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 24-JAN-2024, entry version 156. 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}, POPDC1 GN {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}. 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; 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; 16. DR IntAct; Q8NE79; 4. DR STRING; 9606.ENSP00000313172; -. DR TCDB; 8.A.129.1.1; the blood vessel epicardial substance (bves) family. DR GlyCosmos; Q8NE79; 2 sites, No reported glycans. DR GlyGen; Q8NE79; 2 sites. DR iPTMnet; Q8NE79; -. DR PhosphoSitePlus; Q8NE79; -. DR SwissPalm; Q8NE79; -. DR BioMuta; BVES; -. DR DMDM; 38257661; -. DR MassIVE; Q8NE79; -. DR PaxDb; 9606-ENSP00000313172; -. DR PeptideAtlas; Q8NE79; -. DR ProteomicsDB; 73133; -. DR Antibodypedia; 3082; 229 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 AGR; HGNC:1152; -. 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; SCQEWEQ; -. DR OrthoDB; 5385961at2759; -. DR PhylomeDB; Q8NE79; -. DR TreeFam; TF326644; -. DR PathwayCommons; Q8NE79; -. DR SignaLink; Q8NE79; -. DR SIGNOR; Q8NE79; -. DR BioGRID-ORCS; 11149; 8 hits in 1147 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 150 other cell types or tissues. 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:0016328; C:lateral plasma membrane; IDA:UniProtKB. DR GO; GO:0016020; C: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; Jelly Rolls; 1. DR InterPro; IPR018490; cNMP-bd_dom_sf. DR InterPro; IPR006916; Popeye_prot. DR InterPro; IPR014710; RmlC-like_jellyroll. DR PANTHER; PTHR12101:SF17; BLOOD VESSEL EPICARDIAL SUBSTANCE; 1. DR PANTHER; PTHR12101; POPEYE DOMAIN CONTAINING PROTEIN; 1. DR Pfam; PF04831; Popeye; 1. DR SUPFAM; SSF51206; cAMP-binding domain-like; 1. DR Genevisible; Q8NE79; HS. 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 //