PKD2_DANRE
ID PKD2_DANRE Reviewed; 904 AA.
AC Q6IVV8; Q2VF27;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Polycystin-2 {ECO:0000303|PubMed:16216239};
DE AltName: Full=Curly up {ECO:0000303|PubMed:17360770};
DE Short=Cup {ECO:0000303|PubMed:17360770};
DE AltName: Full=Polycystic kidney disease 2 protein homolog;
DE AltName: Full=Transient receptor potential cation channel subfamily P member 2;
GN Name=pkd2 {ECO:0000312|ZFIN:ZDB-GENE-040827-4};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000312|EMBL:AAT39122.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15269167; DOI=10.1242/dev.01240;
RA Sun Z., Amsterdam A., Pazour G.J., Cole D.G., Miller M.S., Hopkins N.;
RT "A genetic screen in zebrafish identifies cilia genes as a principal cause
RT of cystic kidney.";
RL Development 131:4085-4093(2004).
RN [2] {ECO:0000312|EMBL:ABA60692.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16216239; DOI=10.1016/j.ydbio.2005.08.047;
RA Bisgrove B.W., Snarr B.S., Emrazian A., Yost H.J.;
RT "Polaris and polycystin-2 in dorsal forerunner cells and Kupffer's vesicle
RT are required for specification of the zebrafish left-right axis.";
RL Dev. Biol. 287:274-288(2005).
RN [3] {ECO:0000312|Ensembl:ENSDARP00000027024, ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Ensembl:ENSDARP00000027024,
RC ECO:0000312|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=16943304; DOI=10.1681/asn.2006040412;
RA Obara T., Mangos S., Liu Y., Zhao J., Wiessner S., Kramer-Zucker A.G.,
RA Olale F., Schier A.F., Drummond I.A.;
RT "Polycystin-2 immunolocalization and function in zebrafish.";
RL J. Am. Soc. Nephrol. 17:2706-2718(2006).
RN [5]
RP DISRUPTION PHENOTYPE, AND PHOSPHORYLATION.
RX PubMed=16551655; DOI=10.1093/hmg/ddl070;
RA Streets A.J., Moon D.J., Kane M.E., Obara T., Ong A.C.;
RT "Identification of an N-terminal glycogen synthase kinase 3 phosphorylation
RT site which regulates the functional localization of polycystin-2 in vivo
RT and in vitro.";
RL Hum. Mol. Genet. 15:1465-1473(2006).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP LEU-351.
RX PubMed=17360770; DOI=10.1242/dev.02827;
RA Schottenfeld J., Sullivan-Brown J., Burdine R.D.;
RT "Zebrafish curly up encodes a Pkd2 ortholog that restricts left-side-
RT specific expression of southpaw.";
RL Development 134:1605-1615(2007).
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=23376035; DOI=10.1016/j.yjmcc.2013.01.015;
RA Paavola J., Schliffke S., Rossetti S., Kuo I.Y., Yuan S., Sun Z.,
RA Harris P.C., Torres V.E., Ehrlich B.E.;
RT "Polycystin-2 mutations lead to impaired calcium cycling in the heart and
RT predispose to dilated cardiomyopathy.";
RL J. Mol. Cell. Cardiol. 58:199-208(2013).
RN [8]
RP DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=26432887; DOI=10.1242/bio.014076;
RA Roxo-Rosa M., Jacinto R., Sampaio P., Lopes S.S.;
RT "The zebrafish Kupffer's vesicle as a model system for the molecular
RT mechanisms by which the lack of Polycystin-2 leads to stimulation of
RT CFTR.";
RL Biol. Open 4:1356-1366(2015).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25660539; DOI=10.1016/j.cub.2014.12.051;
RA Yuan S., Zhao L., Brueckner M., Sun Z.;
RT "Intraciliary calcium oscillations initiate vertebrate left-right
RT asymmetry.";
RL Curr. Biol. 25:556-567(2015).
CC -!- FUNCTION: Component of a heteromeric calcium-permeable ion channel
CC formed by PKD1 and PKD2 that is activated by interaction between PKD1
CC and a Wnt family member, such as WNT3A and WNT9B. Can also form a
CC functional, homotetrameric ion channel (By similarity). Functions as
CC non-selective, voltage-gated cation channel (By similarity). Required
CC for normal oscillation of Ca(2+) levels within cilia; these
CC oscillations of the intraciliary Ca(2+) levels can trigger cytoplasmic
CC Ca(2+) signaling cascades (PubMed:25660539). May contribute to the
CC release of Ca(2+) stores from the endoplasmic reticulum (By
CC similarity). Required for normal temporal variation of the
CC intracellular Ca(2+) levels in the heart (PubMed:23376035). Plays a
CC role in fluid-flow mechanosensation (By similarity). Required for
CC normal specification of the body left-right axis during embryogenesis,
CC most likely via its role in ciliary Ca(2+) oscillations in Kupffer's
CC vesicle (PubMed:15269167, PubMed:16216239, PubMed:16943304,
CC PubMed:17360770, PubMed:23376035, PubMed:25660539).
