ID   GABR2_RAT               Reviewed;         940 AA.
AC   O88871; Q9JK36; Q9QWU2;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Gamma-aminobutyric acid type B receptor subunit 2;
DE            Short=GABA-B receptor 2;
DE            Short=GABA-B-R2;
DE            Short=GABA-BR2;
DE            Short=GABABR2;
DE            Short=Gb2;
DE   AltName: Full=G-protein coupled receptor 51;
DE   Flags: Precursor;
GN   Name=Gabbr2; Synonyms=Gpr51;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH GABBR1, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Hypothalamus {ECO:0000303|PubMed:9872315};
RX   PubMed=9872315; DOI=10.1038/25348;
RA   Jones K.A., Borowsky B., Tamm J.A., Craig D.A., Durkin M.M., Dai M.,
RA   Yao W.-J., Johnson M., Gunwaldsen C.A., Huang L.-Y., Tang C., Shen Q.,
RA   Salon J.A., Morse K., Laz T., Smith K.E., Nagarathnam D., Noble S.A.,
RA   Branchek T.A., Gerald C.;
RT   "GABA(B) receptors function as a heteromeric assembly of the subunits
RT   GABA(B)R1 and GABA(B)R2.";
RL   Nature 396:674-679(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH GABBR1,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Brain cortex, and Cerebellum {ECO:0000303|PubMed:9872317};
RX   PubMed=9872317; DOI=10.1038/25360;
RA   Kaupmann K., Malitschek B., Schuler V., Heid J., Froestl W., Beck P.,
RA   Mosbacher J., Bischoff S., Kulik A., Shigemoto R., Karschin A., Bettler B.;
RT   "GABA-B receptor subtypes assemble into functional heteromeric complexes.";
RL   Nature 396:683-687(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain cortex {ECO:0000303|PubMed:10727622};
RX   PubMed=10727622; DOI=10.1016/s0006-8993(00)01958-2;
RA   Clark J.A., Mezey E., Lam A.S., Bonner T.I.;
RT   "Distribution of the GABA(B) receptor subunit gb2 in rat CNS.";
RL   Brain Res. 860:41-52(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Hypothalamus {ECO:0000303|Ref.4};
RA   Borowsky B., Laz T., Gerald C.;
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION.
RX   PubMed=10658574; DOI=10.1016/s0968-0896(99)00214-x;
RA   Belley M., Sullivan R., Reeves A., Evans J.F., O'Neill G.P., Ng G.Y.K.;
RT   "Synthesis of the nanomolar photoaffinity GABA(B) receptor ligand CGP 71872
RT   reveals diversity in the tissue distribution of GABA(B) receptor forms.";
RL   Bioorg. Med. Chem. 7:2697-2704(1999).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=Wistar; TISSUE=Hippocampus;
RX   PubMed=10457184; DOI=10.1046/j.1460-9568.1999.00704.x;
RA   Pfaff T., Malitschek B., Kaupmann K., Prezeau L., Pin J.-P., Bettler B.,
RA   Karschin A.;
RT   "Alternative splicing generates a novel isoform of the rat metabotropic
RT   GABA(B)R1 receptor.";
RL   Eur. J. Neurosci. 11:2874-2882(1999).
RN   [7]
RP   FUNCTION.
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   [8]
RP   FUNCTION, INTERACTION WITH GABBR1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND VARIANTS PRO-19 INS AND TYR-337.
RC   TISSUE=Hippocampus {ECO:0000303|PubMed:9872744};
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   [9]
RP   FUNCTION, AND INTERACTION WITH ATF4.
RX   PubMed=10924501; DOI=10.1074/jbc.m002727200;
RA   Nehring R.B., Horikawa H.P.M., El Far O., Kneussel M., Brandstatter J.H.,
RA   Stamm S., Wischmeyer E., Betz H., Karschin A.;
RT   "The metabotropic GABAB receptor directly interacts with the activating
RT   transcription factor 4.";
RL   J. Biol. Chem. 275:35185-35191(2000).
RN   [10]
RP   SUBCELLULAR LOCATION.
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   [11]
RP   INTERACTION WITH KCTD8; KCTD12 AND KCTD16.
