POPD1_HUMAN
ID POPD1_HUMAN Reviewed; 360 AA.
AC Q8NE79; A8K1R4; E1P5D8; Q5T550; Q5T551; Q8IWC6; Q9HBV0; Q9UNG6;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Blood vessel epicardial substance {ECO:0000312|HGNC:HGNC:1152};
DE Short=hBVES;
DE AltName: Full=Popeye domain-containing protein 1;
DE Short=Popeye protein 1;
GN Name=BVES {ECO:0000312|HGNC:HGNC:1152};
GN Synonyms=POP1 {ECO:0000312|HGNC:HGNC:1152},
GN POPDC1 {ECO:0000312|HGNC:HGNC:1152};
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], POSSIBLE FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
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].
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-360, AND TISSUE SPECIFICITY.
RX PubMed=10441744; DOI=10.1007/s003359901113;
RA Reese D.E., Bader D.M.;
RT "Cloning and expression of hbves, a novel and highly conserved mRNA
RT expressed in the developing and adult heart and skeletal muscle in the
RT human.";
RL Mamm. Genome 10:913-915(1999).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE 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 [8]
RP INVOLVEMENT IN LGMDR25, VARIANT LGMDR25 PHE-201, FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, INTERACTION WITH KCNK2, AND CAMP-BINDING.
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. Plays a role in the regulation of
CC cell shape and movement by modulating the Rho-family GTPase activity
CC through its interaction with ARHGEF25/GEFT. Induces primordial adhesive
CC contact and aggregation of epithelial cells in a Ca(2+)-independent
CC manner. Also involved in striated muscle regeneration and repair and in
CC the regulation of cell spreading (By similarity). Important for the
CC maintenance of cardiac function. Plays a regulatory function in heart
CC rate dynamics mediated, at least in part, through cAMP-binding and,
CC probably, by increasing cell surface expression of the potassium
CC channel KCNK2 and enhancing current density (PubMed:26642364). Is also
CC a caveolae-associated protein important for the preservation of
CC caveolae structural and functional integrity as well as for heart
CC protection against ischemia injury. {ECO:0000250|UniProtKB:Q5PQZ7,
CC ECO:0000250|UniProtKB:Q9ES83, ECO:0000269|PubMed:16188940,
CC ECO:0000269|PubMed:26642364}.
CC -!- SUBUNIT: Homodimer. Homodimerization requires the C-terminus
CC cytoplasmic region. Interacts (via the C-terminus cytoplasmic tail)
CC with TJP1. Interacts (via the C-terminus cytoplasmic tail) with
CC ARHGEF25/GEFT (via the DH domain). Interacts (via the C-terminus
CC cytoplasmic tail) with VAMP3 (By similarity). Interacts with KCNK2; the
CC interaction enhances KCNK2 surface expression and is inhibited by cAMP
CC (By similarity) (PubMed:26642364). Interacts with CAV3 (By similarity).
CC {ECO:0000250|UniProtKB:Q9DG23, ECO:0000250|UniProtKB:Q9ES83,
CC ECO:0000269|PubMed:26642364}.
CC -!- SUBCELLULAR LOCATION: Lateral cell membrane
CC {ECO:0000269|PubMed:16188940}. Cell junction, tight junction
CC {ECO:0000269|PubMed:16188940}. Membrane {ECO:0000269|PubMed:26642364};
CC Multi-pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:26642364}. Membrane, caveola
CC {ECO:0000250|UniProtKB:Q9ES83}. Note=Colocalizes with VAMP3 at the
CC cell-cell contact in cardiac and skeletal muscle (By similarity). Its
CC movement from the cytoplasm to membrane is an early event occurring
CC concurrently with cell-cell contact. Colocalizes in epithelial cells
CC with OCLN and TJP1 in an apical-lateral position within the z axis.
CC Detected at cell-cell contact but never observed at the free surface of
CC epithelial cells. {ECO:0000250|UniProtKB:Q9ES83}.
CC -!- TISSUE SPECIFICITY: Expressed in epithelial cells (at protein level).