CC {ECO:0000250|UniProtKB:O35245, ECO:0000250|UniProtKB:Q13563,
CC ECO:0000269|PubMed:15269167, ECO:0000269|PubMed:16216239,
CC ECO:0000269|PubMed:16943304, ECO:0000269|PubMed:17360770,
CC ECO:0000269|PubMed:23376035, ECO:0000269|PubMed:25660539}.
CC -!- ACTIVITY REGULATION: Channel activity is regulated by phosphorylation.
CC Channel activity is regulated by intracellular Ca(2+).
CC {ECO:0000250|UniProtKB:Q13563}.
CC -!- SUBUNIT: Homotetramer (By similarity). Heterotetramer with pkd1, giving
CC rise to a complex formed by one pkd1 chain and three pkd2 chains (By
CC similarity). Interacts with pkd1l1 (By similarity).
CC {ECO:0000250|UniProtKB:H2LRU7, ECO:0000250|UniProtKB:Q13563}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:16943304}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q13563}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:16943304}. Cytoplasm, myofibril, sarcomere
CC {ECO:0000269|PubMed:16943304}. Sarcoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23376035}. Apical cell membrane
CC {ECO:0000269|PubMed:16943304}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q13563}. Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:26432887}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q13563}. Cell projection, cilium
CC {ECO:0000269|PubMed:16943304, ECO:0000269|PubMed:26432887}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:26432887}.
CC Cytoplasmic vesicle membrane {ECO:0000269|PubMed:16943304}.
CC Note=Detected at the basolateral cell membrane and on apical, lumenal
CC cilia in anterior, proximal pronephric ducts, and in intracellular
CC vesicles in the posterior part of the pronephric duct. Detected on
CC apical cell membranes on epithelial cells in the ear.
CC {ECO:0000269|PubMed:16943304}.
CC -!- TISSUE SPECIFICITY: Detected along cilia and at the cilium basal body
CC in Kupffer's vesicle at the 10 somite stage (PubMed:26432887). Detected
CC in heart at 48hpf (PubMed:23376035). Detected in muscle and pronephric
CC kidney at 48 hpf (PubMed:16943304). Detected on trunk muscle sarcolemma
CC and sarcomere, on ependymal cell cilia in brain, at the apical cell
CC membrane in epithelial cells in the ear, at the lateral line organ and
CC olfactory placode at 56 hpf (PubMed:16943304). Detected in adult kidney
CC (at protein level) (PubMed:16943304). {ECO:0000269|PubMed:16943304,
CC ECO:0000269|PubMed:26432887}.
CC -!- DEVELOPMENTAL STAGE: First detected at the onset of gastrulation in a
CC band at the blastoderm margin (PubMed:16216239, PubMed:17360770).
CC Ubiquitous during gastrulation, somatogenesis and at 48 hpf
CC (PubMed:16943304). During gastrulation, detected at the hypoblast of
CC the dorsal midline and in dorsal forerunner cells that form a ciliated
CC Kupffer's vesicle later on (PubMed:16216239, PubMed:17360770,
CC PubMed:26432887). Ubiquitous during early somite stages, with high
CC levels of expression in Kupffer's vesicle (PubMed:16216239,
CC PubMed:17360770). At subsequent stages, detected in pronephric duct
CC primordia and neural floorplate (PubMed:16216239, PubMed:16943304,
CC PubMed:17360770, PubMed:26432887). Highly expressed in brain at 24 hpf
CC (PubMed:16216239). At 3 dpf, detected at pharyngeal arches and the
CC pectoral fin bud (PubMed:16216239). {ECO:0000269|PubMed:16216239,
CC ECO:0000269|PubMed:16943304, ECO:0000269|PubMed:17360770,
CC ECO:0000269|PubMed:26432887}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is involved in
CC oligomerization. The coiled-coil domain binds calcium and undergoes a
CC calcium-induced conformation change (in vitro).
CC {ECO:0000250|UniProtKB:Q13563}.
CC -!- PTM: Phosphorylated. Phosphorylation is important for protein function;
CC a mutant human construct that lacks the N-terminal phosphorylation
CC sites cannot complement a zebrafish pkd2-deficient mutant.
CC {ECO:0000269|PubMed:16551655}.
CC -!- PTM: N-glycosylated. The four subunits in a tetramer probably differ in
CC the extent of glycosylation; simultaneous glycosylation of all
CC experimentally validated sites would probably create steric hindrance.
