GRM4_HUMAN
ID GRM4_HUMAN Reviewed; 912 AA.
AC Q14833; B3KVL9; B7Z1T9; B7Z1U6; F5GXM5; Q5SZ84; Q6ZMQ2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Metabotropic glutamate receptor 4;
DE Short=mGluR4;
DE Flags: Precursor;
GN Name=GRM4; Synonyms=GPRC1D, MGLUR4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8738157; DOI=10.1016/0169-328x(95)00321-i;
RA Makoff A., Lelchuk R., Oxer M., Harrington K., Emson P.;
RT "Molecular characterization and localization of human metabotropic
RT glutamate receptor type 4.";
RL Brain Res. Mol. Brain Res. 37:239-248(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=9473604; DOI=10.1016/s0169-328x(97)00277-5;
RA Wu S., Wright R.A., Rockey P.K., Burgett S.G., Arnold J.S.,
RA Rosteck P.R. Jr., Johnson B.G., Schoepp D.D., Belagaje R.M.;
RT "Group III human metabotropic glutamate receptors 4, 7 and 8: molecular
RT cloning, functional expression, and comparison of pharmacological
RT properties in RGT cells.";
RL Brain Res. Mol. Brain Res. 53:88-97(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7617140; DOI=10.1016/0028-3908(94)00149-m;
RA Flor P.J., Lukic S., Rueegg D., Leonhardt T., Knoepfel T., Kuhn R.;
RT "Molecular cloning, functional expression and pharmacological
RT characterization of the human metabotropic glutamate receptor type 4.";
RL Neuropharmacology 34:149-155(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
RC TISSUE=Brain, and Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP VARIANT ILE-797.
RX PubMed=11525421; DOI=10.1097/00041444-200106000-00004;
RA Ohtsuki T., Toru M., Arinami T.;
RT "Mutation screening of the metabotropic glutamate receptor mGluR4 (GRM4)
RT gene in patients with schizophrenia.";
RL Psychiatr. Genet. 11:79-83(2001).
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 inhibits adenylate cyclase activity.
CC {ECO:0000269|PubMed:7617140, ECO:0000269|PubMed:8738157,
CC ECO:0000269|PubMed:9473604}.
CC -!- SUBUNIT: Interacts with PICK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7617140,
CC ECO:0000269|PubMed:8738157}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:7617140, ECO:0000269|PubMed:8738157}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q14833-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14833-2; Sequence=VSP_044740, VSP_044741;
CC Name=3;
CC IsoId=Q14833-3; Sequence=VSP_045218;
CC Name=4;
CC IsoId=Q14833-4; Sequence=VSP_046762;
CC Name=5;
CC IsoId=Q14833-5; Sequence=VSP_046761, VSP_046763;
CC -!- TISSUE SPECIFICITY: Strongly expressed in the cerebellum. Expressed at
CC low levels in hippocampus, hypothalamus and thalamus. No expression
CC detected in liver. {ECO:0000269|PubMed:7617140,
CC ECO:0000269|PubMed:8738157}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
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; X80818; CAA56784.1; -; mRNA.
DR EMBL; U92457; AAB51762.1; -; mRNA.
DR EMBL; AK122982; BAG53831.1; -; mRNA.
DR EMBL; AK131536; BAD18673.1; -; mRNA.
DR EMBL; AK293913; BAH11625.1; -; mRNA.
DR EMBL; AK293949; BAH11632.1; -; mRNA.
DR EMBL; AL354740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS4787.1; -. [Q14833-1]
DR CCDS; CCDS59010.1; -. [Q14833-4]
DR CCDS; CCDS59011.1; -. [Q14833-3]
DR CCDS; CCDS59012.1; -. [Q14833-5]
DR RefSeq; NP_000832.1; NM_000841.3. [Q14833-1]
DR RefSeq; NP_001243738.1; NM_001256809.2. [Q14833-5]
DR RefSeq; NP_001243740.1; NM_001256811.2.
DR RefSeq; NP_001243741.1; NM_001256812.2. [Q14833-3]
DR RefSeq; NP_001243742.1; NM_001256813.2. [Q14833-4]
DR RefSeq; NP_001269776.1; NM_001282847.1.
DR RefSeq; XP_016866279.1; XM_017010790.1.
DR RefSeq; XP_016866280.1; XM_017010791.1.
DR RefSeq; XP_016866282.1; XM_017010793.1.
DR PDB; 7E9H; EM; 4.00 A; R/S=33-912.
DR PDBsum; 7E9H; -.
DR AlphaFoldDB; Q14833; -.
DR SMR; Q14833; -.
DR BioGRID; 109171; 5.
DR CORUM; Q14833; -.
DR STRING; 9606.ENSP00000440556; -.
DR BindingDB; Q14833; -.
DR ChEMBL; CHEMBL2736; -.
DR DrugBank; DB00142; Glutamic acid.
