OAMB_DROME
ID OAMB_DROME Reviewed; 645 AA.
AC Q7JQF1; O61730; Q9VDJ6;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Octopamine receptor Oamb {ECO:0000305};
DE AltName: Full=Octopamine receptor in mushroom bodies {ECO:0000303|PubMed:9570796};
GN Name=Oamb {ECO:0000312|FlyBase:FBgn0024944};
GN Synonyms=oa1 {ECO:0000303|PubMed:15816867};
GN ORFNames=CG3856 {ECO:0000312|FlyBase:FBgn0024944};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAQ22572.1};
RN [1] {ECO:0000312|EMBL:AAC17442.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9570796; DOI=10.1523/jneurosci.18-10-03650.1998;
RA Han K.A., Millar N.S., Davis R.L.;
RT "A novel octopamine receptor with preferential expression in Drosophila
RT mushroom bodies.";
RL J. Neurosci. 18:3650-3658(1998).
RN [2] {ECO:0000312|EMBL:CAB38025.1, ECO:0000312|EMBL:CAB38026.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C), FUNCTION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15816867; DOI=10.1111/j.1471-4159.2005.03034.x;
RA Balfanz S., Struenker T., Frings S., Baumann A.;
RT "A family of octopamine receptors that specifically induce cyclic AMP
RT production or Ca2+ release in Drosophila melanogaster.";
RL J. Neurochem. 93:440-451(2005).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5] {ECO:0000312|EMBL:AAQ22572.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAQ22572.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAQ22572.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=14623240; DOI=10.1016/j.ydbio.2003.07.018;
RA Lee H.G., Seong C.S., Kim Y.C., Davis R.L., Han K.A.;
RT "Octopamine receptor OAMB is required for ovulation in Drosophila
RT melanogaster.";
RL Dev. Biol. 264:179-190(2003).
RN [7] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19262750; DOI=10.1371/journal.pone.0004716;
RA Lee H.G., Rohila S., Han K.A.;
RT "The octopamine receptor OAMB mediates ovulation via Ca2+/calmodulin-
RT dependent protein kinase II in the Drosophila oviduct epithelium.";
RL PLoS ONE 4:E4716-E4716(2009).
RN [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20223202; DOI=10.1016/j.neuron.2010.01.032;
RA Crocker A., Shahidullah M., Levitan I.B., Sehgal A.;
RT "Identification of a neural circuit that underlies the effects of
RT octopamine on sleep:wake behavior.";
RL Neuron 65:670-681(2010).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=23055498; DOI=10.1523/jneurosci.0517-12.2012;
RA Zhou C., Huang H., Kim S.M., Lin H., Meng X., Han K.A., Chiang A.S.,
RA Wang J.W., Jiao R., Rao Y.;
RT "Molecular genetic analysis of sexual rejection: roles of octopamine and
RT its receptor OAMB in Drosophila courtship conditioning.";
RL J. Neurosci. 32:14281-14287(2012).
RN [10] {ECO:0000305}
RP FUNCTION.
RX PubMed=23103875; DOI=10.1038/nature11614;
RA Burke C.J., Huetteroth W., Owald D., Perisse E., Krashes M.J., Das G.,
RA Gohl D., Silies M., Certel S., Waddell S.;
RT "Layered reward signalling through octopamine and dopamine in Drosophila.";
RL Nature 492:433-437(2012).
RN [11] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23345239; DOI=10.1523/jneurosci.3042-12.2013;
RA Kim Y.C., Lee H.G., Lim J., Han K.A.;
RT "Appetitive learning requires the alpha1-like octopamine receptor OAMB in
RT the Drosophila mushroom body neurons.";
RL J. Neurosci. 33:1672-1677(2013).
RN [12] {ECO:0000305}
RP FUNCTION.
RX PubMed=24923784; DOI=10.1371/journal.pone.0099732;
RA Luo J., Lushchak O.V., Goergen P., Williams M.J., Naessel D.R.;
RT "Drosophila insulin-producing cells are differentially modulated by
RT serotonin and octopamine receptors and affect social behavior.";
RL PLoS ONE 9:E99732-E99732(2014).
RN [13] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=25743690; DOI=10.1007/s00441-015-2137-4;
RA El-Kholy S., Stephano F., Li Y., Bhandari A., Fink C., Roeder T.;
RT "Expression analysis of octopamine and tyramine receptors in Drosophila.";
RL Cell Tissue Res. 361:669-684(2015).
