POPD1_MOUSE
ID POPD1_MOUSE Reviewed; 358 AA.
AC Q9ES83; A2RS91; Q8C8L3;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Blood vessel epicardial substance {ECO:0000312|MGI:MGI:1346013};
DE Short=mBVES;
DE AltName: Full=Popeye domain-containing protein 1;
DE Short=Popeye protein 1;
GN Name=Bves {ECO:0000312|MGI:MGI:1346013};
GN Synonyms=Pop1 {ECO:0000312|MGI:MGI:1346013},
GN Popdc1 {ECO:0000312|MGI:MGI:1346013};
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], POSSIBLE FUNCTION, DEVELOPMENTAL STAGE, AND
RP TISSUE SPECIFICITY.
RX PubMed=10882522; DOI=10.1006/dbio.2000.9751;
RA Andree B., Hillemann T., Kessler-Icekson G., Schmitt-John T., Jockusch H.,
RA Arnold H.-H., Brand T.;
RT "Isolation and characterization of the novel popeye gene family expressed
RT in skeletal muscle and heart.";
RL Dev. Biol. 223:371-382(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-358.
RX PubMed=10208750; DOI=10.1006/dbio.1999.9246;
RA Reese D.E., Zavaljevski M., Streiff N.L., Bader D.;
RT "bves: a novel gene expressed during coronary blood vessel development.";
RL Dev. Biol. 209:159-171(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 259-358.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=11839816; DOI=10.1128/mcb.22.5.1504-1512.2002;
RA Andree B., Fleige A., Arnold H.H., Brand T.;
RT "Mouse Pop1 is required for muscle regeneration in adult skeletal muscle.";
RL Mol. Cell. Biol. 22:1504-1512(2002).
RN [6]
RP FUNCTION, INTERACTION WITH TJP1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16188940; DOI=10.1242/jcs.02588;
RA Osler M.E., Chang M.S., Bader D.M.;
RT "Bves modulates epithelial integrity through an interaction at the tight
RT junction.";
RL J. Cell Sci. 118:4667-4678(2005).
RN [7]
RP FUNCTION, INTERACTION WITH ARHGEF25, AND TISSUE SPECIFICITY.
RX PubMed=18541910; DOI=10.1073/pnas.0802345105;
RA Smith T.K., Hager H.A., Francis R., Kilkenny D.M., Lo C.W., Bader D.M.;
RT "Bves directly interacts with GEFT, and controls cell shape and movement
RT through regulation of Rac1/Cdc42 activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8298-8303(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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 [9]
RP FUNCTION, INTERACTION WITH VAMP3, AND SUBCELLULAR LOCATION.
RX PubMed=20057356; DOI=10.1038/emboj.2009.379;
RA Hager H.A., Roberts R.J., Cross E.E., Proux-Gillardeaux V., Bader D.M.;
RT "Identification of a novel Bves function: regulation of vesicular
RT transport.";
RL EMBO J. 29:532-545(2010).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, CAMP-BINDING, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ASP-200; PRO-202; GLU-203 AND VAL-217.
RX PubMed=22354168; DOI=10.1172/jci59410;
RA Froese A., Breher S.S., Waldeyer C., Schindler R.F., Nikolaev V.O.,
RA Rinne S., Wischmeyer E., Schlueter J., Becher J., Simrick S., Vauti F.,
RA Kuhtz J., Meister P., Kreissl S., Torlopp A., Liebig S.K., Laakmann S.,
RA Mueller T.D., Neumann J., Stieber J., Ludwig A., Maier S.K., Decher N.,
RA Arnold H.H., Kirchhof P., Fabritz L., Brand T.;
RT "Popeye domain containing proteins are essential for stress-mediated
RT modulation of cardiac pacemaking in mice.";
RL J. Clin. Invest. 122:1119-1130(2012).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH CAV3, AND SUBCELLULAR
RP LOCATION.
RX PubMed=24066022; DOI=10.1371/journal.pone.0071100;
RA Alcalay Y., Hochhauser E., Kliminski V., Dick J., Zahalka M.A., Parnes D.,
RA Schlesinger H., Abassi Z., Shainberg A., Schindler R.F., Brand T.,
RA Kessler-Icekson G.;
RT "Popeye domain containing 1 (Popdc1/Bves) is a caveolae-associated protein
RT involved in ischemia tolerance.";
RL PLoS ONE 8:E71100-E71100(2013).