DR DrugCentral; Q14833; -.
DR GuidetoPHARMACOLOGY; 292; -.
DR GlyGen; Q14833; 5 sites.
DR iPTMnet; Q14833; -.
DR PhosphoSitePlus; Q14833; -.
DR BioMuta; GRM4; -.
DR DMDM; 2495077; -.
DR EPD; Q14833; -.
DR MassIVE; Q14833; -.
DR PaxDb; Q14833; -.
DR PeptideAtlas; Q14833; -.
DR PRIDE; Q14833; -.
DR ProteomicsDB; 24469; -.
DR ProteomicsDB; 3762; -.
DR ProteomicsDB; 60203; -. [Q14833-1]
DR ProteomicsDB; 6370; -.
DR ProteomicsDB; 67900; -.
DR Antibodypedia; 14430; 236 antibodies from 30 providers.
DR DNASU; 2914; -.
DR Ensembl; ENST00000374177.7; ENSP00000363292.3; ENSG00000124493.14. [Q14833-5]
DR Ensembl; ENST00000455714.6; ENSP00000398456.2; ENSG00000124493.14. [Q14833-2]
DR Ensembl; ENST00000535756.5; ENSP00000437925.1; ENSG00000124493.14. [Q14833-4]
DR Ensembl; ENST00000538487.7; ENSP00000440556.1; ENSG00000124493.14. [Q14833-1]
DR Ensembl; ENST00000544773.6; ENSP00000437730.1; ENSG00000124493.14. [Q14833-3]
DR Ensembl; ENST00000609222.5; ENSP00000477466.1; ENSG00000124493.14. [Q14833-4]
DR GeneID; 2914; -.
DR KEGG; hsa:2914; -.
DR MANE-Select; ENST00000538487.7; ENSP00000440556.1; NM_000841.4; NP_000832.1.
DR UCSC; uc003oiq.6; human. [Q14833-1]
DR CTD; 2914; -.
DR DisGeNET; 2914; -.
DR GeneCards; GRM4; -.
DR HGNC; HGNC:4596; GRM4.
DR HPA; ENSG00000124493; Tissue enriched (brain).
DR MIM; 604100; gene.
DR neXtProt; NX_Q14833; -.
DR OpenTargets; ENSG00000124493; -.
DR PharmGKB; PA28993; -.
DR VEuPathDB; HostDB:ENSG00000124493; -.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234648; -.
DR InParanoid; Q14833; -.
DR OMA; RTPEYKV; -.
DR PhylomeDB; Q14833; -.
DR TreeFam; TF313240; -.
DR PathwayCommons; Q14833; -.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR Reactome; R-HSA-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR SignaLink; Q14833; -.
DR SIGNOR; Q14833; -.
DR BioGRID-ORCS; 2914; 11 hits in 1066 CRISPR screens.
DR ChiTaRS; GRM4; human.
DR GeneWiki; Metabotropic_glutamate_receptor_4; -.
DR GenomeRNAi; 2914; -.
DR Pharos; Q14833; Tchem.
DR PRO; PR:Q14833; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q14833; protein.
DR Bgee; ENSG00000124493; Expressed in paraflocculus and 119 other tissues.
DR ExpressionAtlas; Q14833; baseline and differential.
DR Genevisible; Q14833; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
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; IMP:UniProtKB.
DR GO; GO:0008066; F:glutamate receptor activity; IMP:UniProtKB.
DR GO; GO:0007196; P:adenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007269; P:neurotransmitter secretion; TAS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; TAS:UniProtKB.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
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; IPR001786; GPCR_3_mGluR4.
DR InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF07562; NCD3G; 1.
DR PRINTS; PR00248; GPCRMGR.
DR PRINTS; PR01054; MTABOTROPC4R.
DR PRINTS; PR00593; MTABOTROPICR.
