp=3; IntAct=EBI-8795045, EBI-1798780;
CC Q3UVX5; Q9Z214: Homer1; Xeno; NbExp=2; IntAct=EBI-8795045, EBI-2338940;
CC Q3UVX5; Q9Z214-1: Homer1; Xeno; NbExp=3; IntAct=EBI-8795045, EBI-4410552;
CC Q3UVX5; Q9Z214-3: Homer1; Xeno; NbExp=2; IntAct=EBI-8795045, EBI-2339003;
CC Q3UVX5; Q13526: PIN1; Xeno; NbExp=2; IntAct=EBI-8795045, EBI-714158;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UVX5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UVX5-2; Sequence=VSP_028519, VSP_028520;
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; AK136840; BAE23144.1; -; mRNA.
DR EMBL; AC113033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC149088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC163218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS52305.1; -. [Q3UVX5-1]
DR RefSeq; NP_001137306.1; NM_001143834.1. [Q3UVX5-1]
DR RefSeq; XP_011239945.1; XM_011241643.2. [Q3UVX5-1]
DR AlphaFoldDB; Q3UVX5; -.
DR SMR; Q3UVX5; -.
DR BioGRID; 223809; 16.
DR CORUM; Q3UVX5; -.
DR IntAct; Q3UVX5; 10.
DR MINT; Q3UVX5; -.
DR STRING; 10090.ENSMUSP00000129181; -.
DR BindingDB; Q3UVX5; -.
DR ChEMBL; CHEMBL1641352; -.
DR GuidetoPHARMACOLOGY; 293; -.
DR GlyConnect; 2510; 1 N-Linked glycan (1 site).
DR GlyGen; Q3UVX5; 6 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q3UVX5; -.
DR PhosphoSitePlus; Q3UVX5; -.
DR MaxQB; Q3UVX5; -.
DR PaxDb; Q3UVX5; -.
DR PeptideAtlas; Q3UVX5; -.
DR PRIDE; Q3UVX5; -.
DR ProteomicsDB; 271305; -. [Q3UVX5-1]
DR ProteomicsDB; 271306; -. [Q3UVX5-2]
DR ABCD; Q3UVX5; 2 sequenced antibodies.
DR Antibodypedia; 2950; 553 antibodies from 44 providers.
DR Ensembl; ENSMUST00000155358; ENSMUSP00000114927; ENSMUSG00000049583. [Q3UVX5-1]
DR GeneID; 108071; -.
DR KEGG; mmu:108071; -.
DR UCSC; uc009ifp.2; mouse. [Q3UVX5-2]
DR UCSC; uc009ifs.2; mouse. [Q3UVX5-1]
DR CTD; 2915; -.
DR MGI; MGI:1351342; Grm5.
DR VEuPathDB; HostDB:ENSMUSG00000049583; -.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234595; -.
DR InParanoid; Q3UVX5; -.
DR OMA; EVEEHYP; -.
DR PhylomeDB; Q3UVX5; -.
DR TreeFam; TF313240; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 108071; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Grm5; mouse.
DR PRO; PR:Q3UVX5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3UVX5; protein.
DR Bgee; ENSMUSG00000049583; Expressed in lateral septal nucleus and 79 other tissues.
DR ExpressionAtlas; Q3UVX5; baseline and differential.
DR Genevisible; Q3UVX5; MM.
DR GO; GO:0097449; C:astrocyte projection; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0031687; F:A2A adenosine receptor binding; ISO:MGI.
DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0099530; F:G protein-coupled receptor activity involved in regulation of postsynaptic membrane potential; IMP:SynGO.
DR GO; GO:0008066; F:glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0099583; F:neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; IMP:SynGO.
DR GO; GO:0001639; F:PLC activating G protein-coupled glutamate receptor activity; TAS:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IGI:ARUK-UCL.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IGI:ARUK-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:MGI.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0002029; P:desensitization of G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0007611; P:learning or memory; IGI:ARUK-UCL.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0040013; P:negative regulation of locomotion; ISO:MGI.
DR GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IGI:ARUK-UCL.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:1902938; P:regulation of intracellular calcium activated chloride channel activity; ISO:MGI.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006448; P:regulation of translational elongation; ISO:MGI.
DR GO; GO:0050808; P:synapse organization; IGI:ARUK-UCL.
DR GO; GO:0099553; P:trans-synaptic signaling by endocannabinoid, modulating synaptic transmission; ISO:MGI.
DR Gene3D; 2.10.50.30; -; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR000337; GPCR_3.
DR InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR InterPro; IPR038550; GPCR_3_9-Cys_sf.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR017979; GPCR_3_CS.
DR InterPro; IPR000202; GPCR_3_mGluR5.
