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Voltage-dependent calcium channel subunit alpha-2/delta-2 (Protein ducky) (Voltage-gated calcium channel subunit alpha-2/delta-2) [Cleaved into: Voltage-dependent calcium channel subunit alpha-2-2; Voltage-dependent calcium channel subunit delta-2]

 CA2D2_MOUSE             Reviewed;        1154 AA.
Q6PHS9; B2RY16; Q3TPT9; Q3TSS6; Q6REE3; Q8C8R8; Q8CHE9; Q920H5;
Q920H6; Q9EQG2; Q9R142;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
12-SEP-2018, entry version 113.
RecName: Full=Voltage-dependent calcium channel subunit alpha-2/delta-2;
AltName: Full=Protein ducky;
AltName: Full=Voltage-gated calcium channel subunit alpha-2/delta-2;
Contains:
RecName: Full=Voltage-dependent calcium channel subunit alpha-2-2;
Contains:
RecName: Full=Voltage-dependent calcium channel subunit delta-2;
Flags: Precursor;
Name=Cacna2d2; Synonyms=Kiaa0558;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
STRAIN=TKDU;
PubMed=11130987; DOI=10.1007/s003350010211;
Barclay J., Rees M.;
"Genomic organization of the mouse and human alpha2delta2 voltage-
dependent calcium channel subunit genes.";
Mamm. Genome 11:1142-1144(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND INVOLVEMENT IN DU.
STRAIN=TKDU;
PubMed=11487633;
Barclay J., Balaguero N., Mione M., Ackerman S.L., Letts V.A.,
Brodbeck J., Canti C., Meir A., Page K.M., Kusumi K., Perez-Reyes E.,
Lander E.S., Frankel W.N., Gardiner R.M., Dolphin A.C., Rees M.;
"Ducky mouse phenotype of epilepsy and ataxia is associated with
mutations in the Cacna2d2 gene and decreased calcium channel current
in cerebellar Purkinje cells.";
J. Neurosci. 21:6095-6104(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANT
VARIANT ILE-TYR-LYS-ASP-ASN-ARG-ASN-LEU-PHE-GLU-VAL-GLN-GLU-ASN-GLU-
PRO-GLN-LYS-LEU-VAL-GLU-LYS-VAL-ALA-GLY-ASP-ILE-GLU-SER-LEU-LEU-ASP-
ARG-LYS-VAL-GLN-ALA-LEU-LYS-99 INS.
STRAIN=DBA/2J;
PubMed=14660671; DOI=10.1074/jbc.M308778200;
Brill J., Klocke R., Paul D., Boison D., Gouder N., Klugbauer N.,
Hofmann F., Becker C.-M., Becker K.;
"entla, a novel epileptic and ataxic Cacna2d2 mutant of the mouse.";
J. Biol. Chem. 279:7322-7330(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 788-1154 (ISOFORM 6).
STRAIN=C57BL/6J; TISSUE=Hippocampus, Medulla oblongata, and Retina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 53-1154 (ISOFORM 5).
PubMed=12465718; DOI=10.1093/dnares/9.5.179;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
I. The complete nucleotide sequences of 100 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 9:179-188(2002).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 932-1154.
PubMed=10766861; DOI=10.1074/jbc.275.16.12237;
Gao B., Sekido Y., Maximov A., Saad M., Forgacs E., Latif F.,
Wei M.-H., Lerman M., Lee J.-H., Perez-Reyes E., Bezprozvanny I.,
Minna J.D.;
"Functional properties of a new voltage-dependent calcium channel
alpha(2)delta auxiliary subunit gene (CACNA2D2).";
J. Biol. Chem. 275:12237-12242(2000).
[8]
TISSUE SPECIFICITY.
PubMed=10762351; DOI=10.1046/j.1460-9568.2000.01009.x;
Hobom M., Dai S., Marais E., Lacinova L., Hofmann F., Klugbauer N.;
"Neuronal distribution and functional characterization of the calcium
channel alpha2delta-2 subunit.";
Eur. J. Neurosci. 12:1217-1226(2000).
[9]
DISULFIDE BONDS, GLYCOSYLATION, PROTEOLYTIC PROCESSING, AND
GABAPENTIN-BINDING.
PubMed=11306709;
Marais E., Klugbauer N., Hofmann F.;
"Calcium channel alpha(2)delta subunits-structure and Gabapentin
binding.";
Mol. Pharmacol. 59:1243-1248(2001).
[10]
SUBCELLULAR LOCATION, AND INVOLVEMENT IN DU.
