TPC1_MOUSE
ID TPC1_MOUSE Reviewed; 817 AA.
AC Q9EQJ0; Q3V2Z6; Q6ZPW5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Two pore calcium channel protein 1 {ECO:0000305};
DE AltName: Full=Voltage-dependent calcium channel protein TPC1;
GN Name=Tpcn1 {ECO:0000312|MGI:MGI:2182472};
GN Synonyms=Kiaa1169, Tpc1 {ECO:0000303|PubMed:24776928};
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] (ISOFORM 1).
RC STRAIN=C3H/He;
RX PubMed=12080145; DOI=10.1073/pnas.142287799;
RA Perelygin A.A., Scherbik S.V., Zhulin I.B., Stockman B.M., Li Y.,
RA Brinton M.A.;
RT "Positional cloning of the murine flavivirus resistance gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9322-9327(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 228-817 (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R.F., Nagase T., Ohara O., Koga H.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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 [7]
RP FUNCTION.
RX PubMed=23063126; DOI=10.1016/j.cell.2012.08.036;
RA Wang X., Zhang X., Dong X.P., Samie M., Li X., Cheng X., Goschka A.,
RA Shen D., Zhou Y., Harlow J., Zhu M.X., Clapham D.E., Ren D., Xu H.;
RT "TPC proteins are phosphoinositide- activated sodium-selective ion channels
RT in endosomes and lysosomes.";
RL Cell 151:372-383(2012).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23394946; DOI=10.1016/j.cell.2013.01.023;
RA Cang C., Zhou Y., Navarro B., Seo Y.J., Aranda K., Shi L.,
RA Battaglia-Hsu S., Nissim I., Clapham D.E., Ren D.;
RT "mTOR regulates lysosomal ATP-sensitive two-pore Na(+) channels to adapt to
RT metabolic state.";
RL Cell 152:778-790(2013).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24776928; DOI=10.1038/nchembio.1522;
RA Cang C., Bekele B., Ren D.;
RT "The voltage-gated sodium channel TPC1 confers endolysosomal
RT excitability.";
RL Nat. Chem. Biol. 10:463-469(2014).
RN [10]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=25722412; DOI=10.1126/science.1258758;
RA Sakurai Y., Kolokoltsov A.A., Chen C.C., Tidwell M.W., Bauta W.E.,
RA Klugbauer N., Grimm C., Wahl-Schott C., Biel M., Davey R.A.;
RT "Ebola virus. Two-pore channels control Ebola virus host cell entry and are
RT drug targets for disease treatment.";
RL Science 347:995-998(2015).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STX7; STX8 AND STX12,
RP TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=28855648; DOI=10.1038/s41598-017-10607-4;
RA Castonguay J., Orth J.H.C., Mueller T., Sleman F., Grimm C.,
RA Wahl-Schott C., Biel M., Mallmann R.T., Bildl W., Schulte U., Klugbauer N.;
RT "The two-pore channel TPC1 is required for efficient protein processing
RT through early and recycling endosomes.";
RL Sci. Rep. 7:10038-10038(2017).
