GABR1_MOUSE
ID GABR1_MOUSE Reviewed; 960 AA.
AC Q9WV18; Q6PGJ2; Q9WU48; Q9WV15; Q9WV16; Q9WV17;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Gamma-aminobutyric acid type B receptor subunit 1;
DE Short=GABA-B receptor 1;
DE Short=GABA-B-R1;
DE Short=GABA-BR1;
DE Short=GABABR1;
DE Short=Gb1;
DE Flags: Precursor;
GN Name=Gabbr1;
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] (ISOFORM 1A), FUNCTION, INTERACTION WITH GABBR2,
RP AND SUBCELLULAR LOCATION.
RX PubMed=10773016;
RA Sullivan R., Chateauneuf A., Coulombe N., Kolakowski L.F. Jr.,
RA Johnson M.P., Hebert T.E., Ethier N., Belley M., Metters K., Abramovitz M.,
RA O'Neill G.P., Ng G.Y.K.;
RT "Coexpression of full-length gamma-aminobutyric acid(B) (GABA(B)) receptors
RT with truncated receptors and metabotropic glutamate receptor 4 supports the
RT GABA(B) heterodimer as the functional receptor.";
RL J. Pharmacol. Exp. Ther. 293:460-467(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B), AND TISSUE SPECIFICITY.
RX PubMed=11306808; DOI=10.1159/000056880;
RA Lamp K., Humeny A., Nikolic Z., Imai K., Adamski J., Schiebel K.,
RA Becker C.M.;
RT "The murine GABA(B) receptor 1: cDNA cloning, tissue distribution,
RT structure of the Gabbr1 gene, and mapping to chromosome 17.";
RL Cytogenet. Cell Genet. 92:116-121(2001).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1A AND 1B).
RC STRAIN=C57BL/6J; TISSUE=Brain {ECO:0000303|PubMed:15489334};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH GABBR2.
RX PubMed=10075644; DOI=10.1074/jbc.274.12.7607;
RA Ng G.Y.K., Clark J., Coulombe N., Ethier N., Hebert T.E., Sullivan R.,
RA Kargman S., Chateauneuf A., Tsukamoto N., McDonald T., Whiting P.,
RA Mezey E., Johnson M.P., Liu Q., Kolakowski L.F. Jr., Evans J.F.,
RA Bonner T.I., O'Neill G.P.;
RT "Identification of a GABAB receptor subunit, gb2, required for functional
RT GABAB receptor activity.";
RL J. Biol. Chem. 274:7607-7610(1999).
RN [6]
RP INTERACTION WITH GABBR2.
RX PubMed=9872744; DOI=10.1126/science.283.5398.74;
RA Kuner R., Koehr G., Gruenewald S., Eisenhardt G., Bach A., Kornau H.-C.;
RT "Role of heteromer formation in GABAB receptor function.";
RL Science 283:74-77(1999).
RN [7]
RP INTERACTION WITH JAKMIP1.
RX PubMed=14718537; DOI=10.1074/jbc.m311737200;
RA Couve A., Restituito S., Brandon J.M., Charles K.J., Bawagan H.,
RA Freeman K.B., Pangalos M.N., Calver A.R., Moss S.J.;
RT "Marlin-1, a novel RNA-binding protein associates with GABA receptors.";
RL J. Biol. Chem. 279:13934-13943(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-872 AND THR-929, 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).
CC -!- FUNCTION: Component of a heterodimeric G-protein coupled receptor for
CC GABA, formed by GABBR1 and GABBR2 (PubMed:10773016, PubMed:10075644).
CC Within the heterodimeric GABA receptor, only GABBR1 seems to bind
CC agonists, while GABBR2 mediates coupling to G proteins (By similarity).
