KCNQ2_MOUSE
ID KCNQ2_MOUSE Reviewed; 759 AA.
AC Q9Z351; Q3UTI0; Q8R498; Q9QWN9; Q9Z342; Q9Z343; Q9Z344; Q9Z345; Q9Z346;
AC Q9Z347; Q9Z348; Q9Z349; Q9Z350;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 177.
DE RecName: Full=Potassium voltage-gated channel subfamily KQT member 2 {ECO:0000305};
DE AltName: Full=KQT-like 2 {ECO:0000303|PubMed:12223552};
DE AltName: Full=Potassium channel subunit alpha KvLQT2;
DE AltName: Full=Voltage-gated potassium channel subunit Kv7.2;
GN Name=Kcnq2 {ECO:0000312|MGI:MGI:1309503};
GN Synonyms=Kqt2 {ECO:0000303|PubMed:9666519};
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] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 10 AND 11).
RC TISSUE=Brain;
RX PubMed=9666519;
RA Nakamura M., Watanabe H., Kubo Y., Yokoyama M., Matsumoto T., Sasai H.,
RA Nishi Y.;
RT "KQT2, a new putative potassium channel family produced by alternative
RT splicing. Isolation, genomic structure, and alternative splicing of the
RT putative potassium channels.";
RL Recept. Channels 5:255-271(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12), FUNCTION, INTERACTION WITH
RP CALMODULIN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-345; LYS-525 AND
RP ARG-526.
RC STRAIN=BALB/cJ;
RX PubMed=12223552; DOI=10.1523/jneurosci.22-18-07991.2002;
RA Wen H., Levitan I.B.;
RT "Calmodulin is an auxiliary subunit of KCNQ2/3 potassium channels.";
RL J. Neurosci. 22:7991-8001(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-759 (ISOFORM 13).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
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 [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=10854243; DOI=10.1046/j.1471-4159.2000.0750028.x;
RA Watanabe H., Nagata E., Kosakai A., Nakamura M., Yokoyama M., Tanaka K.,
RA Sasai H.;
RT "Disruption of the epilepsy KCNQ2 gene results in neural
RT hyperexcitability.";
RL J. Neurochem. 75:28-33(2000).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438; SER-440; SER-444;
RP SER-448 AND SER-450, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-831
RP (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-813 (ISOFORM
RP 13), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 INTERACTION WITH IQCJ-SCHIP1.
RX PubMed=27979964; DOI=10.1074/jbc.m116.758029;
RA Martin P.M., Cifuentes-Diaz C., Devaux J., Garcia M., Bureau J.,
RA Thomasseau S., Klingler E., Girault J.A., Goutebroze L.;
RT "Schwannomin-interacting protein 1 isoform IQCJ-SCHIP1 is a multipartner
RT ankyrin- and spectrin-binding protein involved in the organization of nodes
RT of Ranvier.";
RL J. Biol. Chem. 292:2441-2456(2017).
CC -!- FUNCTION: Associates with KCNQ3 to form a potassium channel with
CC essentially identical properties to the channel underlying the native
CC M-current, a slowly activating and deactivating potassium conductance
CC which plays a critical role in determining the subthreshold electrical
CC excitability of neurons as well as the responsiveness to synaptic
CC inputs. Therefore, it is important in the regulation of neuronal
CC excitability. {ECO:0000269|PubMed:12223552}.
