NCLX_MOUSE
ID NCLX_MOUSE Reviewed; 585 AA.
AC Q925Q3; Q3U067; Q80XM7;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Mitochondrial sodium/calcium exchanger protein {ECO:0000305};
DE AltName: Full=Na(+)/K(+)/Ca(2+)-exchange protein 6 {ECO:0000303|PubMed:14625281};
DE AltName: Full=Sodium/calcium exchanger protein, mitochondrial {ECO:0000303|PubMed:20018762};
DE AltName: Full=Sodium/potassium/calcium exchanger 6 {ECO:0000303|PubMed:14625281};
DE AltName: Full=Solute carrier family 24 member 6 {ECO:0000312|MGI:MGI:2180781};
DE AltName: Full=Solute carrier family 8 member B1 {ECO:0000312|MGI:MGI:2180781};
DE Flags: Precursor;
GN Name=Slc8b1 {ECO:0000312|MGI:MGI:2180781};
GN Synonyms=Nckx6 {ECO:0000303|PubMed:14625281},
GN Nclx {ECO:0000303|PubMed:20018762}, Slc24a6 {ECO:0000312|MGI:MGI:2180781};
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).
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] (ISOFORM 3).
RC STRAIN=NOD; TISSUE=Spleen;
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 2).
RC STRAIN=FVB/N; TISSUE=Liver;
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 ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=14625281; DOI=10.1074/jbc.m310908200;
RA Cai X., Lytton J.;
RT "Molecular cloning of a sixth member of the K+-dependent Na+/Ca2+ exchanger
RT gene family, NCKX6.";
RL J. Biol. Chem. 279:5867-5876(2004).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20018762; DOI=10.1073/pnas.0908099107;
RA Palty R., Silverman W.F., Hershfinkel M., Caporale T., Sensi S.L.,
RA Parnis J., Nolte C., Fishman D., Shoshan-Barmatz V., Herrmann S.,
RA Khananshvili D., Sekler I.;
RT "NCLX is an essential component of mitochondrial Na+/Ca2+ exchange.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:436-441(2010).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=22677781; DOI=10.1159/000337493;
RA Hu P., Lacruz R.S., Smith C.E., Smith S.M., Kurtz I., Paine M.L.;
RT "Expression of the sodium/calcium/potassium exchanger, NCKX4, in
RT ameloblasts.";
RL Cells Tissues Organs 196:501-509(2012).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24067497; DOI=10.1038/srep02766;
RA Takeuchi A., Kim B., Matsuoka S.;
RT "The mitochondrial Na+-Ca2+ exchanger, NCLX, regulates automaticity of HL-1
RT cardiomyocytes.";
RL Sci. Rep. 3:2766-2766(2013).
RN [8]
RP FUNCTION.
RX PubMed=27328625; DOI=10.1038/srep28378;
RA Kim B., Takeuchi A., Hikida M., Matsuoka S.;
RT "Roles of the mitochondrial Na(+)-Ca(2+) exchanger, NCLX, in B lymphocyte
RT chemotaxis.";
RL Sci. Rep. 6:28378-28378(2016).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=28445457; DOI=10.1038/nature22082;
RA Luongo T.S., Lambert J.P., Gross P., Nwokedi M., Lombardi A.A.,
RA Shanmughapriya S., Carpenter A.C., Kolmetzky D., Gao E., van Berlo J.H.,
RA Tsai E.J., Molkentin J.D., Chen X., Madesh M., Houser S.R., Elrod J.W.;
RT "The mitochondrial Na(+)/Ca(2+) exchanger is essential for Ca(2+)
RT homeostasis and viability.";
RL Nature 545:93-97(2017).
CC -!- FUNCTION: Mitochondrial sodium/calcium antiporter that mediates sodium-
CC dependent calcium efflux from mitochondrion, by mediating the exchange
CC of 3 sodium ions per 1 calcium ion (PubMed:20018762, PubMed:28445457).
CC Plays a central role in mitochondrial calcium homeostasis by mediating
CC mitochondrial calcium extrusion: calcium efflux is essential for
CC mitochondrial function and cell survival, notably in cardiomyocytes
CC (PubMed:24067497, PubMed:28445457). Regulates rates of glucose-
CC dependent insulin secretion in pancreatic beta-cells during the first
CC phase of insulin secretion: acts by mediating efflux of calcium from
CC mitochondrion, thereby affecting cytoplasmic calcium responses (By
CC similarity). Required for store-operated Ca(2+) entry (SOCE) and Ca(2+)
CC release-activated Ca(2+) (CRAC) channel regulation: sodium transport by
CC SLC8B1 leads to promote calcium-shuttling that modulates mitochondrial
CC redox status, thereby regulating SOCE activity (By similarity).
