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Potassium voltage-gated channel subfamily KQT member 5 (KQT-like 5) (Potassium channel subunit alpha KvLQT5) (Voltage-gated potassium channel subunit Kv7.5)

 KCNQ5_HUMAN             Reviewed;         932 AA.
Q9NR82; A6NKT6; A6PVT6; A8MSQ5; B4DS33; B5MC83; B7ZL37; F5GZV0;
Q17RE1; Q5VVP3; Q86W40; Q9NRN0; Q9NYA6;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 3.
27-SEP-2017, entry version 151.
RecName: Full=Potassium voltage-gated channel subfamily KQT member 5;
AltName: Full=KQT-like 5;
AltName: Full=Potassium channel subunit alpha KvLQT5;
AltName: Full=Voltage-gated potassium channel subunit Kv7.5;
Name=KCNQ5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, AND
SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=10787416; DOI=10.1074/jbc.M002378200;
Lerche C., Scherer C.R., Seebohm G., Derst C., Wei A.D., Busch A.E.,
Steinmeyer K.;
"Molecular cloning and functional expression of KCNQ5, a potassium
channel subunit that may contribute to neuronal M-current diversity.";
J. Biol. Chem. 275:22395-22400(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
TISSUE=Placenta;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-822 (ISOFORM 5).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 36-932 (ISOFORMS 1; 2 AND 3).
TISSUE=Brain;
PubMed=10816588; DOI=10.1074/jbc.M003245200;
Schroeder B.C., Hechenberger M., Weinreich F., Kubisch C.,
Jentsch T.J.;
"KCNQ5, a novel potassium channel broadly expressed in brain, mediates
M-type currents.";
J. Biol. Chem. 275:24089-24095(2000).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-932.
Kananura C., Biervert B., Hechenberger M., Engels H., Steinlein O.K.;
"The new voltage gated potassium channel KCNQ5 and early infantile
convulsions.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 72-932 (ISOFORM 1).
TISSUE=Brain, and Retina;
Kniazeva M., Han M.;
"A new gene of the voltage-gated potassium channel KCNQ family, KCNQ5,
is a candidate gene for retinal disorders.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND ACTIVATION BY RETICABINE.
PubMed=11159685; DOI=10.1038/sj.bjp.0703861;
Wickenden A.D., Zou A., Wagoner P.K., Jegla T.;
"Characterization of KCNQ5/Q3 potassium channels expressed in
mammalian cells.";
Br. J. Pharmacol. 132:381-384(2001).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[10]
INTERACTION WITH KCNQ1.
PubMed=24855057; DOI=10.1161/ATVBAHA.114.303801;
Oliveras A., Roura-Ferrer M., Sole L., de la Cruz A., Prieto A.,
Etxebarria A., Manils J., Morales-Cano D., Condom E., Soler C.,
Cogolludo A., Valenzuela C., Villarroel A., Comes N., Felipe A.;
"Functional assembly of Kv7.1/Kv7.5 channels with emerging properties
on vascular muscle physiology.";
Arterioscler. Thromb. Vasc. Biol. 34:1522-1530(2014).
[11]
VARIANTS [LARGE SCALE ANALYSIS] GLY-191 AND CYS-244.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Associates with KCNQ3 to form a potassium channel which
contributes to M-type current, a slowly activating and
deactivating potassium conductance which plays a critical role in
determining the subthreshold electrical excitability of neurons.
Therefore, it is important in the regulation of neuronal
excitability. May contribute, with other potassium channels, to
the molecular diversity of a heterogeneous population of M-
channels, varying in kinetic and pharmacological properties, which
underlie this physiologically important current. Insensitive to
tetraethylammonium, but inhibited by barium, linopirdine and
XE991. Activated by niflumic acid and the anticonvulsant
retigabine. As the native M-channel, the potassium channel
composed of KCNQ3 and KCNQ5 is also suppressed by activation of
the muscarinic acetylcholine receptor CHRM1.
{ECO:0000269|PubMed:10787416, ECO:0000269|PubMed:11159685}.
-!- SUBUNIT: Heteromultimer with KCNQ3 (PubMed:11159685,
PubMed:10787416). Heterotetramer with KCNQ1; has a voltage-gated
potassium channel activity (PubMed:24855057).
