ID NAC2_HUMAN Reviewed; 921 AA. AC Q9UPR5; B4DYQ9; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 27-MAR-2024, entry version 174. DE RecName: Full=Sodium/calcium exchanger 2; DE AltName: Full=Na(+)/Ca(2+)-exchange protein 2; DE AltName: Full=Solute carrier family 8 member 2; DE Flags: Precursor; GN Name=SLC8A2; Synonyms=KIAA1087, NCX2; 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 [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=10470851; DOI=10.1093/dnares/6.3.197; RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:197-205(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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]. 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP REVIEW. RX PubMed=23506867; DOI=10.1016/j.mam.2012.07.003; RA Khananshvili D.; RT "The SLC8 gene family of sodium-calcium exchangers (NCX) - structure, RT function, and regulation in health and disease."; RL Mol. Aspects Med. 34:220-235(2013). RN [5] RP VARIANT LEU-29. RX PubMed=24501278; DOI=10.1093/hmg/ddu056; RA Lee H., Lin M.C., Kornblum H.I., Papazian D.M., Nelson S.F.; RT "Exome sequencing identifies de novo gain of function missense mutation in RT KCND2 in identical twins with autism and seizures that slows potassium RT channel inactivation."; RL Hum. Mol. Genet. 23:3481-3489(2014). CC -!- FUNCTION: Mediates the electrogenic exchange of Ca(2+) against Na(+) CC ions across the cell membrane, and thereby contributes to the CC regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular CC processes. Contributes to cellular Ca(2+) homeostasis in excitable CC cells. Contributes to the rapid decrease of cytoplasmic Ca(2+) levels CC back to baseline after neuronal activation, and thereby contributes to CC modulate synaptic plasticity, learning and memory. Plays a role in CC regulating urinary Ca(2+) and Na(+) excretion. CC {ECO:0000250|UniProtKB:Q8K596}. 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:0000250|UniProtKB:P48768}; CC -!- ACTIVITY REGULATION: Calcium transport is down-regulated by Na(+) and CC stimulated by Ca(2+). {ECO:0000250|UniProtKB:P48768}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48768}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P48768}. Basolateral CC cell membrane {ECO:0000250|UniProtKB:Q8K596}; Multi-pass membrane CC protein {ECO:0000250|UniProtKB:Q8K596}. Perikaryon CC {ECO:0000250|UniProtKB:P48768}. Cell projection, dendrite CC {ECO:0000250|UniProtKB:P48768}. Cell projection, dendritic spine CC {ECO:0000250|UniProtKB:P48768}. CC -!- DOMAIN: The cytoplasmic Calx-beta domains bind the regulatory Ca(2+). CC The first Calx-beta domain can bind up to four Ca(2+) ions. The second CC domain can bind another two Ca(2+) ions that are essential for calcium- CC regulated ion exchange. {ECO:0000250|UniProtKB:P23685}. CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) CC family. SLC8 subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA83039.1; Type=Erroneous initiation; Evidence={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; AB029010; BAA83039.1; ALT_INIT; mRNA. DR EMBL; AK302552; BAG63821.1; -; mRNA. DR EMBL; CH471126; EAW57485.1; -; Genomic_DNA. DR CCDS; CCDS33065.1; -. DR RefSeq; NP_055878.1; NM_015063.2. DR AlphaFoldDB; Q9UPR5; -. DR SMR; Q9UPR5; -. DR BioGRID; 112434; 5. DR IntAct; Q9UPR5; 4. DR MINT; Q9UPR5; -. DR STRING; 9606.ENSP00000236877; -. DR TCDB; 2.A.19.3.5; the ca(2+):cation antiporter (caca) family. DR GlyCosmos; Q9UPR5; 2 sites, No reported glycans. DR GlyGen; Q9UPR5; 2 sites. DR iPTMnet; Q9UPR5; -. DR PhosphoSitePlus; Q9UPR5; -. DR BioMuta; SLC8A2; -. DR EPD; Q9UPR5; -. DR jPOST; Q9UPR5; -. DR MassIVE; Q9UPR5; -. DR MaxQB; Q9UPR5; -. DR PaxDb; 9606-ENSP00000236877; -. DR PeptideAtlas; Q9UPR5; -. DR ProteomicsDB; 85427; -. DR Antibodypedia; 54559; 94 antibodies from 17 providers. DR DNASU; 6543; -. DR Ensembl; ENST00000236877.11; ENSP00000236877.5; ENSG00000118160.14. DR GeneID; 6543; -. DR KEGG; hsa:6543; -. DR MANE-Select; ENST00000236877.11; ENSP00000236877.5; NM_015063.3; NP_055878.1. DR UCSC; uc002pgx.4; human. DR AGR; HGNC:11069; -. DR CTD; 6543; -. DR DisGeNET; 6543; -. DR GeneCards; SLC8A2; -. DR HGNC; HGNC:11069; SLC8A2. DR HPA; ENSG00000118160; Tissue enriched (brain). DR MIM; 601901; gene. DR neXtProt; NX_Q9UPR5; -. DR OpenTargets; ENSG00000118160; -. DR PharmGKB; PA313; -. DR VEuPathDB; HostDB:ENSG00000118160; -. DR eggNOG; KOG1306; Eukaryota. DR GeneTree; ENSGT00940000158344; -. DR HOGENOM; CLU_012872_1_0_1; -. DR InParanoid; Q9UPR5; -. DR OMA; PEDKHQK; -. DR OrthoDB; 462435at2759; -. DR