CC {ECO:0000250|UniProtKB:Q13563}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein impairs
CC specification of the left-right axis during embryonic development and
CC randomization of heart and gut looping, plus misexpression of left-side
CC specific genes (PubMed:16216239, PubMed:16943304, PubMed:17360770,
CC PubMed:26432887, PubMed:25660539). Morpholino knockdown of the protein
CC causes body curvature, tail curling, hydrocephalus and kidney cysts
CC (PubMed:15269167, PubMed:16216239, PubMed:16943304, PubMed:16551655,
CC PubMed:17360770, PubMed:23376035, PubMed:26432887). Morpholino
CC knockdown has no effect on number, length or motility of pronephric
CC cilia, but the fluid flow through the pronephric ducts seems to be
CC impaired due to physical obstruction of the ducts (PubMed:16943304).
CC Likewise, morpholino knockdown of the protein has no effect on the
CC motility of cilia in Kupffer's vesicle (PubMed:25660539). Morpholino
CC knockdown of the protein leads to an increase of the volume of
CC Kupffer's vesicle, without any change in the proliferation of the cells
CC that line the vesicle (PubMed:26432887). Morpholino knockdown of the
CC protein leads to impaired heart function, characterized by arrhytmia
CC and frequently associated with pericardial and abdominal edema and
CC atrioventricular block (PubMed:23376035). {ECO:0000269|PubMed:15269167,
CC ECO:0000269|PubMed:16216239, ECO:0000269|PubMed:16551655,
CC ECO:0000269|PubMed:16943304, ECO:0000269|PubMed:17360770,
CC ECO:0000269|PubMed:23376035, ECO:0000269|PubMed:26432887}.
CC -!- SIMILARITY: Belongs to the polycystin family. {ECO:0000305}.
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DR EMBL; AY618926; AAT39122.1; -; mRNA.
DR EMBL; DQ175629; ABA60692.1; -; mRNA.
DR EMBL; CR788312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001002310.1; NM_001002310.1.
DR RefSeq; XP_009292468.1; XM_009294193.2.
DR AlphaFoldDB; Q6IVV8; -.
DR SMR; Q6IVV8; -.
DR STRING; 7955.ENSDARP00000027024; -.
DR PaxDb; Q6IVV8; -.
DR Ensembl; ENSDART00000020412; ENSDARP00000027024; ENSDARG00000014098.
DR GeneID; 432387; -.
DR KEGG; dre:432387; -.
DR CTD; 5311; -.
DR ZFIN; ZDB-GENE-040827-4; pkd2.
DR eggNOG; KOG3599; Eukaryota.
DR GeneTree; ENSGT00940000159025; -.
DR HOGENOM; CLU_012097_0_0_1; -.
DR InParanoid; Q6IVV8; -.
DR OMA; DGLYWDM; -.
DR OrthoDB; 426073at2759; -.
DR PhylomeDB; Q6IVV8; -.
DR TreeFam; TF316484; -.
DR Reactome; R-DRE-5620916; VxPx cargo-targeting to cilium.
DR PRO; PR:Q6IVV8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000014098; Expressed in Kupffer's vesicle and 39 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ZFIN.
DR GO; GO:0034703; C:cation channel complex; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:ZFIN.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ZFIN.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:ZFIN.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005261; F:cation channel activity; ISS:UniProtKB.
DR GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0005267; F:potassium channel activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0003171; P:atrioventricular valve development; IMP:ZFIN.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0198738; P:cell-cell signaling by wnt; ISS:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0097704; P:cellular response to oscillatory fluid shear stress; IMP:ZFIN.
DR GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR GO; GO:0050982; P:detection of mechanical stimulus; IBA:GO_Central.
DR GO; GO:0061371; P:determination of heart left/right asymmetry; IMP:ZFIN.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:ZFIN.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN.
DR GO; GO:0003143; P:embryonic heart tube morphogenesis; IMP:ZFIN.
DR GO; GO:0007507; P:heart development; IMP:CACAO.
DR GO; GO:0003146; P:heart jogging; IMP:ZFIN.
DR GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:ZFIN.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; IMP:ZFIN.
DR GO; GO:0070121; P:Kupffer's vesicle development; IMP:ZFIN.
DR GO; GO:0060972; P:left/right pattern formation; IMP:ZFIN.
DR GO; GO:0001946; P:lymphangiogenesis; IMP:ZFIN.
DR GO; GO:0007219; P:Notch signaling pathway; IMP:ZFIN.
DR GO; GO:0051284; P:positive regulation of sequestering of calcium ion; IMP:CACAO.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0048793; P:pronephros development; IMP:ZFIN.
DR GO; GO:0072114; P:pronephros morphogenesis; IMP:ZFIN.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; IPI:ZFIN.