RN [14] {ECO:0000305}
RP FUNCTION.
RX PubMed=25728694; DOI=10.1016/j.cub.2015.01.036;
RA Huetteroth W., Perisse E., Lin S., Klappenbach M., Burke C., Waddell S.;
RT "Sweet taste and nutrient value subdivide rewarding dopaminergic neurons in
RT Drosophila.";
RL Curr. Biol. 25:751-758(2015).
RN [15] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26473732; DOI=10.1371/journal.pgen.1005604;
RA Deady L.D., Sun J.;
RT "A follicle rupture assay reveals an essential role for follicular
RT adrenergic signaling in Drosophila ovulation.";
RL PLoS Genet. 11:E1005604-E1005604(2015).
CC -!- FUNCTION: Receptor for octopamine (OA) which is a neurotransmitter,
CC neurohormone and neuromodulator in invertebrates (PubMed:9570796,
CC PubMed:15816867). Stimulates intracellular accumulation of cAMP and
CC Ca(2+) following ligand binding (PubMed:9570796, PubMed:15816867).
CC Required for ovulation (PubMed:14623240, PubMed:19262750). Following
CC activation on mature follicle cells by OA, induces activity of the
CC metalloprotease Mmp2 which leads to breakdown of the posterior follicle
CC wall, resulting in ovulation (PubMed:26473732). Ligand binding probably
CC also leads to activation of CamKII which is also required for ovulation
CC (PubMed:19262750). Modulates sleep/wake behavior by acting in neurons
CC of the pars intercerebralis to promote wakefulness (PubMed:20223202).
CC Plays a role in courtship conditioning where the courtship behavior of
CC males rejected by already mated females is inhibited with further
CC females (PubMed:23055498). Required in the mushroom body for appetitive
CC olfactory learning (PubMed:23103875, PubMed:23345239). Specifically
CC conveys the short-term reinforcing effects of sweet taste
CC (PubMed:23103875, PubMed:25728694). In insulin-producing cells of the
CC brain, plays a role in inhibiting transcription of insulin-like peptide
CC Ilp3 (PubMed:24923784). Also plays a role in social behavior by
CC modulating male agression (PubMed:24923784).
CC {ECO:0000269|PubMed:14623240, ECO:0000269|PubMed:15816867,
CC ECO:0000269|PubMed:19262750, ECO:0000269|PubMed:20223202,
CC ECO:0000269|PubMed:23055498, ECO:0000269|PubMed:23103875,
CC ECO:0000269|PubMed:23345239, ECO:0000269|PubMed:24923784,
CC ECO:0000269|PubMed:25728694, ECO:0000269|PubMed:26473732,
CC ECO:0000269|PubMed:9570796}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=C {ECO:0000312|FlyBase:FBgn0024944}; Synonyms=F
CC {ECO:0000312|FlyBase:FBgn0024944}, OA1B {ECO:0000303|PubMed:15816867};
CC IsoId=Q7JQF1-1; Sequence=Displayed;
CC Name=B {ECO:0000312|FlyBase:FBgn0024944}; Synonyms=OA1A
CC {ECO:0000303|PubMed:15816867};
CC IsoId=Q7JQF1-2; Sequence=VSP_058289, VSP_058290, VSP_058291,
CC VSP_058292, VSP_058293, VSP_058294,
CC VSP_058295, VSP_058296, VSP_058297;
CC -!- TISSUE SPECIFICITY: Highly enriched in mushroom body neuropil and in
CC the ellipsoid body (at protein level) (PubMed:9570796). Expressed in
CC oviduct epithelium (at protein level) (PubMed:19262750). Expressed in
CC the adult and larval brain, thoracic and abdominal ganglia, terminal
CC cells of the larval tracheal system, muscle, mature eggs and
CC reproductive system (PubMed:14623240, PubMed:25743690).
CC {ECO:0000269|PubMed:14623240, ECO:0000269|PubMed:19262750,
CC ECO:0000269|PubMed:25743690, ECO:0000269|PubMed:9570796}.