RN [12]
RP INTERACTION WITH KCNK2.
RX PubMed=26642364; DOI=10.1172/jci79562;
RA Schindler R.F., Scotton C., Zhang J., Passarelli C., Ortiz-Bonnin B.,
RA Simrick S., Schwerte T., Poon K.L., Fang M., Rinne S., Froese A.,
RA Nikolaev V.O., Grunert C., Mueller T., Tasca G., Sarathchandra P.,
RA Drago F., Dallapiccola B., Rapezzi C., Arbustini E., Di Raimo F.R.,
RA Neri M., Selvatici R., Gualandi F., Fattori F., Pietrangelo A., Li W.,
RA Jiang H., Xu X., Bertini E., Decher N., Wang J., Brand T., Ferlini A.;
RT "POPDC1S201F causes muscular dystrophy and arrhythmia by affecting protein
RT trafficking.";
RL J. Clin. Invest. 126:239-253(2016).
CC -!- FUNCTION: Cell adhesion molecule involved in the establishment and/or
CC maintenance of cell integrity. Involved in the formation and regulation
CC of the tight junction (TJ) paracellular permeability barrier in
CC epithelial cells (PubMed:16188940). Plays a role in VAMP3-mediated
CC vesicular transport and recycling of different receptor molecules
CC through its interaction with VAMP3 (PubMed:20057356). Plays a role in
CC the regulation of cell shape and movement by modulating the Rho-family
CC GTPase activity through its interaction with ARHGEF25/GEFT
CC (PubMed:18541910). Induces primordial adhesive contact and aggregation
CC of epithelial cells in a Ca(2+)-independent manner. Also involved in
CC striated muscle regeneration and repair and in the regulation of cell
CC spreading (PubMed:11839816). Important for the maintenance of cardiac
CC function. Plays a regulatory function in heart rate dynamics mediated,
CC at least in part, through cAMP-binding and, probably, by increasing
CC cell surface expression of the potassium channel KCNK2 and enhancing
CC current density (PubMed:26642364). Is a caveolae-associated protein
CC important for the preservation of caveolae structural and functional
CC integrity as well as for heart protection against ischemia injury
CC (PubMed:24066022). {ECO:0000250|UniProtKB:Q8NE79,
CC ECO:0000269|PubMed:10882522, ECO:0000269|PubMed:11839816,
CC ECO:0000269|PubMed:16188940, ECO:0000269|PubMed:18541910,
CC ECO:0000269|PubMed:20057356, ECO:0000269|PubMed:22354168,
CC ECO:0000269|PubMed:24066022}.
CC -!- SUBUNIT: Homodimer. Homodimerization requires the C-terminus
CC cytoplasmic region (By similarity). Interacts (via the C-terminus
CC cytoplasmic tail) with TJP1. Interacts (via the C-terminus cytoplasmic
CC tail) with ARHGEF25/GEFT (via the DH domain). Interacts (via the C-
CC terminus cytoplasmic tail) with VAMP3. Interacts with KCNK2; the
CC interaction enhances KCNK2 surface expression and is inhibited by cAMP
CC (PubMed:22354168, PubMed:26642364). Interacts with CAV3
CC (PubMed:24066022). {ECO:0000250|UniProtKB:Q9DG23,
CC ECO:0000269|PubMed:16188940, ECO:0000269|PubMed:18541910,
CC ECO:0000269|PubMed:20057356, ECO:0000269|PubMed:24066022,
CC ECO:0000269|PubMed:26642364}.
CC -!- INTERACTION:
CC Q9ES83; Q9CWR0: Arhgef25; NbExp=2; IntAct=EBI-7705661, EBI-15708245;
CC Q9ES83; P63025: Vamp3; Xeno; NbExp=3; IntAct=EBI-7705661, EBI-7705696;
CC -!- SUBCELLULAR LOCATION: Lateral cell membrane
CC {ECO:0000250|UniProtKB:Q8NE79}. Cell junction, tight junction
CC {ECO:0000269|PubMed:16188940}. Membrane {ECO:0000269|PubMed:22354168};
CC Multi-pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:24066022}. Membrane, caveola
CC {ECO:0000269|PubMed:24066022}. Note=Its movement from the cytoplasm to
CC membrane is an early event occurring concurrently with cell-cell
CC contact. Detected at cell-cell contact but never observed at the free
CC surface of epithelial cells (By similarity). Colocalizes in epithelial
CC cells with OCLN and TJP1 in an apical-lateral position within the z
CC axis. Colocalizes with VAMP3 at the cell-cell contact in cardiac and
CC skeletal muscle. {ECO:0000269|PubMed:16188940,
CC ECO:0000269|PubMed:20057356}.