CC Involved in B-lymphocyte chemotaxis (PubMed:27328625). Able to
CC transport Ca(2+) in exchange of either Li(+) or Na(+), explaining how
CC Li(+) catalyzes Ca(2+) exchange (By similarity). In contrast to other
CC members of the family its function is independent of K(+) (By
CC similarity). {ECO:0000250|UniProtKB:Q6J4K2,
CC ECO:0000269|PubMed:20018762, ECO:0000269|PubMed:24067497,
CC ECO:0000269|PubMed:27328625, ECO:0000269|PubMed:28445457}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(in) + 3 Na(+)(out) = Ca(2+)(out) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:69955, ChEBI:CHEBI:29101, ChEBI:CHEBI:29108;
CC Evidence={ECO:0000305|PubMed:20018762, ECO:0000305|PubMed:28445457};
CC -!- ACTIVITY REGULATION: Inhibited by the sodium/calcium exchanger
CC inhibitor CGP-37157 (PubMed:28445457). Strongly inhibited by zinc (By
CC similarity). {ECO:0000250|UniProtKB:Q6J4K2}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:20018762, ECO:0000269|PubMed:24067497}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:20018762}. Note=Mainly localizes
CC to mitochondrion inner membrane (PubMed:20018762).
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000269|PubMed:14625281}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14625281}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=L {ECO:0000303|PubMed:14625281}, Long
CC {ECO:0000303|PubMed:14625281};
CC IsoId=Q925Q3-1; Sequence=Displayed;
CC Name=2; Synonyms=S {ECO:0000303|PubMed:14625281}, Short
CC {ECO:0000303|PubMed:14625281};
CC IsoId=Q925Q3-2; Sequence=VSP_016998;
CC Name=3;
CC IsoId=Q925Q3-3; Sequence=VSP_016997;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in dental
CC tissues. {ECO:0000269|PubMed:14625281, ECO:0000269|PubMed:22677781}.
CC -!- PTM: Phosphorylation at Ser-258 by PKA prevents calcium overload.
CC {ECO:0000250|UniProtKB:Q6J4K2}.
CC -!- DISRUPTION PHENOTYPE: Conditional deletion in adult hearts causes
CC sudden death in 87% of the mice. Hearts show substantial cardiac
CC remodeling, including an increase in heart mass and correlative change
CC in cardiomyocyte cross-sectional area, as well as a significant
CC increase in cardiac fibrosis. Defects are probably due to mitochondrial
CC calcium overload leading to increased generation of superoxide and
CC necrotic cell death. {ECO:0000269|PubMed:28445457}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. SLC24A subfamily. {ECO:0000305}.
CC -!- CAUTION: Isoform 1 was reported to not have cation exchanger activity
CC (PubMed:12080145). However, such result is unclear.
CC {ECO:0000305|PubMed:12080145}.
CC -!- CAUTION: Isoform 1 and isoform 2 were reported to localize to the
CC endoplasmic reticulum membrane and cell membrane, respectively
CC (PubMed:14625281). This result is however not supported by other
CC studies that report localization to the mitochondrial membrane
CC (PubMed:20018762, PubMed:24067497). {ECO:0000269|PubMed:14625281,
CC ECO:0000269|PubMed:20018762, ECO:0000269|PubMed:24067497}.
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DR EMBL; AF261233; AAK49407.1; -; mRNA.
DR EMBL; AK157173; BAE33988.1; -; mRNA.
DR EMBL; BC043689; AAH43689.1; -; mRNA.
DR CCDS; CCDS39238.1; -. [Q925Q3-1]
DR CCDS; CCDS51633.1; -. [Q925Q3-2]
DR CCDS; CCDS51634.1; -. [Q925Q3-3]
DR RefSeq; NP_001171065.1; NM_001177594.1. [Q925Q3-3]
DR RefSeq; NP_001171066.1; NM_001177595.1. [Q925Q3-2]
DR RefSeq; NP_573484.2; NM_133221.2. [Q925Q3-1]
DR AlphaFoldDB; Q925Q3; -.
DR BioGRID; 228418; 5.
DR STRING; 10090.ENSMUSP00000064714; -.
DR GlyGen; Q925Q3; 1 site.
DR PhosphoSitePlus; Q925Q3; -.
DR SwissPalm; Q925Q3; -.
DR jPOST; Q925Q3; -.
DR MaxQB; Q925Q3; -.
DR PaxDb; Q925Q3; -.
DR PRIDE; Q925Q3; -.
DR ProteomicsDB; 252792; -. [Q925Q3-1]
DR ProteomicsDB; 252793; -. [Q925Q3-2]
DR ProteomicsDB; 252794; -. [Q925Q3-3]
DR Antibodypedia; 31257; 98 antibodies from 26 providers.
DR DNASU; 170756; -.
DR Ensembl; ENSMUST00000068326; ENSMUSP00000064714; ENSMUSG00000032754. [Q925Q3-1]
DR Ensembl; ENSMUST00000076051; ENSMUSP00000075428; ENSMUSG00000032754. [Q925Q3-2]
DR Ensembl; ENSMUST00000111890; ENSMUSP00000107521; ENSMUSG00000032754. [Q925Q3-3]
DR GeneID; 170756; -.
DR KEGG; mmu:170756; -.
DR UCSC; uc008zhj.2; mouse. [Q925Q3-1]
DR UCSC; uc012eco.1; mouse. [Q925Q3-3]
DR UCSC; uc012ecp.1; mouse. [Q925Q3-2]
DR CTD; 80024; -.