RX   PubMed=20400944; DOI=10.1038/nature08964;
RA   Schwenk J., Metz M., Zolles G., Turecek R., Fritzius T., Bildl W.,
RA   Tarusawa E., Kulik A., Unger A., Ivankova K., Seddik R., Tiao J.Y.,
RA   Rajalu M., Trojanova J., Rohde V., Gassmann M., Schulte U., Fakler B.,
RA   Bettler B.;
RT   "Native GABA(B) receptors are heteromultimers with a family of auxiliary
RT   subunits.";
RL   Nature 465:231-235(2010).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-818 AND SER-883, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [13]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-388, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24090084; DOI=10.1021/pr400783j;
RA   Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA   Graham M.E., Packer N.H., Cordwell S.J.;
RT   "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT   heterogeneity.";
RL   J. Proteome Res. 12:5791-5800(2013).
CC   -!- FUNCTION: Component of a heterodimeric G-protein coupled receptor for
CC       GABA, formed by GABBR1 and GABBR2 (PubMed:9872315, PubMed:9872317,
CC       PubMed:9872744). Within the heterodimeric GABA receptor, only GABBR1
CC       seems to bind agonists, while GABBR2 mediates coupling to G proteins
CC       (PubMed:9872317, PubMed:10658574). Ligand binding causes a conformation
CC       change that triggers signaling via guanine nucleotide-binding proteins
CC       (G proteins) and modulates the activity of down-stream effectors, such
CC       as adenylate cyclase (PubMed:9872315, PubMed:9872317, Ref.4,
CC       PubMed:10075644, PubMed:9872744, PubMed:10924501). Signaling inhibits
CC       adenylate cyclase, stimulates phospholipase A2, activates potassium
CC       channels, inactivates voltage-dependent calcium-channels and modulates
CC       inositol phospholipid hydrolysis (PubMed:9872315, PubMed:9872317,
CC       PubMed:10457184, PubMed:9872744, PubMed:10924501). Plays a critical
CC       role in the fine-tuning of inhibitory synaptic transmission
CC       (PubMed:9872317, PubMed:10457184, PubMed:9872744). Pre-synaptic GABA
CC       receptor inhibits neurotransmitter release by down-regulating high-
CC       voltage activated calcium channels, whereas postsynaptic GABA receptor
CC       decreases neuronal excitability by activating a prominent inwardly
CC       rectifying potassium (Kir) conductance that underlies the late
CC       inhibitory postsynaptic potentials (PubMed:9872744, PubMed:10924501).
CC       Not only implicated in synaptic inhibition but also in hippocampal
CC       long-term potentiation, slow wave sleep, muscle relaxation and
CC       antinociception (By similarity). {ECO:0000250|UniProtKB:O75899,
CC       ECO:0000269|PubMed:10075644, ECO:0000269|PubMed:10457184,
CC       ECO:0000269|PubMed:10658574, ECO:0000269|PubMed:10924501,
CC       ECO:0000269|PubMed:9872315, ECO:0000269|PubMed:9872317,
CC       ECO:0000269|PubMed:9872744, ECO:0000269|Ref.4}.
CC   -!- SUBUNIT: Heterodimer of GABBR1 and GABBR2 (PubMed:9872315,
CC       PubMed:9872317, PubMed:9872744). Homodimers may form, but are inactive
CC       (PubMed:9872317). Interacts (via C-terminus) with ATF4 (via leucine
CC       zipper domain) (PubMed:10924501). Interacts with KCTD8, KCTD12 and
CC       KCTD16; this interaction determines the pharmacology and kinetics of
CC       the receptor response, the KCTD proteins markedly accelerating the
CC       GABA-B response, although to different extents (PubMed:20400944).
CC       {ECO:0000269|PubMed:10924501, ECO:0000269|PubMed:20400944,
CC       ECO:0000269|PubMed:9872317, ECO:0000269|PubMed:9872744}.
CC   -!- INTERACTION:
CC       O88871; P27732: Cacna1d; NbExp=6; IntAct=EBI-7090239, EBI-8072674;
CC       O88871; Q9Z0U4: Gabbr1; NbExp=8; IntAct=EBI-7090239, EBI-7090268;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9872315,
CC       ECO:0000269|PubMed:9872317, ECO:0000305|PubMed:10457184}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:9872317}. Postsynaptic cell
CC       membrane {ECO:0000269|PubMed:9872317}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:9872317}. Perikaryon {ECO:0000269|PubMed:14718537}.
CC       Cell projection, dendrite {ECO:0000269|PubMed:10457184}.
