KCNK2_RAT
ID KCNK2_RAT Reviewed; 426 AA.
AC Q920B6; A3QR52; Q3MMY3; Q5DNW4; Q5DNW5;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Potassium channel subfamily K member 2 {ECO:0000250|UniProtKB:O95069};
DE AltName: Full=Outward rectifying potassium channel protein TREK-1 {ECO:0000250|UniProtKB:O95069};
DE AltName: Full=Stretch-activated potassium channel TREK-1 {ECO:0000303|PubMed:16248991};
DE AltName: Full=TREK-1 K(+) channel subunit {ECO:0000250|UniProtKB:O95069};
DE AltName: Full=Two pore domain potassium channel TREK-1 {ECO:0000303|PubMed:24196565};
DE AltName: Full=Two pore potassium channel TPKC1 {ECO:0000250|UniProtKB:O95069};
GN Name=Kcnk2 {ECO:0000312|EMBL:AAU06141.1,
GN ECO:0000312|Ensembl:ENSRNOP00000003684, ECO:0000312|RGD:621448};
GN Synonyms=Trek {ECO:0000312|EMBL:ABD64605.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL01159.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Brain {ECO:0000312|EMBL:AAL01159.1};
RX PubMed=11319556; DOI=10.1038/87434;
RA Bockenhauer D., Zilberberg N., Goldstein S.A.;
RT "KCNK2: reversible conversion of a hippocampal potassium leak into a
RT voltage-dependent channel.";
RL Nat. Neurosci. 4:486-491(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAL95708.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=Wistar {ECO:0000312|EMBL:AAL95708.1};
RX PubMed=11897838; DOI=10.1113/jphysiol.2001.013432;
RA Gu W., Schlichthorl G., Hirsch J.R., Engels H., Karschin C., Karschin A.,
RA Derst C., Steinlein O.K., Daut J.;
RT "Expression pattern and functional characteristics of two novel splice
RT variants of the two-pore-domain potassium channel TREK-2.";
RL J. Physiol. (Lond.) 539:657-668(2002).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAU25945.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND ACTIVATION.
RX PubMed=16248991; DOI=10.1016/j.cardiores.2005.08.018;
RA Tao Li X., Dyachenko V., Zuzarte M., Putzke C., Preisig-Muller R.,
RA Isenberg G., Daut J.;
RT "The stretch-activated potassium channel TREK-1 in rat cardiac ventricular
RT muscle.";
RL Cardiovasc. Res. 69:86-97(2006).
RN [4] {ECO:0000305, ECO:0000312|EMBL:ABD64605.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=24196565; DOI=10.1007/s00424-013-1384-z;
RA Rinne S., Renigunta V., Schlichthorl G., Zuzarte M., Bittner S.,
RA Meuth S.G., Decher N., Daut J., Preisig-Muller R.;
RT "A splice variant of the two-pore domain potassium channel TREK-1 with only
RT one pore domain reduces the surface expression of full-length TREK-1
RT channels.";
RL Pflugers Arch. 466:1559-1570(2014).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAU06141.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Wistar {ECO:0000312|EMBL:AAU06141.1};
RA Li Z.B., Wang X.L.;
RT "Possible role of TREK-1 in temperature regulation.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000312|Ensembl:ENSRNOP00000003684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Ensembl:ENSRNOP00000003684};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [7] {ECO:0000305, ECO:0000312|EMBL:AAU06141.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ion channel that contributes to passive transmembrane
CC potassium transport. Reversibly converts between a voltage-insensitive
CC potassium leak channel and a voltage-dependent outward rectifying
CC potassium channel in a phosphorylation-dependent manner
CC (PubMed:11319556). In astrocytes, forms mostly heterodimeric potassium
CC channels with KCNK1, with only a minor proportion of functional
CC channels containing homodimeric KCNK2. In astrocytes, the heterodimer
CC formed by KCNK1 and KCNK2 is required for rapid glutamate release in
CC response to activation of G-protein coupled receptors, such as F2R and
CC CNR1 (By similarity). {ECO:0000250|UniProtKB:P97438,
CC ECO:0000269|PubMed:11319556}.
CC -!- FUNCTION: [Isoform 5]: Does not display channel activity but reduces
CC the channel activity of isoform 1, isoform 2 and isoform 4 and reduces
CC cell surface expression of isoform 2. {ECO:0000269|PubMed:24196565}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Heterodimer with
CC KCNK1; disulfide-linked (By similarity). Interacts with BVES; the
CC interaction enhances KCNK2 surface expression and is inhibited by cAMP
CC (By similarity). {ECO:0000250|UniProtKB:O95069,
CC ECO:0000250|UniProtKB:P97438}.