CC -!- FUNCTION: Intracellular channel initially characterized as a non-
CC selective Ca(2+)-permeable channel activated by NAADP (nicotinic acid
CC adenine dinucleotide phosphate), it is also a voltage-gated highly-
CC selective Na(+) channel activated directly by PI(3,5)P2
CC (phosphatidylinositol 3,5-bisphosphate) that senses pH changes and
CC confers electrical excitability to organelles (PubMed:24776928,
CC PubMed:23394946, PubMed:23063126). Localizes to the early and recycling
CC endosomes membranes where it plays a role in the uptake and processing
CC of proteins and regulates organellar membrane excitability, membrane
CC trafficking and pH homeostasis (PubMed:28855648). Ion selectivity is
CC not fixed but rather agonist-dependent and under defined ionic
CC conditions, can be readily activated by both NAADP and PI(3,5)P2 (By
CC similarity). Required for mTOR-dependent nutrient sensing
CC (PubMed:23394946). {ECO:0000250|UniProtKB:Q8NHX9,
CC ECO:0000269|PubMed:23063126, ECO:0000269|PubMed:23394946,
CC ECO:0000269|PubMed:24776928, ECO:0000269|PubMed:28855648}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:24776928};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:34965;
CC Evidence={ECO:0000269|PubMed:24776928};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671,
CC ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q9ULQ1};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29673;
CC Evidence={ECO:0000250|UniProtKB:Q9ULQ1};
CC -!- ACTIVITY REGULATION: Na(+) current is inhibited by ATP in a MTORC-
CC dependent manner. ATP sensitivity is independent of PI(3,5)P2 (By
CC similarity). Probably regulated by Mg(2+) ions, cytosolic Mg(2+)
CC selectively inhibits outward current while lysosomal Mg(2+) modestly
CC inhibits both the outward and inward currents. In the absence of
CC Mg(2+), NAADP readily activates TPCN2, with properties similar to
CC PI(3,5)P2 (By similarity). Both current elicited by PI(3,5)P2 as well
CC as NAADP are inhibited by tetrandrine (By similarity).
CC {ECO:0000250|UniProtKB:Q8NHX9, ECO:0000250|UniProtKB:Q9ULQ1}.
CC -!- SUBUNIT: Dimer. Interacts with MTOR; the interaction is required for
CC TPCN1 ATP sensitivity (By similarity). Interacts with STX7, STX8 and
CC STX12 (PubMed:28855648). Interacts with JPT2 (By similarity). Found in
CC a complex with LSM12, TPCN1 and TPCN2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9ULQ1, ECO:0000269|PubMed:28855648}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9ULQ1};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9ULQ1}. Endosome
CC membrane {ECO:0000250|UniProtKB:Q9ULQ1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9ULQ1}. Early endosome membrane
CC {ECO:0000269|PubMed:28855648}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:28855648}. Recycling endosome membrane
CC {ECO:0000269|PubMed:28855648}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:28855648}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9EQJ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EQJ0-2; Sequence=VSP_023006, VSP_023007;
CC -!- TISSUE SPECIFICITY: Mainly expressed in epithelial tissues like lung,
CC kidney, colon, spleen and liver (at protein level).
CC {ECO:0000269|PubMed:28855648}.
CC -!- DOMAIN: Each of the two internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments represent the voltage-sensor
CC and are characterized by a series of positively charged amino acids at
CC every third position. {ECO:0000250|UniProtKB:Q9ULQ1}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:28855648}.
CC -!- DISRUPTION PHENOTYPE: TPCN1 and TPCN2 double knockouts are viable,
CC fertile, have no obvious morphological abnormalities, and no obvious
CC behavioral defects. After fasting for 3 days, they are less active and
CC endurance performance is reduced by 8.3 fold in contrast to wild-type
CC littermates that show no changes. Two days after re-introduction of
CC food, mutants regain endurance and become as active as before fasting.
CC {ECO:0000269|PubMed:23394946}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. Two pore calcium channel subfamily. {ECO:0000305}.
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DR EMBL; AF217002; AAG44100.1; -; mRNA.
DR EMBL; AK077411; BAE43360.1; -; mRNA.
DR EMBL; AK148129; BAE28363.1; -; mRNA.
DR EMBL; BC058951; AAH58951.1; -; mRNA.
DR EMBL; AK129303; BAC98113.2; -; Transcribed_RNA.
DR CCDS; CCDS39239.1; -. [Q9EQJ0-1]
DR RefSeq; NP_665852.1; NM_145853.2. [Q9EQJ0-1]
DR RefSeq; XP_011246503.1; XM_011248201.2. [Q9EQJ0-1]
DR PDB; 6C96; EM; 3.40 A; A/B=1-817.