CC Ligand binding causes a conformation change that triggers signaling via
CC guanine nucleotide-binding proteins (G proteins) and modulates the
CC activity of down-stream effectors, such as adenylate cyclase
CC (PubMed:10773016, PubMed:10075644). Signaling inhibits adenylate
CC cyclase, stimulates phospholipase A2, activates potassium channels,
CC inactivates voltage-dependent calcium-channels and modulates inositol
CC phospholipid hydrolysis (PubMed:10075644). Calcium is required for high
CC affinity binding to GABA (By similarity). Plays a critical role in the
CC fine-tuning of inhibitory synaptic transmission (By similarity). Pre-
CC synaptic GABA receptor inhibits neurotransmitter release by down-
CC regulating high-voltage activated calcium channels, whereas
CC postsynaptic GABA receptor decreases neuronal excitability by
CC activating a prominent inwardly rectifying potassium (Kir) conductance
CC that underlies the late inhibitory postsynaptic potentials
CC (PubMed:10075644). Not only implicated in synaptic inhibition but also
CC in hippocampal long-term potentiation, slow wave sleep, muscle
CC relaxation and antinociception (By similarity).
CC {ECO:0000250|UniProtKB:Q9UBS5, ECO:0000250|UniProtKB:Q9Z0U4,
CC ECO:0000269|PubMed:10075644, ECO:0000269|PubMed:10773016}.
CC -!- SUBUNIT: Heterodimer of GABBR1 and GABBR2 (PubMed:10773016,
CC PubMed:10075644, PubMed:9872744). Homodimers may form, but are inactive
CC (By similarity). Interacts (via C-terminus) with ATF4 (via leucine
CC zipper domain) (By similarity). Interacts with JAKMIP1
CC (PubMed:14718537). {ECO:0000250|UniProtKB:Q9Z0U4,
CC ECO:0000269|PubMed:10075644, ECO:0000269|PubMed:10773016,
CC ECO:0000269|PubMed:14718537, ECO:0000269|PubMed:9872744}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Cell projection, dendrite
CC {ECO:0000250}. Note=Coexpression of GABBR1 and GABBR2 is required for
CC GABBR1 maturation and transport to the plasma membrane. Colocalizes
CC with ATF4 in hippocampal neuron dendritic membranes (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1A;
CC IsoId=Q9WV18-1; Sequence=Displayed;
CC Name=1B;
CC IsoId=Q9WV18-2; Sequence=VSP_002041;
CC -!- TISSUE SPECIFICITY: Expressed in neuronal tissue including cortex,
CC cerebellum and spinal cord. Not detected in non-neuronal tissues
CC including heart, liver, spleen and kidney.
CC {ECO:0000269|PubMed:11306808}.
CC -!- DOMAIN: Alpha-helical parts of the C-terminal intracellular region
CC mediate heterodimeric interaction with GABBR2. The linker region
CC between the transmembrane domain 3 (TM3) and the transmembrane domain 4
CC (TM4) probably plays a role in the specificity for G-protein coupling.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family. GABA-B
CC receptor subfamily. {ECO:0000305}.
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DR EMBL; AF114168; AAD22194.2; -; mRNA.
DR EMBL; AF008649; AAG29338.1; -; mRNA.
DR EMBL; AF120255; AAG29341.1; -; mRNA.
DR EMBL; AL078630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054735; AAH54735.1; -; mRNA.
DR EMBL; BC056990; AAH56990.1; -; mRNA.
DR CCDS; CCDS37616.1; -. [Q9WV18-1]
DR RefSeq; NP_062312.3; NM_019439.3. [Q9WV18-1]
DR AlphaFoldDB; Q9WV18; -.
DR SMR; Q9WV18; -.
DR BioGRID; 207643; 7.
DR ComplexPortal; CPX-2990; GABA-B receptor complex.
DR IntAct; Q9WV18; 4.
DR MINT; Q9WV18; -.
DR STRING; 10090.ENSMUSP00000025338; -.
DR GlyConnect; 2328; 9 N-Linked glycans (5 sites).
DR GlyGen; Q9WV18; 8 sites, 8 N-linked glycans (5 sites).
DR iPTMnet; Q9WV18; -.
DR PhosphoSitePlus; Q9WV18; -.
DR SwissPalm; Q9WV18; -.
DR MaxQB; Q9WV18; -.
DR PaxDb; Q9WV18; -.
DR PeptideAtlas; Q9WV18; -.
DR PRIDE; Q9WV18; -.
DR ProteomicsDB; 273410; -. [Q9WV18-1]
DR ProteomicsDB; 273411; -. [Q9WV18-2]
DR ABCD; Q9WV18; 1 sequenced antibody.