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 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..912
FT /note="Metabotropic glutamate receptor 4"
FT /id="PRO_0000012930"
FT TOPO_DOM 33..587
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..610
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 611..624
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 625..645
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 646..656
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 657..675
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 676..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 700..720
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 721..750
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 751..772
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 773..785
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 786..808
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 809..821
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..847
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 848..912
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 159
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 180..182
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..109
FT /evidence="ECO:0000250"
FT DISULFID 249..538
FT /evidence="ECO:0000250"
FT DISULFID 372..388
FT /evidence="ECO:0000250"
FT DISULFID 428..435
FT /evidence="ECO:0000250"
FT DISULFID 520..539
FT /evidence="ECO:0000250"
FT DISULFID 524..542
FT /evidence="ECO:0000250"
FT DISULFID 545..557
FT /evidence="ECO:0000250"
FT DISULFID 560..573
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..173
FT /note="MPGKRGLGWWWARLPLCLLLSLYGPWMPSSLGKPKGHPHMNSIRIDGDITLG
FT GLFPVHGRGSEGKPCGELKKEKGIHRLEAMLFALDRINNDPDLLPNITLGARILDTCSR
FT DTHALEQSLTFVQALIEKDGTEVRCGSGGPPIITKPERVVGVIGASGSSVSIMVANILR
FT LFK -> MPAWEPGVAASCGWRAPPCSPLRLCIAPHPCTPPSSHQGNLTCRLPPRSFGF
FT CRCVWVRTRGPSLPGEQVSLAAHESEGAAAQLGSSPEIDPRRPRCLLPESAQ (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046761"
FT VAR_SEQ 1..172
FT /note="MPGKRGLGWWWARLPLCLLLSLYGPWMPSSLGKPKGHPHMNSIRIDGDITLG
FT GLFPVHGRGSEGKPCGELKKEKGIHRLEAMLFALDRINNDPDLLPNITLGARILDTCSR
FT DTHALEQSLTFVQALIEKDGTEVRCGSGGPPIITKPERVVGVIGASGSSVSIMVANILR
FT LF -> MSC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045218"
FT VAR_SEQ 1..172
FT /note="MPGKRGLGWWWARLPLCLLLSLYGPWMPSSLGKPKGHPHMNSIRIDGDITLG
FT GLFPVHGRGSEGKPCGELKKEKGIHRLEAMLFALDRINNDPDLLPNITLGARILDTCSR
FT DTHALEQSLTFVQALIEKDGTEVRCGSGGPPIITKPERVVGVIGASGSSVSIMVANILR
FT LF -> MAVPLGAPCWASALPAWAPPGLPHRSLLTRLLSQHVKPA (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046762"
FT VAR_SEQ 1..33
FT /note="MPGKRGLGWWWARLPLCLLLSLYGPWMPSSLGK -> MVQTLPKLFPHDGAK
FT RKKRTLRTSGPCFGGGGQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044740"
FT VAR_SEQ 34..173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044741"
FT VAR_SEQ 343..390
FT /note="GFDRYFSSRTLDNNRRNIWFAEFWEDNFHCKLSRHALKKGSHVKKCTN ->
FT D (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046763"
FT VARIANT 169
FT /note="L -> F (in dbSNP:rs452752)"
FT /id="VAR_049275"
FT VARIANT 797
FT /note="V -> I (in dbSNP:rs149730753)"
FT /evidence="ECO:0000269|PubMed:11525421"
FT /id="VAR_012992"
FT CONFLICT 449
FT /note="Y -> H (in Ref. 4; BAH11632)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 912 AA; 101868 MW; 4A2F36E63A2EAF5A CRC64;
MPGKRGLGWW WARLPLCLLL SLYGPWMPSS LGKPKGHPHM NSIRIDGDIT LGGLFPVHGR
GSEGKPCGEL KKEKGIHRLE AMLFALDRIN NDPDLLPNIT LGARILDTCS RDTHALEQSL
TFVQALIEKD GTEVRCGSGG PPIITKPERV VGVIGASGSS VSIMVANILR LFKIPQISYA
STAPDLSDNS RYDFFSRVVP SDTYQAQAMV DIVRALKWNY VSTVASEGSY GESGVEAFIQ
KSREDGGVCI AQSVKIPREP KAGEFDKIIR RLLETSNARA VIIFANEDDI RRVLEAARRA
NQTGHFFWMG SDSWGSKIAP VLHLEEVAEG AVTILPKRMS VRGFDRYFSS RTLDNNRRNI
WFAEFWEDNF HCKLSRHALK KGSHVKKCTN RERIGQDSAY EQEGKVQFVI DAVYAMGHAL
HAMHRDLCPG RVGLCPRMDP VDGTQLLKYI RNVNFSGIAG NPVTFNENGD APGRYDIYQY
QLRNDSAEYK VIGSWTDHLH LRIERMHWPG SGQQLPRSIC SLPCQPGERK KTVKGMPCCW
HCEPCTGYQY QVDRYTCKTC PYDMRPTENR TGCRPIPIIK LEWGSPWAVL PLFLAVVGIA
ATLFVVITFV RYNDTPIVKA SGRELSYVLL AGIFLCYATT FLMIAEPDLG TCSLRRIFLG
LGMSISYAAL LTKTNRIYRI FEQGKRSVSA PRFISPASQL AITFSLISLQ LLGICVWFVV
DPSHSVVDFQ DQRTLDPRFA RGVLKCDISD LSLICLLGYS MLLMVTCTVY AIKTRGVPET
FNEAKPIGFT MYTTCIVWLA FIPIFFGTSQ SADKLYIQTT TLTVSVSLSA SVSLGMLYMP
KVYIILFHPE QNVPKRKRSL KAVVTAATMS NKFTQKGNFR PNGEAKSELC ENLEAPALAT
KQTYVTYTNH AI