CC -!- SUBUNIT: Heterotetramer with KCNQ3; form the heterotetrameric M
CC potassium channel (By similarity). Interacts with calmodulin; the
CC interaction is calcium-independent, constitutive and participates in
CC the proper assembly of a functional heterotetrameric M channel
CC (PubMed:12223552). May associate with KCNE2 (By similarity). Interacts
CC with IQCJ-SCHIP1 (PubMed:27979964). {ECO:0000250|UniProtKB:O43526,
CC ECO:0000269|PubMed:12223552, ECO:0000269|PubMed:27979964}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12223552};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=13;
CC Name=1; Synonyms=MKQT2.1;
CC IsoId=Q9Z351-1; Sequence=Displayed;
CC Name=2; Synonyms=MKQT2.2;
CC IsoId=Q9Z351-2; Sequence=VSP_001001;
CC Name=3; Synonyms=MKQT2.3;
CC IsoId=Q9Z351-3; Sequence=VSP_001000;
CC Name=4; Synonyms=MKQT2.4;
CC IsoId=Q9Z351-4; Sequence=VSP_001002;
CC Name=5; Synonyms=MKQT2.5;
CC IsoId=Q9Z351-5; Sequence=VSP_001003, VSP_001004;
CC Name=6; Synonyms=MKQT2.6;
CC IsoId=Q9Z351-6; Sequence=VSP_001005, VSP_001006;
CC Name=7; Synonyms=MKQT2.7;
CC IsoId=Q9Z351-7; Sequence=VSP_000997, VSP_000998, VSP_000999;
CC Name=8; Synonyms=MKQT2.8;
CC IsoId=Q9Z351-8; Sequence=VSP_000998, VSP_000999;
CC Name=9; Synonyms=MKQT2.9;
CC IsoId=Q9Z351-9; Sequence=VSP_000993, VSP_000994;
CC Name=10; Synonyms=MKQT2.10;
CC IsoId=Q9Z351-10; Sequence=VSP_000995, VSP_000996;
CC Name=11; Synonyms=MKQT2.11;
CC IsoId=Q9Z351-11; Sequence=VSP_000991, VSP_000992;
CC Name=12;
CC IsoId=Q9Z351-12; Sequence=VSP_000997, VSP_012365, VSP_001002,
CC VSP_012366;
CC Name=13;
CC IsoId=Q9Z351-13; Sequence=VSP_000997, VSP_022637, VSP_012366;
CC -!- TISSUE SPECIFICITY: Exclusively expressed in the brain. Expressed in
CC every neuron-containing regions of the central nervous system examined,
CC such as the cerebellum, cerebral cortex, occipital pole, substantia
CC nigra, amygdala, caudate nucleus, hippocampus and thalamus. Also
CC detected in the cochlea.
CC -!- DEVELOPMENTAL STAGE: Detected at day 11, 15 and 17 of the embryonic
CC development. Expression increases by a factor of 2.5 at 1 week after
CC birth. Then the expression level remains stable until the adult stage.
CC The mRNAs for shorter forms (isoforms 9, 10 and 11) are specifically
CC expressed in an embryo on the 11th day after gestation.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position. {ECO:0000250}.
CC -!- PTM: KCNQ2/KCNQ3 heteromeric current can be increased by intracellular
CC cyclic AMP, an effect that depends on phosphorylation of Ser-52 in the
CC N-terminal region. {ECO:0000250|UniProtKB:O43526}.
CC -!- PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to
CC protein degradation. Degradation induced by NEDD4L is inhibited by
CC USP36. {ECO:0000250|UniProtKB:O43526}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Kcnq2 present no overt phenotype,
CC but die a few hours after birth of pulmonary atelectasis which is not
CC due to the status of epileptic seizures. {ECO:0000269|PubMed:10854243}.
CC -!- MISCELLANEOUS: [Isoform 6]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 8]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 9]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 10]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 11]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the potassium channel family. KQT (TC 1.A.1.15)
CC subfamily. Kv7.2/KCNQ2 sub-subfamily. {ECO:0000305}.
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DR EMBL; AB000494; BAA37156.1; -; mRNA.
DR EMBL; AB000495; BAA37157.1; -; mRNA.
DR EMBL; AB000496; BAA37158.1; -; mRNA.
DR EMBL; AB000497; BAA37159.1; -; mRNA.
DR EMBL; AB000498; BAA37160.1; -; mRNA.
DR EMBL; AB000499; BAA37161.1; -; mRNA.
DR EMBL; AB000500; BAA37162.1; -; mRNA.
DR EMBL; AB000501; BAA37163.1; -; mRNA.
DR EMBL; AB000502; BAA37164.1; -; mRNA.
DR EMBL; AB000503; BAA37165.1; -; mRNA.
DR EMBL; AB000504; BAA37166.1; -; mRNA.
DR EMBL; AF490773; AAM09696.1; -; mRNA.
DR EMBL; AK139411; BAE24000.1; -; mRNA.
DR CCDS; CCDS17193.1; -. [Q9Z351-1]
DR CCDS; CCDS17194.1; -. [Q9Z351-2]
DR CCDS; CCDS17195.1; -. [Q9Z351-3]
DR CCDS; CCDS17196.1; -. [Q9Z351-4]
DR CCDS; CCDS17197.1; -. [Q9Z351-5]
DR CCDS; CCDS17198.1; -. [Q9Z351-12]
DR RefSeq; NP_001006675.1; NM_001006674.2.
DR RefSeq; NP_001289817.1; NM_001302888.1.
DR RefSeq; NP_034741.2; NM_010611.3.
DR AlphaFoldDB; Q9Z351; -.
DR SMR; Q9Z351; -.
DR BioGRID; 200918; 14.
DR CORUM; Q9Z351; -.
DR IntAct; Q9Z351; 2.
DR STRING; 10090.ENSMUSP00000122915; -.