DR MGI; MGI:2180781; Slc8b1.
DR VEuPathDB; HostDB:ENSMUSG00000032754; -.
DR eggNOG; KOG2399; Eukaryota.
DR GeneTree; ENSGT00940000157433; -.
DR HOGENOM; CLU_004979_3_2_1; -.
DR InParanoid; Q925Q3; -.
DR OMA; MNIANEV; -.
DR OrthoDB; 478735at2759; -.
DR PhylomeDB; Q925Q3; -.
DR TreeFam; TF323444; -.
DR Reactome; R-MMU-425561; Sodium/Calcium exchangers.
DR Reactome; R-MMU-8949215; Mitochondrial calcium ion transport.
DR BioGRID-ORCS; 170756; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Slc8b1; mouse.
DR PRO; PR:Q925Q3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q925Q3; protein.
DR Bgee; ENSMUSG00000032754; Expressed in granulocyte and 185 other tissues.
DR ExpressionAtlas; Q925Q3; baseline and differential.
DR Genevisible; Q925Q3; MM.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0030061; C:mitochondrial crista; ISS:BHF-UCL.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0005432; F:calcium:sodium antiporter activity; IDA:BHF-UCL.
DR GO; GO:0086038; F:calcium:sodium antiporter activity involved in regulation of cardiac muscle cell membrane potential; IMP:UniProtKB.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0099093; P:calcium export from the mitochondrion; IMP:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:MGI.
DR GO; GO:0006812; P:cation transport; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; IDA:MGI.
DR GO; GO:0086036; P:regulation of cardiac muscle cell membrane potential; IC:BHF-UCL.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:BHF-UCL.
DR GO; GO:0050796; P:regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:1901623; P:regulation of lymphocyte chemotaxis; IMP:UniProtKB.
DR GO; GO:2001256; P:regulation of store-operated calcium entry; ISO:MGI.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IDA:MGI.
DR Gene3D; 1.20.1420.30; -; 2.
DR InterPro; IPR004837; NaCa_Exmemb.
DR InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR Pfam; PF01699; Na_Ca_ex; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Antiport; Calcium; Calcium transport; Cell membrane;
KW Glycoprotein; Ion transport; Lithium; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Sensory transduction; Sodium; Sodium transport; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..585
FT /note="Mitochondrial sodium/calcium exchanger protein"
FT /id="PRO_0000045757"
FT TOPO_DOM 27..95
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..168
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..229
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..360
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..416
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..491
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..546
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 547..559
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 560..580
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255"
FT TOPO_DOM 581..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 258
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q6J4K2"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 122..140
FT /note="FCPNLSAISTNLKLSHNVA -> PH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016997"
FT VAR_SEQ 471..585
FT /note="DAFSDFTLARQGYPRMAFSACFGGIIFNILVGVGLGCLLQIIRNHVVEVKLE
FT PDGLLVWVLASALGLSLIFSLVSVPLQCFQLSKAYGLCLLLFYICFLVVVLLTEFGVIH
FT LKKA -> AGARRITGVGAGQCPGPQLDLLPGLRAASVFPAQQGLRPLPPPLLHLFPCC
FT GPAHRVWGDSPEEGVTEAAWPRGVGAILLAS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016998"
FT CONFLICT 20
FT /note="I -> L (in Ref. 1; AAK49407)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="T -> A (in Ref. 1; AAK49407)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="R -> Q (in Ref. 1; AAK49407)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="I -> L (in Ref. 1; AAK49407)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="F -> L (in Ref. 1; AAK49407)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="I -> V (in Ref. 1; AAK49407)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 585 AA; 64365 MW; 83B001A9C78B2620 CRC64;
MASRWLALLW APVFLCVALI LETASGTGDP STKAHGHIQF SAGSVNQTAM ADCRAVCGLN
TSDRCDFVRR NPDCRSEAGY LDYLEGIFCY FPPNLLPLAI TLYVFWLLYL FLILGVTAAK
FFCPNLSAIS TNLKLSHNVA GVTFLAFGNG APDIFSALVA FSDPRTAGLA IGALFGAGVL
VTTVVAGGIT ILHPFMAASR PFLRDIAFYM VAVFLTFTAL YLGRITLTWA LGYLGLYVFY
VVTVIICTWV YQRQRSRSLV HSISETPELL SESEEDQMSS NTNSYDYGDE YRPLLLGRET
TVQILIQALN PLDYRKWRTQ SISWRVLKVV KLPVEFLLLL TVPVVDPDKD DRNWKRPLNC
LQLVISPLVL VLTLQSGVYG IYEIGGLLPV WAVVVIVGTA LASVTFFATS NREPPRLHWL
FAFLGFLTSA LWINAAATEV VNILRSLGVI FRLSNTVLGL TLLAWGNSIG DAFSDFTLAR
QGYPRMAFSA CFGGIIFNIL VGVGLGCLLQ IIRNHVVEVK LEPDGLLVWV LASALGLSLI
FSLVSVPLQC FQLSKAYGLC LLLFYICFLV VVLLTEFGVI HLKKA