PubMed=11756448; DOI=10.1074/jbc.M109404200;
Brodbeck J., Davies A., Courtney J.-M., Meir A., Balaguero N.,
Canti C., Moss F.J., Page K.M., Pratt W.S., Hunt S.P., Barclay J.,
Rees M., Dolphin A.C.;
"The ducky mutation in Cacna2d2 results in altered Purkinje cell
morphology and is associated with the expression of a truncated alpha
2 delta-2 protein with abnormal function.";
J. Biol. Chem. 277:7684-7693(2002).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15331424; DOI=10.1016/S0002-9440(10)63362-7;
Ivanov S.V., Ward J.M., Tessarollo L., McAreavey D., Sachdev V.,
Fananapazir L., Banks M.K., Morris N., Djurickovic D.,
Devor-Henneman D.E., Wei M.-H., Alvord G.W., Gao B., Richardson J.A.,
Minna J.D., Rogawski M.A., Lerman M.I.;
"Cerebellar ataxia, seizures, premature death, and cardiac
abnormalities in mice with targeted disruption of the Cacna2d2 gene.";
Am. J. Pathol. 165:1007-1018(2004).
[12]
METAL-BINDING, MIDAS-LIKE MOTIF, AND MUTAGENESIS OF ASP-300; SER-302
AND SER-304.
PubMed=16061813; DOI=10.1073/pnas.0504183102;
Canti C., Nieto-Rostro M., Foucault I., Heblich F., Wratten J.,
Richards M.W., Hendrich J., Douglas L., Page K.M., Davies A.,
Dolphin A.C.;
"The metal-ion-dependent adhesion site in the Von Willebrand factor-A
domain of alpha2delta subunits is key to trafficking voltage-gated
Ca2+ channels.";
Proc. Natl. Acad. Sci. U.S.A. 102:11230-11235(2005).
[13]
GLYCOSYLATION, AND LACK OF PROTEOLYTIC PROCESSING.
PubMed=17052222; DOI=10.1042/BST0340894;
Douglas L., Davies A., Wratten J., Dolphin A.C.;
"Do voltage-gated calcium channel alpha2delta subunits require
proteolytic processing into alpha2 and delta to be functional?";
Biochem. Soc. Trans. 34:894-898(2006).
[14]
SUBCELLULAR LOCATION, INTERACTION WITH STOML2, GABAPENTIN-BINDING, AND
MUTAGENESIS OF ARG-282.
PubMed=16928863; DOI=10.1523/JNEUROSCI.2764-06.2006;
Davies A., Douglas L., Hendrich J., Wratten J., Tran Van Minh A.,
Foucault I., Koch D., Pratt W.S., Saibil H.R., Dolphin A.C.;
"The calcium channel alpha2delta-2 subunit partitions with CaV2.1 into
lipid rafts in cerebellum: implications for localization and
function.";
J. Neurosci. 26:8748-8757(2006).
[15]
INVOLVEMENT IN DU.
PubMed=17135419; DOI=10.1523/JNEUROSCI.3080-06.2006;
Donato R., Page K.M., Koch D., Nieto-Rostro M., Foucault I.,
Davies A., Wilkinson T., Rees M., Edwards F.A., Dolphin A.C.;
"The ducky(2J) mutation in Cacna2d2 results in reduced spontaneous
Purkinje cell activity and altered gene expression.";
J. Neurosci. 26:12576-12586(2006).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Heart;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium
channels regulates calcium current density and
activation/inactivation kinetics of the calcium channel. Acts as a
regulatory subunit for P/Q-type calcium channel (CACNA1A), N-type
(CACNA1B), L-type (CACNA1C OR CACNA1D) and possibly T-type
(CACNA1G). {ECO:0000269|PubMed:15331424}.