DR PDB; 6C9A; EM; 3.20 A; A/B=1-817.
DR PDBsum; 6C96; -.
DR PDBsum; 6C9A; -.
DR AlphaFoldDB; Q9EQJ0; -.
DR SMR; Q9EQJ0; -.
DR STRING; 10090.ENSMUSP00000042188; -.
DR TCDB; 1.A.1.11.22; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; Q9EQJ0; 3 sites.
DR iPTMnet; Q9EQJ0; -.
DR PhosphoSitePlus; Q9EQJ0; -.
DR jPOST; Q9EQJ0; -.
DR MaxQB; Q9EQJ0; -.
DR PaxDb; Q9EQJ0; -.
DR PRIDE; Q9EQJ0; -.
DR ProteomicsDB; 259162; -. [Q9EQJ0-1]
DR ProteomicsDB; 259163; -. [Q9EQJ0-2]
DR Antibodypedia; 31242; 64 antibodies from 18 providers.
DR DNASU; 252972; -.
DR Ensembl; ENSMUST00000046426; ENSMUSP00000042188; ENSMUSG00000032741. [Q9EQJ0-1]
DR GeneID; 252972; -.
DR KEGG; mmu:252972; -.
DR UCSC; uc008zhl.1; mouse. [Q9EQJ0-1]
DR UCSC; uc008zhn.1; mouse. [Q9EQJ0-2]
DR CTD; 53373; -.
DR MGI; MGI:2182472; Tpcn1.
DR VEuPathDB; HostDB:ENSMUSG00000032741; -.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000158958; -.
DR HOGENOM; CLU_019500_0_0_1; -.
DR InParanoid; Q9EQJ0; -.
DR OMA; QHACDQR; -.
DR OrthoDB; 761764at2759; -.
DR PhylomeDB; Q9EQJ0; -.
DR TreeFam; TF328550; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 252972; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Tpcn1; mouse.
DR PRO; PR:Q9EQJ0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9EQJ0; protein.
DR Bgee; ENSMUSG00000032741; Expressed in lacrimal gland and 224 other tissues.
DR Genevisible; Q9EQJ0; MM.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0036019; C:endolysosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0097682; F:intracellular phosphatidylinositol-3,5-bisphosphate-sensitive cation channel activity; IDA:UniProtKB.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; IDA:UniProtKB.
DR GO; GO:0072345; F:NAADP-sensitive calcium-release channel activity; ISS:UniProtKB.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:UniProtKB.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IMP:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IDA:UniProtKB.
DR Gene3D; 1.20.120.350; -; 1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR028801; TPC1_animal.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR46474; PTHR46474; 1.
DR Pfam; PF00520; Ion_trans; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Calcium channel;
KW Calcium transport; Coiled coil; Endosome; Glycoprotein; Ion channel;
KW Ion transport; Lysosome; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..817
FT /note="Two pore calcium channel protein 1"
FT /id="PRO_0000276854"
FT TOPO_DOM 1..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..137
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..221
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..263
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 264..287
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..298
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..480
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 505..527
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 528..535
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..550
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 551..569
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..590
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 591..630
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 631..654
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000255"
FT TOPO_DOM 655..671
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 672..692
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 693..817
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 20..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 770..794
FT /evidence="ECO:0000255"
FT COMPBIAS 24..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 449..488
FT /note="YLVVAVNGVWILVETFMLKGGNFTSKHVPWSYLVFLTIYG -> CKCDPSQL
FT WAPVLLSPSFLKVERQTIQKTPSTGFCPQYFS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023006"
FT VAR_SEQ 489..817
