NAC2_HUMAN
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 03-AUG-2022, entry version 165.
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};
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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 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; Q9UPR5; -.
DR PeptideAtlas; Q9UPR5; -.
DR PRIDE; Q9UPR5; -.
DR ProteomicsDB; 85427; -.
DR Antibodypedia; 54559; 82 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 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; HRQEFIE; -.
DR OrthoDB; 490546at2759; -.
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; 9 hits in 1069 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 119 other tissues.
DR ExpressionAtlas; Q9UPR5; baseline and differential.
DR Genevisible; Q9UPR5; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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; TAS:Reactome.
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: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:0015491; F:cation:cation antiporter activity; IBA:GO_Central.
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:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0050890; P:cognition; ISS:ARUK-UCL.
DR GO; GO:0006811; P:ion transport; TAS:Reactome.
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:0030001; P:metal ion transport; IBA:GO_Central.
DR GO; GO:0098815; P:modulation of excitatory postsynaptic potential; ISS:ARUK-UCL.
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; 1.20.1420.30; -; 2.
DR Gene3D; 2.60.40.2030; -; 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 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; SSF141072; 2.
DR TIGRFAMs; TIGR00845; caca; 1.
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; unknown pathological 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