DR Antibodypedia; 50418; 546 antibodies from 44 providers.
DR DNASU; 54393; -.
DR Ensembl; ENSMUST00000025338; ENSMUSP00000025338; ENSMUSG00000024462. [Q9WV18-1]
DR Ensembl; ENSMUST00000172792; ENSMUSP00000134268; ENSMUSG00000024462. [Q9WV18-2]
DR GeneID; 54393; -.
DR KEGG; mmu:54393; -.
DR UCSC; uc008cma.1; mouse. [Q9WV18-1]
DR UCSC; uc008cmd.1; mouse. [Q9WV18-2]
DR CTD; 2550; -.
DR MGI; MGI:1860139; Gabbr1.
DR VEuPathDB; HostDB:ENSMUSG00000024462; -.
DR eggNOG; KOG1055; Eukaryota.
DR GeneTree; ENSGT00940000157642; -.
DR HOGENOM; CLU_005240_2_0_1; -.
DR InParanoid; Q9WV18; -.
DR OMA; WAGGEAC; -.
DR OrthoDB; 590810at2759; -.
DR PhylomeDB; Q9WV18; -.
DR TreeFam; TF313965; -.
DR Reactome; R-MMU-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR Reactome; R-MMU-977444; GABA B receptor activation.
DR Reactome; R-MMU-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR BioGRID-ORCS; 54393; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Gabbr1; mouse.
DR PRO; PR:Q9WV18; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9WV18; protein.
DR Bgee; ENSMUSG00000024462; Expressed in habenula and 254 other tissues.
DR ExpressionAtlas; Q9WV18; baseline and differential.
DR Genevisible; Q9WV18; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030673; C:axolemma; 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:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:1902712; C:G protein-coupled GABA receptor complex; ISO:MGI.
DR GO; GO:0038037; C:G protein-coupled receptor dimeric complex; IDA:MGI.
DR GO; GO:0038039; C:G protein-coupled receptor heterodimeric complex; ISS:UniProtKB.
DR GO; GO:1902710; C:GABA receptor complex; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; IMP:SynGO.
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:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR GO; GO:0098793; C:presynapse; IDA:ParkinsonsUK-UCL.
DR GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:1990430; F:extracellular matrix protein binding; ISO:MGI.
DR GO; GO:0004965; F:G protein-coupled GABA receptor activity; ISS:UniProtKB.
DR GO; GO:0099579; F:G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential; IMP:SynGO.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IDA:MGI.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0033602; P:negative regulation of dopamine secretion; ISO:MGI.
DR GO; GO:0032811; P:negative regulation of epinephrine secretion; ISO:MGI.
DR GO; GO:0014053; P:negative regulation of gamma-aminobutyric acid secretion; ISO:MGI.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; ISO:MGI.
DR GO; GO:0150099; P:neuron-glial cell signaling; ISO:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; ISO:MGI.
DR GO; GO:0014049; P:positive regulation of glutamate secretion; ISO:MGI.
DR GO; GO:0060124; P:positive regulation of growth hormone secretion; ISO:MGI.
DR GO; GO:0014048; P:regulation of glutamate secretion; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IC:ComplexPortal.
DR CDD; cd15291; 7tmC_GABA-B-R1; 1.
DR CDD; cd00033; CCP; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR002455; GPCR3_GABA-B.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR002456; GPCR_3_GABA_rcpt_B1.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR10519; PTHR10519; 1.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00084; Sushi; 1.
DR SMART; SM00032; CCP; 2.
DR SUPFAM; SSF53822; SSF53822; 1.