DR BindingDB; Q9Z351; -.
DR ChEMBL; CHEMBL2985; -.
DR DrugCentral; Q9Z351; -.
DR iPTMnet; Q9Z351; -.
DR PhosphoSitePlus; Q9Z351; -.
DR PRIDE; Q9Z351; -.
DR ProteomicsDB; 263404; -. [Q9Z351-1]
DR ProteomicsDB; 263405; -. [Q9Z351-2]
DR ProteomicsDB; 263406; -. [Q9Z351-3]
DR ProteomicsDB; 263407; -. [Q9Z351-4]
DR ProteomicsDB; 263408; -. [Q9Z351-5]
DR ProteomicsDB; 263409; -. [Q9Z351-6]
DR ProteomicsDB; 263410; -. [Q9Z351-7]
DR ProteomicsDB; 263411; -. [Q9Z351-8]
DR ProteomicsDB; 263412; -. [Q9Z351-9]
DR ProteomicsDB; 263413; -. [Q9Z351-10]
DR ProteomicsDB; 263414; -. [Q9Z351-11]
DR ProteomicsDB; 263415; -. [Q9Z351-12]
DR ProteomicsDB; 263416; -. [Q9Z351-13]
DR ABCD; Q9Z351; 1 sequenced antibody.
DR DNASU; 16536; -.
DR GeneID; 16536; -.
DR KEGG; mmu:16536; -.
DR UCSC; uc008olg.2; mouse. [Q9Z351-11]
DR CTD; 3785; -.
DR MGI; MGI:1309503; Kcnq2.
DR eggNOG; KOG1419; Eukaryota.
DR InParanoid; Q9Z351; -.
DR OrthoDB; 1168835at2759; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 16536; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q9Z351; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9Z351; protein.
DR GO; GO:0043194; C:axon initial segment; IDA:BHF-UCL.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0033268; C:node of Ranvier; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IGI:MGI.
DR GO; GO:0030506; F:ankyrin binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IPI:MGI.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IGI:MGI.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
DR InterPro; IPR003947; K_chnl_volt-dep_KCNQ2.
DR InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
DR InterPro; IPR028325; VG_K_chnl.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR PANTHER; PTHR11537:SF6; PTHR11537:SF6; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF03520; KCNQ_channel; 2.
DR PRINTS; PR01461; KCNQ2CHANNEL.
DR PRINTS; PR01459; KCNQCHANNEL.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..759
FT /note="Potassium voltage-gated channel subfamily KQT member
FT 2"
FT /id="PRO_0000054031"
FT TOPO_DOM 1..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..122
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..197
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..221
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 265..285
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..759
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 317..512
FT /note="Mediates interaction with calmodulin"
FT /evidence="ECO:0000250|UniProtKB:O43526"
FT REGION 393..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 277..282
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 431..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:O43526"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88943"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88943"
FT VAR_SEQ 310..338
FT /note="GILGSGFALKVQEQHRPKHFEKRRNPAAG -> VSPAHLPTLEMLGVLEAPH
FT KAWPWPTCEL (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:9666519"
FT /id="VSP_000991"
FT VAR_SEQ 339..759
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:9666519"
FT /id="VSP_000992"
FT VAR_SEQ 342..349
FT /note="SAWRFYAT -> GQVRCAGH (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:9666519"
FT /id="VSP_000993"
FT VAR_SEQ 342..347
FT /note="SAWRFY -> VSLSPC (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:9666519"
FT /id="VSP_000995"
FT VAR_SEQ 348..759
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:9666519"
FT /id="VSP_000996"
FT VAR_SEQ 350..759
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:9666519"
FT /id="VSP_000994"
FT VAR_SEQ 372
FT /note="Y -> YSSQTQTYGAS (in isoform 7, isoform 12 and
FT isoform 13)"
FT /evidence="ECO:0000303|PubMed:12223552,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9666519"