CC Expressed in fetal and adult heart and skeletal muscle.
CC {ECO:0000269|PubMed:10441744, ECO:0000269|PubMed:10882522,
CC ECO:0000269|PubMed:16188940, ECO:0000269|PubMed:26642364}.
CC -!- DISEASE: Muscular dystrophy, limb-girdle, autosomal recessive 25
CC (LGMDR25) [MIM:616812]: An autosomal recessive muscular disorder
CC characterized by slowly progressive onset of proximal lower limb
CC weakness in adulthood, syncopal episodes, and markedly increased serum
CC creatine kinase, which can increase further after strenuous exercise.
CC {ECO:0000269|PubMed:26642364}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the popeye family. {ECO:0000305}.
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DR EMBL; AF204172; AAG23405.1; -; mRNA.
DR EMBL; AK289979; BAF82668.1; -; mRNA.
DR EMBL; AL356775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z95329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48430.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48431.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48432.1; -; Genomic_DNA.
DR EMBL; BC034425; AAH34425.1; -; mRNA.
DR EMBL; BC040502; AAH40502.2; -; mRNA.
DR EMBL; AF124512; AAD51780.1; -; mRNA.
DR CCDS; CCDS5051.1; -.
DR RefSeq; NP_001186492.1; NM_001199563.1.
DR RefSeq; NP_009004.2; NM_007073.4.
DR RefSeq; NP_671488.1; NM_147147.3.
DR RefSeq; XP_011533700.1; XM_011535398.2.
DR AlphaFoldDB; Q8NE79; -.
DR SMR; Q8NE79; -.
DR BioGRID; 116321; 15.
DR IntAct; Q8NE79; 4.
DR STRING; 9606.ENSP00000313172; -.
DR TCDB; 8.A.129.1.1; the blood vessel epicardial substance (bves) family.
DR GlyGen; Q8NE79; 2 sites.
DR iPTMnet; Q8NE79; -.
DR PhosphoSitePlus; Q8NE79; -.
DR BioMuta; BVES; -.
DR DMDM; 38257661; -.
DR MassIVE; Q8NE79; -.
DR PaxDb; Q8NE79; -.
DR PeptideAtlas; Q8NE79; -.
DR PRIDE; Q8NE79; -.
DR ProteomicsDB; 73133; -.
DR Antibodypedia; 3082; 219 antibodies from 31 providers.
DR DNASU; 11149; -.
DR Ensembl; ENST00000314641.10; ENSP00000313172.5; ENSG00000112276.14.
DR Ensembl; ENST00000336775.9; ENSP00000337259.5; ENSG00000112276.14.
DR Ensembl; ENST00000446408.2; ENSP00000397310.2; ENSG00000112276.14.
DR GeneID; 11149; -.
DR KEGG; hsa:11149; -.
DR MANE-Select; ENST00000314641.10; ENSP00000313172.5; NM_001199563.2; NP_001186492.1.
DR UCSC; uc003pqw.4; human.
DR CTD; 11149; -.
DR DisGeNET; 11149; -.
DR GeneCards; BVES; -.
DR HGNC; HGNC:1152; BVES.
DR HPA; ENSG00000112276; Tissue enhanced (heart muscle, skeletal muscle, tongue).
DR MalaCards; BVES; -.
DR MIM; 604577; gene.
DR MIM; 616812; phenotype.
DR neXtProt; NX_Q8NE79; -.
DR OpenTargets; ENSG00000112276; -.
DR Orphanet; 476084; BVES-related limb-girdle muscular dystrophy.
DR PharmGKB; PA25469; -.
DR VEuPathDB; HostDB:ENSG00000112276; -.
DR eggNOG; ENOG502QRV2; Eukaryota.
DR GeneTree; ENSGT00390000002563; -.
DR HOGENOM; CLU_048494_0_0_1; -.
DR InParanoid; Q8NE79; -.
DR OMA; TSCQEWE; -.
DR OrthoDB; 1369469at2759; -.
DR PhylomeDB; Q8NE79; -.
DR TreeFam; TF326644; -.