{ECO:0000269|PubMed:10787416, ECO:0000269|PubMed:11159685,
ECO:0000269|PubMed:24855057}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10787416,
ECO:0000269|PubMed:11159685}; Multi-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1;
IsoId=Q9NR82-1; Sequence=Displayed;
Name=2;
IsoId=Q9NR82-2; Sequence=VSP_001014;
Name=3;
IsoId=Q9NR82-3; Sequence=VSP_001015;
Name=4;
IsoId=Q9NR82-4; Sequence=VSP_022318, VSP_022319;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q9NR82-5; Sequence=VSP_045487;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q9NR82-6; Sequence=VSP_056731;
Note=No experimental confirmation available.;
Name=7;
IsoId=Q9NR82-7; Sequence=VSP_056730;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Strongly expressed in brain and skeletal
muscle. In brain, expressed in cerebral cortex, occipital pole,
frontal lobe and temporal lobe. Lower levels in hippocampus and
putamen. Low to undetectable levels in medulla, cerebellum and
thalamus.
-!- DOMAIN: The segment S4 is probably the voltage-sensor and is
characterized by a series of positively charged amino acids at
every third position. {ECO:0000250}.
-!- SIMILARITY: Belongs to the potassium channel family. KQT (TC
1.A.1.15) subfamily. Kv7.5/KCNQ5 sub-subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAG61495.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF249278; AAF91335.1; -; mRNA.
EMBL; AL445569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL049845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL360232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL360236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL365232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; FO393414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL513522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL671823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC050689; AAH50689.1; -; mRNA.
EMBL; BC117359; AAI17360.1; -; mRNA.
EMBL; BC143554; AAI43555.1; -; mRNA.
EMBL; AK299550; BAG61495.1; ALT_INIT; mRNA.
EMBL; AF202977; AAF69797.1; -; mRNA.
EMBL; AJ272506; CAC88112.1; -; Genomic_DNA.
EMBL; AJ272507; CAC88112.1; JOINED; Genomic_DNA.
EMBL; AJ272508; CAC88112.1; JOINED; Genomic_DNA.
EMBL; AJ272509; CAC88112.1; JOINED; Genomic_DNA.
EMBL; AJ272510; CAC88112.1; JOINED; Genomic_DNA.
EMBL; AJ272511; CAC88112.1; JOINED; Genomic_DNA.
EMBL; AJ272512; CAC88112.1; JOINED; Genomic_DNA.
EMBL; AJ272513; CAC88112.1; JOINED; Genomic_DNA.
EMBL; AJ272514; CAC88112.1; JOINED; Genomic_DNA.
EMBL; AJ272515; CAC88112.1; JOINED; Genomic_DNA.
EMBL; AJ272516; CAC88112.1; JOINED; Genomic_DNA.
EMBL; AJ272517; CAC88112.1; JOINED; Genomic_DNA.
EMBL; AJ272518; CAC88112.1; JOINED; Genomic_DNA.
EMBL; AJ272519; CAC88112.1; JOINED; Genomic_DNA.
EMBL; AF263835; AAF73446.1; -; mRNA.
CCDS; CCDS4976.1; -. [Q9NR82-1]
CCDS; CCDS55034.1; -. [Q9NR82-6]
CCDS; CCDS55035.1; -. [Q9NR82-5]
CCDS; CCDS55037.1; -. [Q9NR82-2]
RefSeq; NP_001153602.1; NM_001160130.1. [Q9NR82-2]
RefSeq; NP_001153604.1; NM_001160132.1. [Q9NR82-3]
RefSeq; NP_001153605.1; NM_001160133.1. [Q9NR82-6]
RefSeq; NP_001153606.1; NM_001160134.1. [Q9NR82-5]
RefSeq; NP_062816.2; NM_019842.3. [Q9NR82-1]
UniGene; Hs.445324; -.
ProteinModelPortal; Q9NR82; -.
SMR; Q9NR82; -.
BioGrid; 121149; 6.
CORUM; Q9NR82; -.
STRING; 9606.ENSP00000345055; -.
BindingDB; Q9NR82; -.
ChEMBL; CHEMBL2925; -.