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023007"
FT HELIX 68..83
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:6C9A"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 108..123
FT /evidence="ECO:0007829|PDB:6C9A"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:6C9A"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:6C96"
FT HELIX 138..162
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 165..169
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 172..194
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 231..255
FT /evidence="ECO:0007829|PDB:6C9A"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 267..278
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 298..308
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 310..349
FT /evidence="ECO:0007829|PDB:6C9A"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 361..368
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 377..388
FT /evidence="ECO:0007829|PDB:6C9A"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:6C9A"
FT TURN 404..408
FT /evidence="ECO:0007829|PDB:6C9A"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:6C9A"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:6C9A"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 429..439
FT /evidence="ECO:0007829|PDB:6C9A"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 444..465
FT /evidence="ECO:0007829|PDB:6C9A"
FT TURN 466..468
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 478..498
FT /evidence="ECO:0007829|PDB:6C9A"
FT TURN 501..503
FT /evidence="ECO:0007829|PDB:6C9A"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 507..527
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 531..534
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 535..538
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 540..550
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 552..561
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 565..589
FT /evidence="ECO:0007829|PDB:6C9A"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:6C9A"
FT STRAND 602..604
FT /evidence="ECO:0007829|PDB:6C96"
FT TURN 605..607
FT /evidence="ECO:0007829|PDB:6C9A"
FT STRAND 610..613
FT /evidence="ECO:0007829|PDB:6C96"
FT HELIX 615..617
FT /evidence="ECO:0007829|PDB:6C96"
FT STRAND 620..623
FT /evidence="ECO:0007829|PDB:6C96"
FT HELIX 626..628
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 634..645
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 650..660
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 664..698
FT /evidence="ECO:0007829|PDB:6C9A"
FT STRAND 710..716
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 719..731
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 736..750
FT /evidence="ECO:0007829|PDB:6C9A"
FT STRAND 756..762
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 766..773
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 775..777
FT /evidence="ECO:0007829|PDB:6C9A"
FT HELIX 779..793
FT /evidence="ECO:0007829|PDB:6C9A"
SQ SEQUENCE 817 AA; 94496 MW; 269930E1D1136B10 CRC64;
MAVSLDDDVP LILTLDEAES APLPPSNSLG QEQLPSKNGG SHSIHNSQVP SLVSGADSPP
SSPTGHNWEM NYQEAAIYLQ EGQNNDKFFT HPKDARALAA YLFVHNHFFY MMELLTALLL
LLLSLCESPA VPVLKLHTYV HATLELFALM VVVFELCMKL RWLGFHTFVR HKRTMVKTSV
LVVQFIEAIV VLVRQTSHVR VTRALRCIFL VDCRYCGGVR RNLRQIFQSL PPFMDILLLL
LFFMIIFAIL GFYLFSTNPS DPYFSTLENS IVNLFVLLTT ANFPDVMMPS YSRNPWSCVF
FIVYLSIELY FIMNLLLAVV FDTFNDIEKH KFKSLLLHKR TAIQHAYGLL ASQRRPAGIS
YRQFEGLMRF YKPRMSARER FLTFKALNQS NTPLLSLKDF YDIYEVAALQ WKAKRNRQHW
FDELPRTAFL IFKGINILVN SKAFQYFMYL VVAVNGVWIL VETFMLKGGN FTSKHVPWSY
LVFLTIYGVE LFMKVAGLGP VEYLSSGWNL FDFSVTAFAF LGLLALTLNM EPFYFIVVLR
PLQLLRLFKL KKRYRNVLDT MFELLPRMAS LGLTLLTFYY SFAIVGMEFF NGRLTPNCCN
TSTVADAYRF INHTVGNKTK VEEGYYYLNN FDNILNSFVT LFELTVVNNW YIIMEGVTSQ
TSHWSRLYFM TFYIVTMVVM TIIVAFILEA FVFRMNYSRK SQDSEVDSGI VIEKEMSKEE
LMAVLELYRE ERGTSSDVTR LLDTLSQMEK YQQNSMVFLG RRSRTKSDLS LKMYQEEIQE
WYEEHAREQE QQKLRGSVPG PAAQQPPGSR QRSQTVT