-!- SUBUNIT: Dimer formed of alpha-2-2 and delta-2 chains; disulfide-
linked. Voltage-dependent calcium channels are multisubunit
complexes, consisting of alpha-1 (CACNA1), alpha-2 (CACNA2D), beta
(CACNB) and delta (CACNA2D) subunits in a 1:1:1:1 ratio
(Probable). {ECO:0000305|PubMed:11306709}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}. Note=Colocalizes with CACNA1A in
lipid raft fractions. {ECO:0000269|PubMed:11756448,
ECO:0000269|PubMed:16928863}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=Alpha2delta-2a;
IsoId=Q6PHS9-1; Sequence=Displayed;
Name=2;
IsoId=Q6PHS9-2; Sequence=VSP_028061, VSP_028062;
Name=3; Synonyms=Alpha2delta-2c;
IsoId=Q6PHS9-3; Sequence=VSP_028063;
Name=4; Synonyms=Alpha2delta-2b;
IsoId=Q6PHS9-4; Sequence=VSP_028061;
Name=5;
IsoId=Q6PHS9-5; Sequence=VSP_028061, VSP_028062, VSP_028063;
Name=6;
IsoId=Q6PHS9-6; Sequence=VSP_028062, VSP_028063;
-!- TISSUE SPECIFICITY: Predominantly expressed in brain in a
restricted pattern. Also expressed at lower level in kidney and
testis Not expressed in lung at any moment of development. In
brain, it localizes to sections of P21 brain. Expressed at high
level in the cerebellum, with moderate levels in medulla, pons,
and striatum. Also expressed in cortex, hippocampus, habenula and
nucleus reticularis thalami (nRT). Strongly expressed in
cerebellar Purkinje cells. {ECO:0000269|PubMed:10762351}.
-!- DOMAIN: The MIDAS-like motif in the VWFA domain binds divalent
metal cations and is required to promote trafficking of the alpha-
1 (CACNA1) subunit to the plasma membrane by an integrin-like
switch.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:11306709,
ECO:0000269|PubMed:17052222}.
-!- PTM: May be proteolytically processed into subunits alpha-2-2 and
delta-2 that are disulfide-linked. It is however unclear whether
such cleavage really takes place in vivo and has a functional
role. According to PubMed:11306709, it is processed, at least in
vitro, while according to PubMed:17052222, it is only poorly
processed in vivo. {ECO:0000269|PubMed:11306709}.
-!- DISEASE: Note=Defects in Cacna2d2 are the cause of ducky phenotype
(du). Du mice have spike-wave seizures characteristic of absence
epilepsy and ataxia, with accompanying decreased calcium channel
current in cerebellar Purkinje cells.
{ECO:0000269|PubMed:11487633, ECO:0000269|PubMed:11756448,
ECO:0000269|PubMed:14660671, ECO:0000269|PubMed:17135419}.
-!- DISRUPTION PHENOTYPE: Mice exhibit growth retardation, reduced
life span, ataxic gait with apoptosis of cerebellar granule cells
followed by Purkinje cell depletion, enhanced susceptibility to
seizures, and cardiac abnormalities.
{ECO:0000269|PubMed:15331424}.
-!- MISCELLANEOUS: Binds gabapentin, an antiepileptic drug.
-!- SIMILARITY: Belongs to the calcium channel subunit alpha-2/delta
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAL01651.1; Type=Frameshift; Positions=301; Evidence={ECO:0000305};
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EMBL; AF247139; AAG47846.1; -; mRNA.
EMBL; AF247141; AAL01650.1; -; mRNA.
EMBL; AF247142; AAL01651.1; ALT_FRAME; mRNA.
EMBL; AY502107; AAR89454.1; -; mRNA.
EMBL; AK044603; BAC31998.1; -; mRNA.
EMBL; AK164143; BAE37646.1; -; mRNA.
EMBL; AK161839; BAE36599.1; -; mRNA.
EMBL; BC056389; AAH56389.1; -; mRNA.
EMBL; BC158058; AAI58059.1; -; mRNA.
EMBL; AB093246; BAC41430.1; -; mRNA.
EMBL; AF169633; AAD48037.1; -; mRNA.
CCDS; CCDS52916.1; -. [Q6PHS9-1]
CCDS; CCDS52917.1; -. [Q6PHS9-2]
CCDS; CCDS72304.1; -. [Q6PHS9-3]
CCDS; CCDS72305.1; -. [Q6PHS9-5]
RefSeq; NP_001167518.1; NM_001174047.1. [Q6PHS9-3]
RefSeq; NP_001167519.1; NM_001174048.1. [Q6PHS9-5]
RefSeq; NP_001167520.1; NM_001174049.1. [Q6PHS9-4]
RefSeq; NP_001167521.1; NM_001174050.1. [Q6PHS9-2]
RefSeq; NP_064659.2; NM_020263.3. [Q6PHS9-1]
RefSeq; XP_011241201.1; XM_011242899.2. [Q6PHS9-6]
UniGene; Mm.273084; -.
ProteinModelPortal; Q6PHS9; -.
IntAct; Q6PHS9; 1.
STRING; 10090.ENSMUSP00000082173; -.
PhosphoSitePlus; Q6PHS9; -.
PaxDb; Q6PHS9; -.