CC -!- INTERACTION:
CC Q920B6; P50150: GNG4; Xeno; NbExp=3; IntAct=EBI-6530063, EBI-6395970;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:24196565}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:24196565}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000269|PubMed:24196565}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:24196565}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24196565}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:24196565}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1 {ECO:0000269|PubMed:11319556, ECO:0000269|PubMed:11897838};
CC Synonyms=TREK-1b {ECO:0000303|PubMed:24196565};
CC IsoId=Q920B6-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16248991}; Synonyms=TREK-1a
CC {ECO:0000303|PubMed:24196565};
CC IsoId=Q920B6-2; Sequence=VSP_053954;
CC Name=3 {ECO:0000269|PubMed:24196565}; Synonyms=TREK-1c
CC {ECO:0000303|PubMed:24196565};
CC IsoId=Q920B6-3; Sequence=VSP_053952;
CC Name=4 {ECO:0000269|PubMed:24196565}; Synonyms=TREK-1d
CC {ECO:0000303|PubMed:24196565};
CC IsoId=Q920B6-4; Sequence=VSP_053953;
CC Name=5 {ECO:0000269|PubMed:24196565}; Synonyms=TREK-1e
CC {ECO:0000303|PubMed:24196565};
CC IsoId=Q920B6-5; Sequence=VSP_053954, VSP_053955, VSP_053956;
CC -!- TISSUE SPECIFICITY: Expressed in cardiomyocytes (at protein level).
CC Expressed in various brain regions including the lateral olfactory
CC tract, piriform cortex of the forebrain, paraventricular and
CC anteromedial thalamic nuclei, brainstem, caudate putamen, nucleus
CC accumbens, neocortex and interpeduncular nucleus. Isoform 5 is
CC expressed in brain and kidney. {ECO:0000269|PubMed:11897838,
CC ECO:0000269|PubMed:16248991, ECO:0000269|PubMed:24196565}.
CC -!- DOMAIN: The C-terminal region of isoform 5 mediates its intracellular
CC retention. {ECO:0000269|PubMed:24196565}.
CC -!- PTM: Phosphorylation at Ser-348 controls the reversible conversion from
CC a leak channel to a voltage-dependent channel.
CC {ECO:0000250|UniProtKB:O95069}.
CC -!- MISCELLANEOUS: Activated by arachadonic acid, mechanical stretching and
CC intracellular acidification. {ECO:0000269|PubMed:16248991}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000255}.
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DR EMBL; AF325671; AAL01159.1; -; mRNA.
DR EMBL; AF385402; AAL95708.1; -; mRNA.
DR EMBL; AY727922; AAU25945.1; -; mRNA.
DR EMBL; AY555072; AAT64134.1; -; mRNA.
DR EMBL; AY555073; AAT64135.1; -; mRNA.
DR EMBL; DQ403851; ABD64605.1; -; mRNA.
DR EMBL; AY695826; AAU06141.1; -; mRNA.
DR EMBL; AABR06076806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06076807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06076808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06076809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473985; EDL94961.1; -; Genomic_DNA.
DR EMBL; CH473985; EDL94962.1; -; Genomic_DNA.
DR RefSeq; NP_742038.2; NM_172041.2.
DR RefSeq; NP_742039.1; NM_172042.1. [Q920B6-1]
DR RefSeq; XP_006250495.1; XM_006250433.3. [Q920B6-4]
DR RefSeq; XP_006250496.1; XM_006250434.3. [Q920B6-2]
DR AlphaFoldDB; Q920B6; -.
DR SMR; Q920B6; -.
DR IntAct; Q920B6; 9.
DR STRING; 10116.ENSRNOP00000003684; -.
DR BindingDB; Q920B6; -.
DR ChEMBL; CHEMBL3817718; -.
DR GlyGen; Q920B6; 2 sites.
DR PaxDb; Q920B6; -.
DR Ensembl; ENSRNOT00000003684; ENSRNOP00000003684; ENSRNOG00000002653. [Q920B6-1]
DR Ensembl; ENSRNOT00000077282; ENSRNOP00000068842; ENSRNOG00000002653. [Q920B6-3]
DR Ensembl; ENSRNOT00000103519; ENSRNOP00000077148; ENSRNOG00000002653. [Q920B6-4]
DR Ensembl; ENSRNOT00000107139; ENSRNOP00000087071; ENSRNOG00000002653. [Q920B6-2]
DR GeneID; 170899; -.