CC -!- DEVELOPMENTAL STAGE: Isoform C: Barely detectable in adult body but is
CC expressed in adult head and third instar larva. Isoform B: Detected in
CC adult head, adult body, pupa, third instar larva, 0-4 hour embryo, 0-18
CC hour embryo and 17-19 hour embryo with lowest expression observed in
CC adult body and 17-19 hour embryo. {ECO:0000269|PubMed:15816867}.
CC -!- DISRUPTION PHENOTYPE: Viable with no gross anatomical defects and
CC females display normal courtship and copulation but are impaired in
CC ovulation (PubMed:14623240). Many mature eggs are retained in the
CC ovaries with mutant females laying significantly fewer eggs and taking
CC much longer to ovulate an egg (PubMed:14623240, PubMed:26473732).
CC Increased sleep with longer sleep bouts during the night and a greater
CC number of sleep bouts during the day (PubMed:20223202). Severely
CC impaired learning in appetitive olfactory conditioning which tests the
CC capacity to learn and remember the odor associated with a sugar reward
CC (PubMed:23345239). {ECO:0000269|PubMed:14623240,
CC ECO:0000269|PubMed:20223202, ECO:0000269|PubMed:23345239,
CC ECO:0000269|PubMed:26473732}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|RuleBase:RU000688}.
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DR EMBL; AF065443; AAC17442.1; -; mRNA.
DR EMBL; AJ007617; CAB38025.1; -; mRNA.
DR EMBL; AJ007618; CAB38026.1; -; mRNA.
DR EMBL; AE014297; AAF55796.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55797.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55798.2; -; Genomic_DNA.
DR EMBL; BT010103; AAQ22572.1; -; mRNA.
DR RefSeq; NP_524669.2; NM_079930.4. [Q7JQF1-2]
DR RefSeq; NP_732541.1; NM_169913.2. [Q7JQF1-1]
DR RefSeq; NP_732542.1; NM_169914.2. [Q7JQF1-1]
DR AlphaFoldDB; Q7JQF1; -.
DR SMR; Q7JQF1; -.
DR STRING; 7227.FBpp0083342; -.
DR GlyGen; Q7JQF1; 2 sites.
DR PaxDb; Q7JQF1; -.
DR DNASU; 43982; -.
DR EnsemblMetazoa; FBtr0083933; FBpp0083341; FBgn0024944. [Q7JQF1-2]
DR EnsemblMetazoa; FBtr0083934; FBpp0083342; FBgn0024944. [Q7JQF1-1]
DR EnsemblMetazoa; FBtr0330713; FBpp0303557; FBgn0024944. [Q7JQF1-1]
DR GeneID; 43982; -.
DR KEGG; dme:Dmel_CG3856; -.
DR UCSC; CG3856-RA; d. melanogaster. [Q7JQF1-1]
DR UCSC; CG3856-RB; d. melanogaster.
DR CTD; 43982; -.
DR FlyBase; FBgn0024944; Oamb.
DR VEuPathDB; VectorBase:FBgn0024944; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000154484; -.
DR InParanoid; Q7JQF1; -.
DR OMA; ICKCFCK; -.
DR PhylomeDB; Q7JQF1; -.
DR BioGRID-ORCS; 43982; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Oamb; fly.
DR GenomeRNAi; 43982; -.
DR PRO; PR:Q7JQF1; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0024944; Expressed in oviduct (Drosophila) and 11 other tissues.
DR ExpressionAtlas; Q7JQF1; baseline and differential.
DR Genevisible; Q9VDJ6; DM.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0008227; F:G protein-coupled amine receptor activity; ISS:FlyBase.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0004989; F:octopamine receptor activity; IDA:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1904068; P:G protein-coupled receptor signaling pathway involved in social behavior; IMP:UniProtKB.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0007612; P:learning; IMP:FlyBase.
DR GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0007211; P:octopamine or tyramine signaling pathway; ISS:FlyBase.
DR GO; GO:0030728; P:ovulation; IMP:FlyBase.
DR GO; GO:0010841; P:positive regulation of circadian sleep/wake cycle, wakefulness; IMP:UniProtKB.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IDA:UniProtKB.
DR GO; GO:1905050; P:positive regulation of metallopeptidase activity; IMP:UniProtKB.
DR GO; GO:0060279; P:positive regulation of ovulation; IMP:UniProtKB.
DR GO; GO:0090328; P:regulation of olfactory learning; IMP:UniProtKB.