PhylomeDB; Q9UPR5; -. DR TreeFam; TF314308; -. DR PathwayCommons; Q9UPR5; -. DR Reactome; R-HSA-418359; Reduction of cytosolic Ca++ levels. DR Reactome; R-HSA-425561; Sodium/Calcium exchangers. DR Reactome; R-HSA-5578775; Ion homeostasis. DR SignaLink; Q9UPR5; -. DR BioGRID-ORCS; 6543; 12 hits in 1147 CRISPR screens. DR ChiTaRS; SLC8A2; human. DR GenomeRNAi; 6543; -. DR Pharos; Q9UPR5; Tbio. DR PRO; PR:Q9UPR5; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q9UPR5; Protein. DR Bgee; ENSG00000118160; Expressed in right hemisphere of cerebellum and 121 other cell types or tissues. DR ExpressionAtlas; Q9UPR5; baseline and differential. DR GO; GO:0030424; C:axon; ISS:ARUK-UCL. DR GO; GO:0043679; C:axon terminus; ISS:ARUK-UCL. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030425; C:dendrite; ISS:ARUK-UCL. DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell. DR GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL. DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0098794; C:postsynapse; IBA:GO_Central. DR GO; GO:0014069; C:postsynaptic density; ISS:ARUK-UCL. DR GO; GO:0098793; C:presynapse; IDA:ARUK-UCL. DR GO; GO:0042383; C:sarcolemma; IBA:GO_Central. DR GO; GO:0045202; C:synapse; ISS:ARUK-UCL. DR GO; GO:0015085; F:calcium ion transmembrane transporter activity; ISS:ARUK-UCL. DR GO; GO:1905060; F:calcium:monoatomic cation antiporter activity involved in regulation of postsynaptic cytosolic calcium ion concentration; ISS:ARUK-UCL. DR GO; GO:0005432; F:calcium:sodium antiporter activity; ISS:UniProtKB. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; ISS:ARUK-UCL. DR GO; GO:1990034; P:calcium ion export across plasma membrane; ISS:ARUK-UCL. DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central. DR GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB. DR GO; GO:0007154; P:cell communication; IEA:InterPro. DR GO; GO:0050890; P:cognition; ISS:ARUK-UCL. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; ISS:UniProtKB. DR GO; GO:0007612; P:learning; ISS:UniProtKB. DR GO; GO:0007611; P:learning or memory; ISS:ARUK-UCL. DR GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB. DR GO; GO:0007613; P:memory; ISS:UniProtKB. DR GO; GO:0098815; P:modulation of excitatory postsynaptic potential; ISS:ARUK-UCL. DR GO; GO:0006811; P:monoatomic ion transport; TAS:Reactome. DR GO; GO:0070050; P:neuron cellular homeostasis; ISS:ARUK-UCL. DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISS:ARUK-UCL. DR GO; GO:0099608; P:regulation of action potential firing pattern; ISS:ARUK-UCL. DR GO; GO:0106056; P:regulation of calcineurin-mediated signaling; ISS:ARUK-UCL. DR GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome. DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISS:ARUK-UCL. DR GO; GO:0010468; P:regulation of gene expression; ISS:ARUK-UCL. DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:UniProtKB. DR GO; GO:0002931; P:response to ischemia; ISS:ARUK-UCL. DR GO; GO:0035725; P:sodium ion transmembrane transport; ISS:UniProtKB. DR GO; GO:0050808; P:synapse organization; ISS:ARUK-UCL. DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL. DR Gene3D; 2.60.40.2030; -; 2. DR Gene3D; 1.20.1420.30; NCX, central ion-binding region; 2. DR InterPro; IPR038081; CalX-like_sf. DR InterPro; IPR003644; Calx_beta. DR InterPro; IPR004836; Na_Ca_Ex. DR InterPro; IPR032452; Na_Ca_Ex_C-exten. DR InterPro; IPR004837; NaCa_Exmemb. DR InterPro; IPR044880; NCX_ion-bd_dom_sf. DR NCBIfam; TIGR00845; caca; 1. DR PANTHER; PTHR11878; SODIUM/CALCIUM EXCHANGER; 1. DR PANTHER; PTHR11878:SF8; SODIUM_CALCIUM EXCHANGER 2; 1. DR Pfam; PF03160; Calx-beta; 2. DR Pfam; PF01699; Na_Ca_ex; 2. DR Pfam; PF16494; Na_Ca_ex_C; 1. DR PRINTS; PR01259; NACAEXCHNGR. DR SMART; SM00237; Calx_beta; 2. DR SUPFAM; SSF141072; CalX-like; 2. DR Genevisible; Q9UPR5; HS. PE 2: Evidence at transcript level; KW Antiport; Calcium; Calcium transport; Calmodulin-binding; Cell membrane; KW Cell projection; Glycoprotein; Ion transport; Membrane; Metal-binding; KW Phosphoprotein; Reference proteome; Repeat; Signal; Sodium; KW Sodium transport; Synapse; Transmembrane; Transmembrane helix; Transport. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..921 FT /note="Sodium/calcium exchanger 2" FT /id="PRO_0000019382" FT TOPO_DOM 21..68 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 69..90 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 91..130 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 131..152 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 153..164 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 165..185 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 186..196 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 197..219 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 220..222 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 223..246 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 247..720 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 721..740 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 741..747 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 748..770 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 771..772 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 773..791 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 792..822 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 823..843 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 844..854 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 855..875 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 876..892 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 893..909 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 910..921 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 135..175 FT /note="Alpha-1" FT DOMAIN 384..483 FT /note="Calx-beta 1" FT DOMAIN 512..612 FT /note="Calx-beta 2" FT REPEAT 790..826 FT /note="Alpha-2" FT REGION 22..42 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 248..267 FT /note="Putative calmodulin-binding region" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 407 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 407 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 407 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 443 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 443 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 468 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 469 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 469 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 469 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 469 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 471 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 473 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 473 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 473 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 476 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 518 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 519 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 520 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 520 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 536 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 598 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 598 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 599 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 600 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 600 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000250|UniProtKB:P23685" FT BINDING 665 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P23685" FT MOD_RES 622 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8K596" FT CARBOHYD 34 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 817 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 29 FT /note="P -> L (found in a family with atypical autism and FT severe epilepsy; uncertain significance; FT dbSNP:rs201723439)" FT /evidence="ECO:0000269|PubMed:24501278" FT /id="VAR_072078" FT VARIANT 429 FT /note="V -> L (in dbSNP:rs17759929)" FT /id="VAR_050226" SQ SEQUENCE 921 AA; 100368 MW; 798CDF7E32B9410C CRC64; MAPLALVGVT LLLAAPPCSG AATPTPSLPP PPANDSDTST GGCQGSYRCQ PGVLLPVWEP DDPSLGDKAA RAVVYFVAMV YMFLGVSIIA DRFMAAIEVI TSKEKEITIT KANGETSVGT VRIWNETVSN LTLMALGSSA PEILLSVIEV CGHNFQAGEL GPGTIVGSAA FNMFVVIAVC IYVIPAGESR KIKHLRVFFV TASWSIFAYV WLYLILAVFS PGVVQVWEAL LTLVFFPVCV VFAWMADKRL LFYKYVYKRY RTDPRSGIII GAEGDPPKSI ELDGTFVGAE APGELGGLGP GPAEARELDA SRREVIQILK DLKQKHPDKD LEQLVGIANY YALLHQQKSR AFYRIQATRL MTGAGNVLRR HAADASRRAA PAEGAGEDED DGASRIFFEP SLYHCLENCG SVLLSVTCQG GEGNSTFYVD YRTEDGSAKA GSDYEYSEGT LVFKPGETQK ELRIGIIDDD IFEEDEHFFV RLLNLRVGDA QGMFEPDGGG RPKGRLVAPL LATVTILDDD HAGIFSFQDR LLHVSECMGT VDVRVVRSSG ARGTVRLPYR TVDGTARGGG VHYEDACGEL EFGDDETMKT LQVKIVDDEE YEKKDNFFIE LGQPQWLKRG ISALLLNQGD GDRKLTAEEE EARRIAEMGK PVLGENCRLE VIIEESYDFK NTVDKLIKKT NLALVIGTHS WREQFLEAIT VSAGDEEEEE DGSREERLPS CFDYVMHFLT VFWKVLFACV PPTEYCHGWA CFGVSILVIG LLTALIGDLA SHFGCTVGLK DSVNAVVFVA LGTSIPDTFA SKVAALQDQC ADASIGNVTG SNAVNVFLGL GVAWSVAAVY WAVQGRPFEV RTGTLAFSVT LFTVFAFVGI AVLLYRRRPH IGGELGGPRG PKLATTALFL GLWLLYILFA SLEAYCHIRG F //