CC -!- TISSUE SPECIFICITY: Expressed in epithelial cells, skeletal muscle,
CC heart and intestinal smooth muscle (at protein level). Expressed in
CC fetal and adult heart and skeletal muscle.
CC {ECO:0000269|PubMed:10882522, ECO:0000269|PubMed:11839816,
CC ECO:0000269|PubMed:16188940, ECO:0000269|PubMed:18541910}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the mesoderm of the cardiac crescent
CC at 9.5 dpc. Expressed in cardiac myocytes of the sinoatrial compartment
CC and some restricted areas of the dorsal part of the ventricle chambers
CC at 10.5 dpc and 12.5 dpc. Expressed in branchial arches, myotome and in
CC a posterior domain in the limb at 10.5 dpc. Expressed in the heart,
CC mainly in the compact layer myocardium, peridigital mesenchyme, the
CC somites of the tail bud, the smooth muscle cells of the trachea and the
CC developing bronchial tree, the smooth muscle cells lining the digestive
CC tract, the dorsal root ganglia and the pancreas anlage at 13.5 dpc (at
CC protein level). Expressed in the sinoatrial compartment and some
CC restricted areas in the dorsal part of the ventricle at 9.5 dpc, 10.5
CC dpc and 11.5 dpc. At 12.5 dpc, expression was observed in the ventral
CC half of the ventricle where it was limited to the subepicardial compact
CC layer. {ECO:0000269|PubMed:10882522, ECO:0000269|PubMed:11839816}.
CC -!- DISRUPTION PHENOTYPE: Skeletal muscle regeneration appears to be less
CC efficient and delayed (PubMed:11839816). Knockout mice are deficient to
CC adapt heart rate to physiological stress, this deficiency develops in
CC older mice. They show severe sinus node dysfunction with long pauses
CC and intercurrent periods of normal synus rhythm. The sinus node
CC structure is abnormal with a loss of pacemaker tissue from the inferior
CC part of the sinus node and a compact structure of the superior sinus
CC node (PubMed:22354168). They have inpaired functional recovery after
CC ischemia/reperfusion injury (PubMed:24066022).
CC {ECO:0000269|PubMed:11839816, ECO:0000269|PubMed:22354168,
CC ECO:0000269|PubMed:24066022}.
CC -!- SIMILARITY: Belongs to the popeye family. {ECO:0000305}.
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DR EMBL; AF204174; AAG23407.1; -; mRNA.
DR EMBL; AF124510; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC132018; AAI32019.1; -; mRNA.
DR EMBL; BC132044; AAI32045.1; -; mRNA.
DR EMBL; AK046765; BAC32859.1; -; mRNA.
DR CCDS; CCDS23828.1; -.
DR RefSeq; NP_077247.1; NM_024285.2.
DR RefSeq; XP_006512799.1; XM_006512736.3.
DR RefSeq; XP_006512800.1; XM_006512737.2.
DR AlphaFoldDB; Q9ES83; -.
DR SMR; Q9ES83; -.
DR DIP; DIP-46118N; -.
DR IntAct; Q9ES83; 3.
DR MINT; Q9ES83; -.
DR STRING; 10090.ENSMUSP00000093382; -.
DR GlyGen; Q9ES83; 2 sites.
DR iPTMnet; Q9ES83; -.
DR PhosphoSitePlus; Q9ES83; -.
DR MaxQB; Q9ES83; -.
DR PaxDb; Q9ES83; -.
DR PeptideAtlas; Q9ES83; -.
DR PRIDE; Q9ES83; -.
DR ProteomicsDB; 289867; -.
DR Antibodypedia; 3082; 219 antibodies from 31 providers.
DR DNASU; 23828; -.
DR Ensembl; ENSMUST00000095715; ENSMUSP00000093382; ENSMUSG00000071317.