DR GO; GO:0060278; P:regulation of ovulation; IMP:FlyBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IMP:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 2.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Behavior; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..645
FT /note="Octopamine receptor Oamb"
FT /id="PRO_0000436178"
FT TOPO_DOM 1..25
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 26..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 57..77
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..94
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 95..115
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 139..159
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..295
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 296..316
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..520
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 521..541
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..551
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 552..572
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 573..645
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 190..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 93..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 340..352
FT /note="KGIGSRFEEQRLT -> PRESGNNRVDESQLI (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15816867"
FT /id="VSP_058289"
FT VAR_SEQ 360..408
FT /note="GSNQQDSMHSNGSTQSTTTTLGTPSPERLSKYATRRLHHHDKIKISVSY ->
FT PCSTPQRTPLSVHSMSSTLSVNSNGGGGGAVASGLGASTEDHLQGGAPKRATSMRVCRQ
FT RHEKVAIKVSF (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15816867"
FT /id="VSP_058290"
FT VAR_SEQ 414..506
FT /note="ISELAGHGDVGHERRQSGNALFAVHYNGTNGRESTESQLYRQQQQHGVASSC
FT YLQVGKGLPELARRQSNTSEAGGSGHSRPANKKMGRRNIKA -> VLDAGQQPQASPHY
FT AVISSANGRRASFKTSLFDIGETTFNLDAAASGPGDLETGLSTTSLSAKKRAGKRSAKF
FT (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15816867"
FT /id="VSP_058291"
FT VAR_SEQ 527..533
FT /note="MFIFCWC -> GFIVCWL (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15816867"
FT /id="VSP_058292"
FT VAR_SEQ 540..553
FT /note="IIRPFCQDCVDPLL -> LIRAFCDHCIQPTV (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15816867"
FT /id="VSP_058293"
FT VAR_SEQ 567
FT /note="V -> I (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15816867"
FT /id="VSP_058294"
FT VAR_SEQ 577..581
FT /note="KDFRF -> NEFRI (in isoform B)"
FT /id="VSP_058295"
FT VAR_SEQ 587..634
FT /note="ICRCFCSRQSVSLKSSRRGSDMSAIRIRARTPSITPSAAAHSFGDESE ->
FT VCRCVCTRSGFRASENFQMIAARALMAPATFHKTISGCSDDGEGVDFS (in
FT isoform B)"
FT /evidence="ECO:0000303|PubMed:15816867"
FT /id="VSP_058296"
FT VAR_SEQ 635..645
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15816867"
FT /id="VSP_058297"
FT CONFLICT 180
FT /note="T -> I (in Ref. 1; AAC17442 and 2; CAB38026)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 645 AA; 71702 MW; F3BDAB7B28CEFD1F CRC64;
MNETECEDLI KSVKWTEPAN LISLAVLEFI NVLVIGGNCL VIAAVFCSNK LRSVTNFFIV
NLAVADLLVG LAVLPFSATW EVFKVWIFGD LWCRIWLAVD VWMCTASILN LCAISLDRYV
AVTRPVTYPS IMSTKKAKSL IAGIWVLSFF ICFPPLVGWK DQKAVIQPTY PKGNHTLYYT
TTMSSSEDGQ LGLDSIKDQG EASLPPSPPH IGNGNAYNPY DPGFAPIDGS AEIRIAAIDS
TSTSTTATTT TTASSSSTTE TEMDLDLLNA PPQNRPQTIS GSCPWKCELT NDRGYVLYSA
LGSFYIPMFV MLFFYWRIYR AAVRTTRAIN QGFKTTKGSK GIGSRFEEQR LTLRIHRGRG
SNQQDSMHSN GSTQSTTTTL GTPSPERLSK YATRRLHHHD KIKISVSYPS SENISELAGH
GDVGHERRQS GNALFAVHYN GTNGRESTES QLYRQQQQHG VASSCYLQVG KGLPELARRQ
SNTSEAGGSG HSRPANKKMG RRNIKAQVKR FRMETKAAKT LAIIVGMFIF CWCPFFTMYI
IRPFCQDCVD PLLFSVLFWL GYCNSAVNPM IYALFSKDFR FAFKRIICRC FCSRQSVSLK
SSRRGSDMSA IRIRARTPSI TPSAAAHSFG DESELHHSEM SNDPR