CC       Note=Coexpression of GABBR1 and GABBR2 is required for GABBR1
CC       maturation and transport to the plasma membrane (PubMed:10457184). In
CC       contrast, GABBR2 does not depend on GABBR1 for transport to the cell
CC       membrane. {ECO:0000305|PubMed:10457184}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in areas of the brain including
CC       thalamic nuclei, the hippocampus, cerebellar Purkinje cells and the
CC       medial habenula, and moderately expressed in the cerebral cortex,
CC       certain anterioventral thalamic nuclei, dorsal medial hypothalamic
CC       nucleus and suprachiasmatic nuclei (PubMed:9872315, PubMed:9872317,
CC       PubMed:10727622, PubMed:9872744). Also weakly expressed in the testis
CC       (PubMed:9872744). {ECO:0000269|PubMed:10727622,
CC       ECO:0000269|PubMed:9872315, ECO:0000269|PubMed:9872317,
CC       ECO:0000269|PubMed:9872744}.
CC   -!- DEVELOPMENTAL STAGE: On the day of birth, expressed in the regions of
CC       the brain including hippocampus, thalamic nuclei and cortex
CC       (PubMed:9872744). Abundant in brain cortex and cerebellum throughout
CC       postnatal development whereas its expression in spinal cord gradually
CC       decreases (PubMed:9872317). {ECO:0000269|PubMed:9872317,
CC       ECO:0000269|PubMed:9872744}.
CC   -!- DOMAIN: Alpha-helical parts of the C-terminal intracellular region
CC       mediate heterodimeric interaction with GABA-B receptor 1.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family. GABA-B
CC       receptor subfamily. {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; AF074482; AAD03335.1; -; mRNA.
DR   EMBL; AJ011318; CAA09592.1; -; Genomic_DNA.
DR   EMBL; AF058795; AAC63994.1; -; mRNA.
DR   EMBL; AF109405; AAD03338.1; -; mRNA.
DR   RefSeq; NP_113990.1; NM_031802.1.
DR   AlphaFoldDB; O88871; -.
DR   SMR; O88871; -.
DR   BioGRID; 249797; 6.
DR   ComplexPortal; CPX-404; GABA-B receptor complex.
DR   CORUM; O88871; -.
DR   IntAct; O88871; 4.
DR   MINT; O88871; -.
DR   STRING; 10116.ENSRNOP00000011573; -.
DR   BindingDB; O88871; -.
DR   ChEMBL; CHEMBL2111474; -.
DR   DrugCentral; O88871; -.
DR   GuidetoPHARMACOLOGY; 241; -.
DR   GlyCosmos; O88871; 5 sites, 2 glycans.
DR   GlyGen; O88871; 5 sites, 3 N-linked glycans (1 site).
DR   iPTMnet; O88871; -.
DR   PhosphoSitePlus; O88871; -.
DR   PaxDb; 10116-ENSRNOP00000011573; -.
DR   ABCD; O88871; 2 sequenced antibodies.
DR   GeneID; 83633; -.
DR   KEGG; rno:83633; -.
DR   UCSC; RGD:619864; rat.
DR   AGR; RGD:619864; -.
DR   CTD; 9568; -.
DR   RGD; 619864; Gabbr2.
DR   eggNOG; KOG1055; Eukaryota.
DR   InParanoid; O88871; -.
DR   OrthoDB; 2970339at2759; -.
DR   PhylomeDB; O88871; -.
DR   TreeFam; TF313965; -.
DR   Reactome; R-RNO-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   Reactome; R-RNO-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR   Reactome; R-RNO-977444; GABA B receptor activation.
DR   Reactome; R-RNO-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR   PRO; PR:O88871; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:1902712; C:G protein-coupled GABA receptor complex; IPI:ComplexPortal.
DR   GO; GO:0038039; C:G protein-coupled receptor heterodimeric complex; ISS:UniProtKB.
DR   GO; GO:1902710; C:GABA receptor complex; ISO:RGD.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0043005; C:neuron projection; ISO:RGD.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
DR   GO; GO:0004965; F:G protein-coupled GABA receptor activity; IDA:RGD.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:ComplexPortal.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IDA:RGD.
DR   GO; GO:0150099; P:neuron-glial cell signaling; IGI:ARUK-UCL.
DR   GO; GO:0051932; P:synaptic transmission, GABAergic; NAS:ComplexPortal.
DR   CDD; cd15294; 7tmC_GABA-B-R2; 1.
DR   CDD; cd06366; PBP1_GABAb_receptor; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR041689; GBR2_CC.
DR   InterPro; IPR002455; GPCR3_GABA-B.
DR   InterPro; IPR000337; GPCR_3.
DR   InterPro; IPR017978; GPCR_3_C.
DR   InterPro; IPR017979; GPCR_3_CS.