FT /id="VSP_000997"
FT VAR_SEQ 406..463
FT /note="SQKVSLKDRVFSSPRGMAAKGKGSPQAQTVRRSPSADQSLDDSPSKVPKSWS
FT FGDRSR -> RSVPPASSRPGVCCTHLALLSLCIHHVSWGRATMGPCVCFYVQQVTVCP
FT GTPRVTSQL (in isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:9666519"
FT /id="VSP_000998"
FT VAR_SEQ 406
FT /note="S -> SKGRPCRGCLCGCCPGHSS (in isoform 12)"
FT /evidence="ECO:0000303|PubMed:12223552"
FT /id="VSP_012365"
FT VAR_SEQ 407..418
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9666519"
FT /id="VSP_001000"
FT VAR_SEQ 464..759
FT /note="Missing (in isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:9666519"
FT /id="VSP_000999"
FT VAR_SEQ 562..623
FT /note="IDMIVGPPPPSTPRDKKYPTKGPTAPSRESPQYSPRVDHIVGRGPTITDKDR
FT TKGPAETELP -> QEPLPVQSGHEQGPPGQNQAWHKGHQGLGDRCAEQGQYQLWRSLP
FT TLLASCCFLLCFHTVCF (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:9666519"
FT /id="VSP_001005"
FT VAR_SEQ 562..597
FT /note="Missing (in isoform 4 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:12223552,
FT ECO:0000303|PubMed:9666519"
FT /id="VSP_001002"
FT VAR_SEQ 562..596
FT /note="IDMIVGPPPPSTPRDKKYPTKGPTAPSRESPQYSP -> QEPLPVQSGHEQG
FT PPGQNQAWHKGHQGLGD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9666519"
FT /id="VSP_001001"
FT VAR_SEQ 562..570
FT /note="IDMIVGPPP -> SCDWRGVLA (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9666519"
FT /id="VSP_001003"
FT VAR_SEQ 571..759
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9666519"
FT /id="VSP_001004"
FT VAR_SEQ 571..606
FT /note="Missing (in isoform 13)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022637"
FT VAR_SEQ 624..759
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:9666519"
FT /id="VSP_001006"
FT VAR_SEQ 747..759
FT /note="LRLERSAGMMSCH -> RIPPPPAHERSLSAYGGGNRASTEFLRLEGTPACR
FT PSEAALRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALGSCYAAVAPCAKVRPYI
FT AEGESDTDSDLCTPCGPPPRSATGEGPFGDVAWAGPRK (in isoform 12 and
FT isoform 13)"
FT /evidence="ECO:0000303|PubMed:12223552,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_012366"
FT MUTAGEN 345
FT /note="R->E: Loss of interaction with calmodulin."
FT /evidence="ECO:0000269|PubMed:12223552"
FT MUTAGEN 525
FT /note="K->E: Loss of interaction with calmodulin; when
FT associated with E-526."
FT /evidence="ECO:0000269|PubMed:12223552"
FT MUTAGEN 526
FT /note="R->E: Loss of interaction with calmodulin; when
FT associated with E-525."
FT /evidence="ECO:0000269|PubMed:12223552"
FT CONFLICT 125
FT /note="A -> P (in Ref. 1; BAA37161)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="P -> Q (in Ref. 1; BAA37160/BAA37165 and 2;
FT AAM09696)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="H -> Q (in Ref. 2; AAM09696)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9Z351-12:831
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9Z351-13:813
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 759 AA; 84450 MW; C1D12DBFF3979D3F CRC64;
MVQKSRNGGV YPGTSGEKKL KVGFVGLDPG APDSTRDGAL LIAGSEAPKR GSVLSKPRTG
GAGAGKPPKR NAFYRKLQNF LYNVLERPRG WAFIYHAYVF LLVFSCLVLS VFSTIKEYEK
SSEGALYILE IVTIVVFGVE YFVRIWAAGC CCRYRGWRGR LKFARKPFCV IDIMVLIASI
AVLAAGSQGN VFATSALRSL RFLQILRMIR MDRRGGTWKL LGSVVYAHSK ELVTAWYIGF
LCLILASFLV YLAEKGENDH FDTYADALWW GLITLTTIGY GDKYPQTWNG RLLAATFTLI
GVSFFALPAG ILGSGFALKV QEQHRPKHFE KRRNPAAGLI QSAWRFYATN LSRTDLHSTW
QYYERTVTVP MYRLIPPLNQ LELLRNLKSK SGLTFRKEPQ PEPSPSQKVS LKDRVFSSPR
GMAAKGKGSP QAQTVRRSPS ADQSLDDSPS KVPKSWSFGD RSRTRQAFRI KGAASRQNSE
EASLPGEDIV EDNKSCNCEF VTEDLTPGLK VSIRAVCVMR FLVSKRKFKE SLRPYDVMDV
IEQYSAGHLD MLSRIKSLQS RIDMIVGPPP PSTPRDKKYP TKGPTAPSRE SPQYSPRVDH
IVGRGPTITD KDRTKGPAET ELPEDPSMMG RLGKVEKQVL SMEKKLDFLV SIYTQRMGIP
PAETEAYFGA KEPEPAPPYH SPEDSRDHAD KHGCIIKIVR STSSTGQRNY AAPPAIPPAQ
CPPSTSWQQS HQRHGTSPVG DHGSLVLRLE RSAGMMSCH