DrugBank; DB04953; Ezogabine.
DrugBank; DB06089; ICA-105665.
GuidetoPHARMACOLOGY; 564; -.
iPTMnet; Q9NR82; -.
PhosphoSitePlus; Q9NR82; -.
BioMuta; KCNQ5; -.
DMDM; 122065285; -.
PaxDb; Q9NR82; -.
PeptideAtlas; Q9NR82; -.
PRIDE; Q9NR82; -.
Ensembl; ENST00000342056; ENSP00000345055; ENSG00000185760. [Q9NR82-6]
Ensembl; ENST00000370392; ENSP00000359419; ENSG00000185760. [Q9NR82-4]
Ensembl; ENST00000370398; ENSP00000359425; ENSG00000185760. [Q9NR82-1]
Ensembl; ENST00000628967; ENSP00000486187; ENSG00000185760. [Q9NR82-5]
Ensembl; ENST00000629977; ENSP00000485743; ENSG00000185760. [Q9NR82-2]
GeneID; 56479; -.
KEGG; hsa:56479; -.
UCSC; uc003pgj.5; human. [Q9NR82-1]
CTD; 56479; -.
DisGeNET; 56479; -.
EuPathDB; HostDB:ENSG00000185760.15; -.
GeneCards; KCNQ5; -.
HGNC; HGNC:6299; KCNQ5.
HPA; HPA016655; -.
MIM; 607357; gene.
neXtProt; NX_Q9NR82; -.
OpenTargets; ENSG00000185760; -.
PharmGKB; PA30077; -.
eggNOG; KOG1419; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00550000074513; -.
HOGENOM; HOG000220839; -.
HOVERGEN; HBG059014; -.
InParanoid; Q9NR82; -.
KO; K04930; -.
OMA; RMYTSRK; -.
PhylomeDB; Q9NR82; -.
TreeFam; TF315186; -.
Reactome; R-HSA-1296072; Voltage gated Potassium channels.
ChiTaRS; KCNQ5; human.
GeneWiki; KCNQ5; -.
GenomeRNAi; 56479; -.
PRO; PR:Q9NR82; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000185760; -.
CleanEx; HS_KCNQ5; -.
ExpressionAtlas; Q9NR82; baseline and differential.
Genevisible; Q9NR82; HS.
GO; GO:0030118; C:clathrin coat; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
InterPro; IPR028325; VG_K_chnl.
PANTHER; PTHR11537; PTHR11537; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF03520; KCNQ_channel; 1.
PRINTS; PR00169; KCHANNEL.
PRINTS; PR01459; KCNQCHANNEL.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Ion channel;
Ion transport; Membrane; Phosphoprotein; Polymorphism; Potassium;
Potassium channel; Potassium transport; Reference proteome;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 932 Potassium voltage-gated channel subfamily
KQT member 5.
/FTId=PRO_0000054040.
TOPO_DOM 1 125 Cytoplasmic. {ECO:0000255}.
TRANSMEM 126 146 Helical; Name=Segment S1. {ECO:0000255}.
TOPO_DOM 147 156 Extracellular. {ECO:0000255}.
TRANSMEM 157 177 Helical; Name=Segment S2. {ECO:0000255}.
TOPO_DOM 178 200 Cytoplasmic. {ECO:0000255}.
TRANSMEM 201 221 Helical; Name=Segment S3. {ECO:0000255}.
TOPO_DOM 222 229 Extracellular. {ECO:0000255}.
TRANSMEM 230 252 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000255}.
TOPO_DOM 253 266 Cytoplasmic. {ECO:0000255}.
TRANSMEM 267 287 Helical; Name=Segment S5. {ECO:0000255}.
TOPO_DOM 288 298 Extracellular. {ECO:0000255}.
INTRAMEM 299 319 Pore-forming; Name=Segment H5.
{ECO:0000255}.
TOPO_DOM 320 325 Extracellular. {ECO:0000255}.
TRANSMEM 326 346 Helical; Name=Segment S6. {ECO:0000255}.
TOPO_DOM 347 932 Cytoplasmic. {ECO:0000255}.
MOTIF 311 316 Selectivity filter. {ECO:0000250}.