DR KEGG; rno:170899; -.
DR UCSC; RGD:621448; rat. [Q920B6-1]
DR CTD; 3776; -.
DR RGD; 621448; Kcnk2.
DR eggNOG; KOG1418; Eukaryota.
DR GeneTree; ENSGT00940000156560; -.
DR HOGENOM; CLU_022504_10_0_1; -.
DR InParanoid; Q920B6; -.
DR OMA; TSQISHW; -.
DR OrthoDB; 616474at2759; -.
DR PhylomeDB; Q920B6; -.
DR TreeFam; TF313947; -.
DR Reactome; R-RNO-1299503; TWIK related potassium channel (TREK).
DR Reactome; R-RNO-5576886; Phase 4 - resting membrane potential.
DR PRO; PR:Q920B6; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Proteomes; UP000234681; Chromosome 13.
DR Bgee; ENSRNOG00000002653; Expressed in frontal cortex and 15 other tissues.
DR Genevisible; Q920B6; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0097449; C:astrocyte projection; IDA:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0044305; C:calyx of Held; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:RGD.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:0019870; F:potassium channel inhibitor activity; IDA:UniProtKB.
DR GO; GO:0022841; F:potassium ion leak channel activity; IDA:UniProtKB.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:RGD.
DR GO; GO:0003231; P:cardiac ventricle development; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0090102; P:cochlea development; IEP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0007613; P:memory; IEP:RGD.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IMP:RGD.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IMP:RGD.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:RGD.
DR GO; GO:1900039; P:positive regulation of cellular response to hypoxia; IMP:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR003976; 2pore_dom_K_chnl_TREK.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003; PTHR11003; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01499; TREKCHANNEL.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..426
FT /note="Potassium channel subfamily K member 2"
FT /id="PRO_0000426718"
FT TOPO_DOM 1..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 144..170
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 253..283
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 354..426
FT /note="Required for basal channel activity"
FT /evidence="ECO:0000250|UniProtKB:P97438"
FT REGION 378..426
FT /note="Essential for chloroform and halothane sensitivity"
FT /evidence="ECO:0000250|UniProtKB:P97438"
FT MOD_RES 348
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:O95069"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P97438"
FT VAR_SEQ 1..16
FT /note="MLASASRERPGYTAGV -> MMNPRAKRSVYL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:24196565"
FT /id="VSP_053952"
FT VAR_SEQ 1..15
FT /note="MLASASRERPGYTAG -> MGA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:24196565"
FT /id="VSP_053953"
FT VAR_SEQ 2..16
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16248991,
FT ECO:0000303|PubMed:24196565"
FT /id="VSP_053954"
FT VAR_SEQ 213..241
FT /note="KWNVSQTKIRIISTIIFILFGCVLFVALP -> VGRTLNIWTSTSSSCGSGS
FT SLGWPTLRLF (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:24196565"
FT /id="VSP_053955"
FT VAR_SEQ 242..426
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:24196565"
FT /id="VSP_053956"
FT CONFLICT 416
FT /note="A -> R (in Ref. 4; ABD64605)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 46912 MW; CACDA05BBE95FDBC CRC64;
MLASASRERP GYTAGVAAPD LLDPKSAAQN SKPRLSFSAK PTVLASRVES DSAINVMKWK
TVSTIFLVVV LYLIIGATVF KALEQPQEIS QRTTIVIQKQ NFIAQHACVN STELDELIQQ
IVTAINAGII PLGNNSNQVS HWDLGSSFFF AGTVITTIGF GNISPRTEGG KIFCIIYALL
GIPLFGFLLA GVGDQLGTIF GKGIAKVEDT FIKWNVSQTK IRIISTIIFI LFGCVLFVAL
PAVIFKHIEG WSALDAIYFV VITLTTIGFG DYVAGGSDIE YLDFYKPVVW FWILVGLAYF
AAVLSMIGDW LRVISKKTKE EVGEFRAHAA EWTANVTAEF KETRRRLSVE IYDKFQRATS
VKRKLSAELA GNHNQELTPC RRTLSVNHLT SEREVLPPLL KAESIYLNGL TPHCAAEDIA
VIENMK