DR PathwayCommons; Q8NE79; -.
DR SignaLink; Q8NE79; -.
DR SIGNOR; Q8NE79; -.
DR BioGRID-ORCS; 11149; 8 hits in 1067 CRISPR screens.
DR ChiTaRS; BVES; human.
DR GeneWiki; Blood_vessel_epicardial_substance; -.
DR GenomeRNAi; 11149; -.
DR Pharos; Q8NE79; Tbio.
DR PRO; PR:Q8NE79; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8NE79; protein.
DR Bgee; ENSG00000112276; Expressed in left ventricle myocardium and 148 other tissues.
DR Genevisible; Q8NE79; HS.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0031253; C:cell projection membrane; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR GO; GO:0030552; F:cAMP binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
DR GO; GO:0060973; P:cell migration involved in heart development; IEA:Ensembl.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0007517; P:muscle organ development; NAS:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; ISS:UniProtKB.
DR GO; GO:0001921; P:positive regulation of receptor recycling; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:2001135; P:regulation of endocytic recycling; IEA:Ensembl.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0002931; P:response to ischemia; ISS:UniProtKB.
DR GO; GO:0060931; P:sinoatrial node cell development; IEA:Ensembl.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:UniProtKB.
DR GO; GO:0051146; P:striated muscle cell differentiation; IBA:GO_Central.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0048278; P:vesicle docking; IEA:Ensembl.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR006916; Popeye_prot.
DR InterPro; IPR014710; RmlC-like_jellyroll.
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; Limb-girdle muscular dystrophy;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Tight junction; Transmembrane; Transmembrane helix.
FT CHAIN 1..360
FT /note="Blood vessel epicardial substance"
FT /id="PRO_0000046791"
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..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 93..115
FT /note="Required for interaction with CAV3"
FT /evidence="ECO:0000250|UniProtKB:Q9ES83"
FT REGION 136..186
FT /note="Required for interaction with KCNK2"
FT /evidence="ECO:0000269|PubMed:26642364"
FT REGION 317..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES83"
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 VARIANT 127
FT /note="M -> I (in dbSNP:rs9486039)"
FT /id="VAR_053600"
FT VARIANT 129
FT /note="R -> W (in dbSNP:rs2275289)"
FT /id="VAR_017155"
FT VARIANT 201
FT /note="S -> F (in LGMDR25; reduces membrane localization of
FT BVES and POPDC2; decreases by 50% affinity for cAMP;
FT disrupts enhancement of KCKN2 surface expression; increases
FT KCKN2 outward currents; no effect on total protein levels;
FT dbSNP:rs869025337)"
FT /evidence="ECO:0000269|PubMed:26642364"
FT /id="VAR_075625"
FT CONFLICT 27
FT /note="V -> P (in Ref. 6; AAD51780)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="Y -> I (in Ref. 1; AAG23405)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="E -> D (in Ref. 1; AAG23405)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="Y -> V (in Ref. 1; AAG23405)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="F -> V (in Ref. 1; AAG23405)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="D -> G (in Ref. 5; AAH40502)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="Q -> R (in Ref. 2; BAF82668)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 41451 MW; 15B21A995FEEA351 CRC64;
MNYTESSPLR ESTAIGFTPE LESIIPVPSN KTTCENWREI HHLVFHVANI CFAVGLVIPT
TLHLHMIFLR GMLTLGCTLY IVWATLYRCA LDIMIWNSVF LGVNILHLSY LLYKKRPVKI
EKELSGMYRR LFEPLRVPPD LFRRLTGQFC MIQTLKKGQT YAAEDKTSVD DRLSILLKGK
MKVSYRGHFL HNIYPCAFID SPEFRSTQMH KGEKFQVTII ADDNCRFLCW SRERLTYFLE
SEPFLYEIFR YLIGKDITNK LYSLNDPTLN DKKAKKLEHQ LSLCTQISML EMRNSIASSS
DSDDGLHQFL RGTSSMSSLH VSSPHQRASA KMKPIEEGAE DDDDVFEPAS PNTLKVHQLP