MOD_RES 88 88 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JK45}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JK45}.
MOD_RES 831 831 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 407 416 KKEQGEASSS -> N (in isoform 2).
{ECO:0000303|PubMed:10816588,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_001014.
VAR_SEQ 407 416 KKEQGEASSS -> NKFCSNKQKLFRMYTSRKQS (in
isoform 3).
{ECO:0000303|PubMed:10816588}.
/FTId=VSP_001015.
VAR_SEQ 408 416 KEQGEASSS -> QNQQGESQSC (in isoform 7).
{ECO:0000305}.
/FTId=VSP_056730.
VAR_SEQ 416 525 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045487.
VAR_SEQ 416 427 SQKLSFKERVRM -> RFVISLLLHVCL (in isoform
4). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_022318.
VAR_SEQ 416 416 S -> SKFCSNKQKLFRMYTSRKQS (in isoform 6).
{ECO:0000305}.
/FTId=VSP_056731.
VAR_SEQ 428 932 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022319.
VARIANT 191 191 W -> G (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035772.
VARIANT 244 244 R -> C (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035773.
CONFLICT 92 93 KP -> SR (in Ref. 1; AAF91335).
{ECO:0000305}.
CONFLICT 109 109 R -> Q (in Ref. 4; BAG61495).
{ECO:0000305}.
CONFLICT 129 129 Y -> H (in Ref. 7; AAF73446).
{ECO:0000305}.
CONFLICT 727 727 A -> V (in Ref. 7; AAF73446).
{ECO:0000305}.
CONFLICT 799 799 T -> P (in Ref. 7; AAF73446).
{ECO:0000305}.
CONFLICT 857 857 S -> R (in Ref. 7; AAF73446).
{ECO:0000305}.
CONFLICT 909 909 R -> Q (in Ref. 7; AAF73446).
{ECO:0000305}.
SEQUENCE 932 AA; 102179 MW; CB41C243FD2B00FC CRC64;
MPRHHAGGEE GGAAGLWVKS GAAAAAAGGG RLGSGMKDVE SGRGRVLLNS AAARGDGLLL
LGTRAATLGG GGGGLRESRR GKQGARMSLL GKPLSYTSSQ SCRRNVKYRR VQNYLYNVLE
RPRGWAFIYH AFVFLLVFGC LILSVFSTIP EHTKLASSCL LILEFVMIVV FGLEFIIRIW
SAGCCCRYRG WQGRLRFARK PFCVIDTIVL IASIAVVSAK TQGNIFATSA LRSLRFLQIL
RMVRMDRRGG TWKLLGSVVY AHSKELITAW YIGFLVLIFS SFLVYLVEKD ANKEFSTYAD
ALWWGTITLT TIGYGDKTPL TWLGRLLSAG FALLGISFFA LPAGILGSGF ALKVQEQHRQ
KHFEKRRNPA ANLIQCVWRS YAADEKSVSI ATWKPHLKAL HTCSPTKKEQ GEASSSQKLS
FKERVRMASP RGQSIKSRQA SVGDRRSPST DITAEGSPTK VQKSWSFNDR TRFRPSLRLK
SSQPKPVIDA DTALGTDDVY DEKGCQCDVS VEDLTPPLKT VIRAIRIMKF HVAKRKFKET
LRPYDVKDVI EQYSAGHLDM LCRIKSLQTR VDQILGKGQI TSDKKSREKI TAEHETTDDL
SMLGRVVKVE KQVQSIESKL DCLLDIYQQV LRKGSASALA LASFQIPPFE CEQTSDYQSP
VDSKDLSGSA QNSGCLSRST SANISRGLQF ILTPNEFSAQ TFYALSPTMH SQATQVPISQ
SDGSAVAATN TIANQINTAP KPAAPTTLQI PPPLPAIKHL PRPETLHPNP AGLQESISDV
TTCLVASKEN VQVAQSNLTK DRSMRKSFDM GGETLLSVCP MVPKDLGKSL SVQNLIRSTE
ELNIQLSGSE SSGSRGSQDF YPKWRESKLF ITDEEVGPEE TETDTFDAAP QPAREAAFAS
DSLRTGRSRS SQSICKAGES TDALSLPHVK LK


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