PRIDE; Q6PHS9; -.
Ensembl; ENSMUST00000010210; ENSMUSP00000010210; ENSMUSG00000010066. [Q6PHS9-2]
Ensembl; ENSMUST00000085092; ENSMUSP00000082173; ENSMUSG00000010066. [Q6PHS9-1]
Ensembl; ENSMUST00000166799; ENSMUSP00000126029; ENSMUSG00000010066. [Q6PHS9-6]
Ensembl; ENSMUST00000168532; ENSMUSP00000132512; ENSMUSG00000010066. [Q6PHS9-3]
Ensembl; ENSMUST00000170737; ENSMUSP00000125943; ENSMUSG00000010066. [Q6PHS9-5]
GeneID; 56808; -.
KEGG; mmu:56808; -.
UCSC; uc009rli.2; mouse. [Q6PHS9-2]
UCSC; uc009rlj.2; mouse. [Q6PHS9-4]
UCSC; uc012haf.1; mouse. [Q6PHS9-1]
UCSC; uc057apw.1; mouse. [Q6PHS9-3]
UCSC; uc057apx.1; mouse. [Q6PHS9-5]
CTD; 9254; -.
MGI; MGI:1929813; Cacna2d2.
eggNOG; KOG2353; Eukaryota.
eggNOG; ENOG410XPDX; LUCA.
GeneTree; ENSGT00530000062904; -.
HOVERGEN; HBG057779; -.
InParanoid; Q6PHS9; -.
KO; K04859; -.
PhylomeDB; Q6PHS9; -.
TreeFam; TF315824; -.
Reactome; R-MMU-112308; Presynaptic depolarization and calcium channel opening.
Reactome; R-MMU-422356; Regulation of insulin secretion.
Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
Reactome; R-MMU-5576893; Phase 2 - plateau phase.
PRO; PR:Q6PHS9; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000010066; Expressed in 260 organ(s), highest expression level in heart.
ExpressionAtlas; Q6PHS9; baseline and differential.
Genevisible; Q6PHS9; MM.
GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:MGI.
GO; GO:0006816; P:calcium ion transport; ISO:MGI.
GO; GO:0048747; P:muscle fiber development; IMP:MGI.
GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
GO; GO:0046622; P:positive regulation of organ growth; IMP:MGI.
GO; GO:0008016; P:regulation of heart contraction; ISO:MGI.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
GO; GO:0060024; P:rhythmic synaptic transmission; IMP:MGI.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR013680; VDCC_a2/dsu.
InterPro; IPR013608; VWA_N.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF08473; VGCC_alpha2; 1.
Pfam; PF00092; VWA; 1.
Pfam; PF08399; VWA_N; 1.
SMART; SM00327; VWA; 1.
SUPFAM; SSF53300; SSF53300; 1.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Calcium channel; Calcium transport;
Complete proteome; Disease mutation; Disulfide bond; Glycoprotein;
Ion channel; Ion transport; Membrane; Metal-binding;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Transport; Voltage-gated channel.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 1154 Voltage-dependent calcium channel subunit
alpha-2/delta-2.
/FTId=PRO_0000304640.
CHAIN 19 1004 Voltage-dependent calcium channel subunit
alpha-2-2. {ECO:0000255}.
/FTId=PRO_0000304641.
CHAIN 1005 1154 Voltage-dependent calcium channel subunit
delta-2. {ECO:0000255}.
/FTId=PRO_0000304642.
TOPO_DOM 19 1116 Extracellular. {ECO:0000255}.
TRANSMEM 1117 1137 Helical. {ECO:0000255}.
TOPO_DOM 1138 1154 Cytoplasmic. {ECO:0000255}.
DOMAIN 294 472 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 488 577 Cache.
MOTIF 300 304 MIDAS-like motif.
METAL 300 300 Divalent metal cation. {ECO:0000305}.
METAL 302 302 Divalent metal cation. {ECO:0000305}.
METAL 304 304 Divalent metal cation. {ECO:0000305}.
CARBOHYD 205 205 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 389 389 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 421 421 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 510 510 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 543 543 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 627 627 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 864 864 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 446 1101 Interchain (between alpha-2-2 and delta-2
chains). {ECO:0000250}.
VAR_SEQ 665 672 LPISKLKD -> Y (in isoform 2, isoform 4
and isoform 5).
{ECO:0000303|PubMed:12465718,
ECO:0000303|PubMed:14660671,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_028061.