DR GO; GO:0072019; P:proximal convoluted tubule development; IMP:ZFIN.
DR GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IMP:ZFIN.
DR GO; GO:0032965; P:regulation of collagen biosynthetic process; IMP:ZFIN.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR GO; GO:0003173; P:ventriculo bulbo valve development; IMP:ZFIN.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR013122; PKD1_2_channel.
DR InterPro; IPR003915; PKD_2.
DR Pfam; PF08016; PKD_channel; 1.
DR PRINTS; PR01433; POLYCYSTIN2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Repeat; Sarcoplasmic reticulum; Transmembrane; Transmembrane helix;
KW Transport; Voltage-gated channel; Wnt signaling pathway.
FT CHAIN 1..904
FT /note="Polycystin-2"
FT /id="PRO_0000439854"
FT TOPO_DOM 1..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT TRANSMEM 156..177
FT /note="Helical; Name=S1"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT TOPO_DOM 178..404
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT TRANSMEM 405..425
FT /note="Helical; Name=S2"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT TOPO_DOM 426..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT TRANSMEM 442..462
FT /note="Helical; Name=S3"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT TOPO_DOM 463..489
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT TRANSMEM 490..510
FT /note="Helical; Name=S4"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT TOPO_DOM 511..534
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT TRANSMEM 535..556
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT TOPO_DOM 557..568
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT INTRAMEM 569..583
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT TOPO_DOM 584..591
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT TRANSMEM 592..612
FT /note="Helical; Name=S6"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT TOPO_DOM 613..904
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT DOMAIN 687..722
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 768..786
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..759
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT REGION 854..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 770..809
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT MOTIF 578..580
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 700
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT BINDING 702
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT BINDING 704
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT BINDING 706
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT BINDING 711
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 267..280
FT /evidence="ECO:0000250|UniProtKB:Q13563"
FT MUTAGEN 351
FT /note="L->P: In ty30b; curly tail phenotype and impaired
FT left-right patterning."
FT /evidence="ECO:0000269|PubMed:17360770"
FT CONFLICT 15
FT /note="A -> V (in Ref. 2; ABA60692)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="L -> P (in Ref. 2; ABA60692)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="G -> R (in Ref. 2; ABA60692)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="T -> A (in Ref. 2; ABA60692)"
FT /evidence="ECO:0000305"
FT CONFLICT 604..608
FT /note="FIFMI -> LIFMV (in Ref. 2; ABA60692)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 904 AA; 103269 MW; 53B45F174BB50E5E CRC64;
MSSSRVRPQA PQSPAASASA SPPPHEGIEM EKMHHEEVGL GVPDETPSSP PTSSSRQAWS
RDNPGFEPEE GMMEADWPPE SQGRRSVSTT SSSSSGGVPG NFSGISARIN RGLYPTPPAQ
EHRSCGKRIL EKMRVLWDTR LLGESNSNRE MYLKTVLREM ITYILFLLTL CIITYGMVST
NMYYYTKVMS QLFLDTPLSS GEPTNFKSLS TMEDFWKFTE GPFLNGMYWE LWYNNKSLPE
NQSLIYYENL LLGVPRLRQL RVRNESCSVH EDLRDEVYDC YNVYSPANED KAPFGPKNGT
AWRFKDESSL GESSYWGQVS TYGGGGYYQD LSRTREKSAN QLQELKNNLW LDRGTRAVFL
DFSIYNGNVN LFCIVRLLVE FPATGGAVPS WQFQTVRLLR YVSSWDYFVG MCEVSFCLFV
LYYLVEEALE IRLHRLRYFK SLWNCLDVLI VALSVPAIIM NICRTSAVSH RLHFLLENHS
TYPNFEPLAR LQVHFNNLAA IIVFLSWVKL FKFINFNKTM NQLSTTMSRC AKDLMGFAIM
FFIVFLAYAQ LAYLVFGTQV NDFSTFQACI FTQFRIILGD FDFSEIEEAD SVLGPIYFTT
FVFFIFMILL NMFLAIINDT YSEVKADMAQ QRSEMEITDL IKKSYNRAMV KLKLKKSSIN
DIPDSLQQAA GKLSFDELRQ DLRGKGHSDA EIEAIFAKYD LDGDQELTEH EHQQMRDDLE
KEREDLDLEH SSLPRPASGR SFSRSQDDSE EDDDEDSGHS SRRRGSSSGG VSYEEFQVLV
RRVDRMEHSI GSIVSKIDAV IVKLEAMERA KMKRRDVLGR ILDGVMEDER MGRDPELQRE
QMDRLVRDEL ERWESDDTMS QVSHHHHQAT PIISSAQLRP RSSRPPSSLS NEGPDAAASG
PAHL