DR   InterPro; IPR002457; GPCR_3_GABA_rcpt_B2.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   PANTHER; PTHR10519; GABA-B RECEPTOR; 1.
DR   PANTHER; PTHR10519:SF20; GAMMA-AMINOBUTYRIC ACID TYPE B RECEPTOR SUBUNIT 2; 1.
DR   Pfam; PF00003; 7tm_3; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF18455; GBR2_CC; 1.
DR   PRINTS; PR01178; GABAB2RECPTR.
DR   PRINTS; PR01176; GABABRECEPTR.
DR   PRINTS; PR00248; GPCRMGR.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 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   Cell membrane; Cell projection; Coiled coil; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..940
FT                   /note="Gamma-aminobutyric acid type B receptor subunit 2"
FT                   /id="PRO_0000012953"
FT   TOPO_DOM        41..482
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        483..503
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        504..521
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        522..542
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        543..550
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        551..571
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        572..596
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        597..617
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        618..653
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        654..674
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        675..690
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        691..711
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        712..719
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        720..740
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        741..940
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          762..789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          780..818
FT                   /evidence="ECO:0000255"
FT   MOD_RES         775
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80T41"
FT   MOD_RES         778
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80T41"
FT   MOD_RES         818
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         883
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         892
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80T41"
FT   MOD_RES         912
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80T41"
FT   MOD_RES         915
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80T41"
FT   MOD_RES         919
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80T41"
FT   MOD_RES         923
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80T41"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        388
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007744|PubMed:24090084"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        452
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        107..134
FT                   /evidence="ECO:0000250"
FT   DISULFID        236..265
FT                   /evidence="ECO:0000250"
FT   DISULFID        264..301
FT                   /evidence="ECO:0000250"
FT   VARIANT         19
FT                   /note="P -> PP"
FT                   /evidence="ECO:0000269|PubMed:9872744"
FT   VARIANT         19
FT                   /note="P -> R"
FT   VARIANT         337
FT                   /note="F -> Y"
FT                   /evidence="ECO:0000269|PubMed:9872744"
FT   CONFLICT        343
FT                   /note="S -> T (in Ref. 2; CAA09592)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   940 AA;  105751 MW;  77BB42D833C7505D CRC64;
     MASPPSSGQP RPPPPPPPPA RLLLPLLLSL LLWLAPGAWG WTRGAPRPPP SSPPLSIMGL
     MPLTKEVAKG SIGRGVLPAV ELAIEQIRNE SLLRPYFLDL RLYDTECDNA KGLKAFYDAI
     KYGPNHLMVF GGVCPSVTSI IAESLQGWNL VQLSFAATTP VLADKKKYPY FFRTVPSDNA
     VNPAILKLLK HFRWRRVGTL TQDVQRFSEV RNDLTGVLYG EDIEISDTES FSNDPCTSVK
     KLKGNDVRII LGQFDQNMAA KVFCCAFEES MFGSKYQWII PGWYEPAWWE QVHVEANSSR
     CLRRSLLAAM EGYIGVDFEP LSSKQIKTIS GKTPQQFERE YNSKRSGVGP SKFHGYAYDG
     IWVIAKTLQR AMETLHASSR HQRIQDFNYT DHTLGKIILN AMNETNFFGV TGQVVFRNGE
     RMGTIKFTQF QDSREVKVGE YNAVADTLEI INDTIRFQGS EPPKDKTIIL EQLRKISLPL
     YSILSALTIL GMIMASAFLF FNIKNRNQKL IKMSSPYMNN LIILGGMLSY ASIFLFGLDG
     SFVSEKTFET LCTVRTWILT VGYTTAFGAM FAKTWRVHAI FKNVKMKKKI IKDQKLLVIV
     GGMLLIDLCI LICWQAVDPL RRTVERYSME PDPAGRDISI RPLLEHCENT HMTIWLGIVY
     AYKGLLMLFG CFLAWETRNV SIPALNDSKY IGMSVYNVGI MCIIGAAVSF LTRDQPNVQF
     CIVALVIIFC STITLCLVFV PKLITLRTNP DAATQNRRFQ FTQNQKKEDS KTSTSVTSVN
     QASTSRLEGL QSENHRLRMK ITELDKDLEE VTMQLQDTPE KTTYIKQNHY QELNDILSLG
     NFTESTDGGK AILKNHLDQN PQLQWNTTEP SRTCKDPIED INSPEHIQRR LSLQLPILHH
     AYLPSIGGVD ASCVSPCVSP TASPRHRHVP PSFRVMVSGL
//