VAR_SEQ 873 873 K -> KQ (in isoform 2, isoform 5 and
isoform 6). {ECO:0000303|PubMed:12465718,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_028062.
VAR_SEQ 1079 1080 HS -> HCPA (in isoform 3, isoform 5 and
isoform 6). {ECO:0000303|PubMed:11130987,
ECO:0000303|PubMed:11487633,
ECO:0000303|PubMed:12465718,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_028063.
VARIANT 99 99 E -> EIYKDNRNLFEVQENEPQKLVEKVAGDIESLLDRKV
QALK (in du; variant allele entla).
MUTAGEN 282 282 R->A: Induces a strong decrease in
gabapentin-binding.
{ECO:0000269|PubMed:16928863}.
MUTAGEN 300 300 D->A: Abolishes metal-binding and ability
to regulate calcium current.
{ECO:0000269|PubMed:16061813}.
MUTAGEN 302 302 S->A: Abolishes metal-binding and ability
to regulate calcium current.
{ECO:0000269|PubMed:16061813}.
MUTAGEN 304 304 S->A: Abolishes metal-binding and ability
to regulate calcium current.
{ECO:0000269|PubMed:16061813}.
CONFLICT 657 657 S -> R (in Ref. 1; AAG47846, 2; AAL01650
and 3; AAR89454). {ECO:0000305}.
CONFLICT 704 704 N -> S (in Ref. 1; AAG47846, 2; AAL01650
and 3; AAR89454). {ECO:0000305}.
CONFLICT 710 710 N -> D (in Ref. 1; AAG47846, 2; AAL01650
and 3; AAR89454). {ECO:0000305}.
SEQUENCE 1154 AA; 130385 MW; AE4F646D89A96053 CRC64;
MAVPARTCGA SWPGPVRTAR PWPGRGPRPC PDPRGPASGP ARPLLLLLPP LLLLPLLTAP
GASAYSFPQQ HTMQHWARRL EQEIDGVMRI FGGVQQLREI YKDNRNLFEV QENEPQKLVE
KVAGDIESLL DRKVQALKRL ADAAENFQKA HRWQDNIKEE DIMYYDAKAD AELDDPESED
MERGSKTSAL RLDFIEDPNF KNKVNYSYTA VQIPTDIYKG STVILNELNW TEALENVFIE
NRRQDPTLLW QVFGSATGVT RYYPATPWRA PKKIDLYDVR RRPWYIQGAS SPKDMVIIVD
VSGSVSGLTL KLMKTSVCEM LDTLSDDDYV NVASFNEKAQ PVSCFTHLVQ ANVRNKKVFK
EAVQGMVAKG TTGYKAGFEY AFDQLQNSNI TRANCNKMIM MFTDGGEDRV QDVFEKYNWP
NRTVRVFTFS VGQHNYDVTP LQWMACTNKG YYFEIPSIGA IRINTQEYLD VLGRPMVLAG
KDAKQVQWTN VYEDALGLGL VVTGTLPVFN LTQDGPGEKK NQLILGVMGI DVALNDIKRL
TPNYTLGANG YVFAIDLNGY VLLHPNLKPQ TTNFREPVTL DFLDAELEDE NKEEIRRSMI
DGDKGHKQIR TLVKSLDERY IDEVIRNYTW VPIRSTNYSL GLVLPPYSTY YLQANLSDQI
LQVKLPISKL KDFEFLLPSS FESEGHVFIA PREYCKDLNA SDNNTEFLKN FIELMEKVTP
DSKQCNNFLL HNLILDTGIT QQLVERVWRD QDLNTYSLLA VFAATDGGIT RVFPNKAAED
WTENPEPFNA SFYRRSLDNH GYIFKPPHQD SLLRPLELEN DTVGVLVSTA VELSLGRRTL
RPAVVGVKLD LEAWAEKFKV LASNRTHQDQ PQKCGPSSHC EMDCEVNNED LLCVLIDDGG
FLVLSNQNHQ WDQVGRFFSE VDANLMLALY NNSFYTRKES YDYQAACAPQ PPGNLGAAPR
GVFVPTIADF LNLAWWTSAA AWSLFQQLLY GLIYHSWFQA DPAEAEGSPE TRESSCVMKQ
TQYYFGSVNA SYNAIIDCGN CSRLFHAQRL TNTNLLFVVA EKPLCSQCEA GRLLQKETHS
DGPEQCELVQ RPRYRRGPHI CFDYNATEDT SDCGRGASFP PSLGVLVSLQ LLLLLGLPPR
PQPQVHSFAA SRHL


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