DR InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR InterPro; IPR019588; Metabotropic_Glu_rcpt_Homer-bd.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF10606; GluR_Homer-bdg; 1.
DR Pfam; PF07562; NCD3G; 1.
DR PRINTS; PR00248; GPCRMGR.
DR PRINTS; PR01055; MTABOTROPC5R.
DR PRINTS; PR00593; MTABOTROPICR.
DR SMART; SM01229; GluR_Homer-bdg; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
DR PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
DR PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Methylation;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1203
FT /note="Metabotropic glutamate receptor 5"
FT /id="PRO_0000306853"
FT TOPO_DOM 19..579
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 580..602
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 603..612
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 613..635
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 636..643
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 644..666
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 667..692
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 693..713
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 714..736
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 737..758
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 759..771
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 772..794
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 795..797
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 798..819
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 820..1203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 892..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 172..174
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 395
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31424"
FT MOD_RES 868
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 924
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1016
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..99
FT /evidence="ECO:0000250"
FT DISULFID 240..529
FT /evidence="ECO:0000250"
FT DISULFID 275..277
FT /evidence="ECO:0000250"
FT DISULFID 364..380
FT /evidence="ECO:0000250"
FT DISULFID 418..425
FT /evidence="ECO:0000250"
FT DISULFID 510..530
FT /evidence="ECO:0000250"
FT DISULFID 514..533
FT /evidence="ECO:0000250"
FT DISULFID 536..548
FT /evidence="ECO:0000250"
FT DISULFID 551..564
FT /evidence="ECO:0000250"
FT DISULFID 643..732
FT /evidence="ECO:0000250"
FT VAR_SEQ 303
FT /note="S -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028519"
FT VAR_SEQ 304..1203
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028520"
SQ SEQUENCE 1203 AA; 131865 MW; 2A09D7EC272ED23C CRC64;
MVLLLILSVL LLKEDVRGSA QSSERRVVAH MPGDIIIGAL FSVHHQPTVD KVHERKCGAV
REQYGIQRVE AMLHTLERIN SDPTLLPNIT LGCEIRDSCW HSAVALEQSI EFIRDSLISS
EEEEGLVRCV DGSSSFRSKK PIVGVIGPGS SSVAIQVQNL LQLFNIPQIA YSATSMDLSD
KTLFKYFMRV VPSDAQQARA MVDIVKRYNW TYVSAVHTEG NYGESGMEAF KDMSAKEGIC
IAHSYKIYSN AGEQSFDKLL KKLRSHLPKA RVVACFCEGM TVRGLLMAMR RLGLAGEFLL
LGSDGWADRY DVTDGYQREA VGGITIKLQS PDVKWFDDYY LKLRPETNLR NPWFQEFWQH
RFQCRLEGFA QENSKYNKTC NSSLTLRTHH VQDSKMGFVI NAIYSMAYGL HNMQMSLCPG
YAGLCDAMKP IDGRKLLDSL MKTNFTGVSG DMILFDENGD SPGRYEIMNF KEMGKDYFDY
INVGSWDNGE LKMDDDEVWS KKNNIIRSVC SEPCEKGQIK VIRKGEVSCC WTCTPCKENE
YVFDEYTCKA CQLGSWPTDD LTGCDLIPVQ YLRWGDPEPI AAVVFACLGL LATLFVTVIF
IIYRDTPVVK SSSRELCYII LAGICLGYLC TFCLIAKPKQ IYCYLQRIGI GLSPAMSYSA
LVTKTNRIAR ILAGSKKKIC TKKPRFMSAC AQLVIAFILI CIQLGIIVAL FIMEPPDIMH
DYPSIREVYL ICNTTNLGVV TPLGYNGLLI LSCTFYAFKT RNVPANFNEA KYIAFTMYTT
CIIWLAFVPI YFGSNYKIIT MCFSVSLSAT VALGCMFVPK VYIILAKPER NVRSAFTTST
VVRMHVGDGK SSSAASRSSS LVNLWKRRGS SGETLRYKDR RLAQHKSEIE CFTPKGSMGN
GGRATMSSSN GKSVTWAQNE KSTRGQHLWQ RLSVHINKKE NPNQTAVIKP FPKSTESRGQ
GAGAGGGSGP GAAGAGSAGC TATGGPEPPD AGPKALYDVA EAEERFPAAA RPRSPSPIST
LSHLAGSAGR TDDDAPSLHS ETAARSSSSQ GSLMEQISSV VTRFTANITE LNSMMLSTAA
APGPPGTPIC SSYLIPKEIQ LPTTMTTFAE IQPLPAIEVT GGAQPATGPS PAQETPAGAE
AAPGKPDLEE LVALTPPSPF RDSVDSGSTT PNSPVSESAL CIPSSPKYDT LIIRDYTQSS
SSL