DR GeneID; 23828; -.
DR KEGG; mmu:23828; -.
DR UCSC; uc007ezz.1; mouse.
DR CTD; 11149; -.
DR MGI; MGI:1346013; Bves.
DR VEuPathDB; HostDB:ENSMUSG00000071317; -.
DR eggNOG; ENOG502QRV2; Eukaryota.
DR GeneTree; ENSGT00390000002563; -.
DR HOGENOM; CLU_048494_0_0_1; -.
DR InParanoid; Q9ES83; -.
DR OMA; TSCQEWE; -.
DR OrthoDB; 1369469at2759; -.
DR PhylomeDB; Q9ES83; -.
DR TreeFam; TF326644; -.
DR BioGRID-ORCS; 23828; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q9ES83; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9ES83; protein.
DR Bgee; ENSMUSG00000071317; Expressed in interventricular septum and 116 other tissues.
DR Genevisible; Q9ES83; MM.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0031253; C:cell projection membrane; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR GO; GO:0030552; F:cAMP binding; IDA:MGI.
DR GO; GO:0005198; F:structural molecule activity; ISS:UniProtKB.
DR GO; GO:0060973; P:cell migration involved in heart development; IMP:BHF-UCL.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR GO; GO:0040017; P:positive regulation of locomotion; IDA:UniProtKB.
DR GO; GO:0001921; P:positive regulation of receptor recycling; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB.
DR GO; GO:2001135; P:regulation of endocytic recycling; IMP:BHF-UCL.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IGI:MGI.
DR GO; GO:0002931; P:response to ischemia; IMP:UniProtKB.
DR GO; GO:0060931; P:sinoatrial node cell development; IMP:MGI.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISS:UniProtKB.
DR GO; GO:0051146; P:striated muscle cell differentiation; IBA:GO_Central.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR GO; GO:0048278; P:vesicle docking; IMP:BHF-UCL.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA:UniProtKB.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR006916; Popeye_prot.
DR PANTHER; PTHR12101; PTHR12101; 1.
DR Pfam; PF04831; Popeye; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
PE 1: Evidence at protein level;
KW cAMP; cAMP-binding; Cell adhesion; Cell junction; Cell membrane;
KW Developmental protein; Glycoprotein; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Tight junction; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..358
FT /note="Blood vessel epicardial substance"
FT /id="PRO_0000046792"
FT TOPO_DOM 1..48
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 93..115
FT /note="Required for interaction with CAV3"
FT /evidence="ECO:0000269|PubMed:24066022"
FT REGION 136..186
FT /note="Required for interaction with KCNK2"
FT /evidence="ECO:0000250|UniProtKB:Q8NE79"
FT REGION 313..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3BCU4"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 200
FT /note="D->A: Almost abolishes cAMP-binding. Interaction
FT with KCNK2 is not inhibited by cAMP."
FT /evidence="ECO:0000269|PubMed:22354168"
FT MUTAGEN 202
FT /note="P->A: No effect on cAMP-binding."
FT /evidence="ECO:0000269|PubMed:22354168"
FT MUTAGEN 203
FT /note="E->A: Decreases cAMP-binding."
FT /evidence="ECO:0000269|PubMed:22354168"
FT MUTAGEN 217
FT /note="V->F: Decreases cAMP-binding."
FT /evidence="ECO:0000269|PubMed:22354168"
SQ SEQUENCE 358 AA; 41016 MW; B92F1942F1713027 CRC64;
MNSTESIPLA QSTVAGFTSE LESLTPVPSN ETTCENWREI HHLVFHVANV CFAVGLLIPT
TLHLHMILLR VMLSLGCTLY VVWATLYRCA LDVMIWNSVF LGINILHLSY LLYKKRPVKI
EKELGGVYHR LFEPLRVPPD LFRRLTGQFC MIQTLKRGQV YATEDKTSVD DRLSILLKGR
MKVSYRGHFL HNIYPCAFID SPEFRSTQMH KGEKFQVTIV ADDNCRFLCW SRERLTYFLE
SEPFLYEIFR YLIGKDITNK LYSLNDPTLN DKKVKKLEPQ MSLCTQISML EMRNSITSSS
DGEDGLHHFL RGSSSTASLP MSSPQQRASA KMKPIEEGVE DDDEVFVSPD ALKVHQLP