DR SUPFAM; SSF57535; SSF57535; 2.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
DR PROSITE; PS50923; SUSHI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Coiled coil;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW Repeat; Signal; Sushi; Synapse; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..960
FT /note="Gamma-aminobutyric acid type B receptor subunit 1"
FT /id="PRO_0000012950"
FT TOPO_DOM 17..590
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..611
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 612..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 631..651
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 652..666
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 667..687
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 688..709
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..767
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 768..788
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 789..803
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 804..824
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 825..832
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 833..853
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 854..960
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..95
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 97..158
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 866..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..915
FT /note="Interaction with ATF4"
FT /evidence="ECO:0000250"
FT REGION 908..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 868..924
FT /evidence="ECO:0000255"
FT COMPBIAS 866..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..940
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS5"
FT BINDING 269
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS5"
FT BINDING 286
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS5"
FT BINDING 366
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS5"
FT BINDING 465
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS5"
FT MOD_RES 872
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 929
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 130..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 219..245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 375..409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT VAR_SEQ 1..163
FT /note="MLLLLLVPLFLRPLGAGGAQTPNVTSEGCQIIHPPWEGGIRYRGLTRDQVKA
FT INFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGKV
FT FLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPH -> MGP
FT GGPCTPVGWPLPLLLVMAAGVAPVWASHSPHLPRPHPRVPPHPS (in isoform
FT 1B)"
FT /evidence="ECO:0000303|PubMed:11306808,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_002041"
FT CONFLICT 7..8
FT /note="VP -> LL (in Ref. 1; AAD22194)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="T -> I (in Ref. 1; AAD22194)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="V -> A (in Ref. 1; AAD22194)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="A -> V (in Ref. 1; AAD22194)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="W -> R (in Ref. 4; AAH56990)"
FT /evidence="ECO:0000305"
FT CONFLICT 721
FT /note="I -> V (in Ref. 1; AAD22194)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="A -> P (in Ref. 2; AAG29338/AAG29341)"
FT /evidence="ECO:0000305"
FT CONFLICT 869
FT /note="A -> T (in Ref. 1; AAD22194)"
FT /evidence="ECO:0000305"
FT CONFLICT 921
FT /note="I -> L (in Ref. 1; AAD22194)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 960 AA; 108216 MW; E4B5A9401E23E8B4 CRC64;
MLLLLLVPLF LRPLGAGGAQ TPNVTSEGCQ IIHPPWEGGI RYRGLTRDQV KAINFLPVDY
EIEYVCRGER EVVGPKVRKC LANGSWTDMD TPSRCVRICS KSYLTLENGK VFLTGGDLPA
LDGARVDFRC DPDFHLVGSS RSICSQGQWS TPKPHCQVNR TPHSERRAVY IGALFPMSGG
WPGGQACQPA VEMALEDVNS RRDILPDYEL KLIHHDSKCD PGQATKYLYE LLYNDPIKII
LMPGCSSVST LVAEAARMWN LIVLSYGSSS PALSNRQRFP TFFRTHPSAT LHNPTRVKLF
EKWGWKKIAT IQQTTEVFTS TLDDLEERVK EAGIEITFRQ SFFSDPAVPV KNLKRQDARI
IVGLFYETEA RKVFCEVYKE RLFGKKYVWF LIGWYADNWF KTYDPSINCT VEEMTEAVEG
HITTEIVMLN PANTRSISNM TSQEFVEKLT KRLKRHPEET GGFQEAPLAY DAIWALALAL
NKTSGGGGRS GVRLEDFNYN NQTITDQIYR AMNSSSFEGV SGHVVFDASG SRMAWTLIEQ
LQGGSYKKIG YYDSTKDDLS WSKTDKWIGG SPPADQTLVI KTFRFLSQKL FISVSVLSSL
GIVLAVVCLS FNIYNSHVRY IQNSQPNLNN LTAVGCSLAL AAVFPLGLDG YHIGRSQFPF
VCQARLWLLG LGFSLGYGSM FTKIWWVHTV FTKKEEKKEW RKTLEPWKLY ATVGLLVGMD
ILTLAIWQIV DPLHRTIETF AKEEPKEDID VSILPQLEHC SSKKMNTWLG IFYGYKGLLL
LLGIFLAYET KSVSTEKIND HRAVGMAIYN VAVLCLITAP VTMILSSQQD AAFAFASLAI
VFSSYITLVV LFVPKMRRLI TRGEWQSEAQ DTMKTGSSTN NNEEEKSRLL EKENRELEKI
IAEKEERVSE LRHQLQSRQQ IRSRRHPPTP PDPSGGLPRG PSEPPDRLSC DGSRVHLLYK
