KCNA3_HUMAN
ID KCNA3_HUMAN Reviewed; 575 AA.
AC P22001; Q5VWN2;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Potassium voltage-gated channel subfamily A member 3;
DE AltName: Full=HGK5;
DE AltName: Full=HLK3;
DE AltName: Full=HPCN3;
DE AltName: Full=Voltage-gated K(+) channel HuKIII;
DE AltName: Full=Voltage-gated potassium channel subunit Kv1.3;
GN Name=KCNA3; Synonyms=HGK5;
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 [MRNA].
RC TISSUE=Blood;
RX PubMed=7829094; DOI=10.1006/geno.1994.1500;
RA Folander K., Douglass J., Swanson R.;
RT "Confirmation of the assignment of the gene encoding Kv1.3, a voltage-gated
RT potassium channel (KCNA3) to the proximal short arm of human chromosome
RT 1.";
RL Genomics 23:295-296(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-575.
RC TISSUE=Skeletal muscle;
RX PubMed=1986382; DOI=10.1073/pnas.88.1.53;
RA Philipson L.H., Hice R.E., Schaefer K., Lamendola J., Bell G.I.,
RA Nelson D.J., Steiner D.F.;
RT "Sequence and functional expression in Xenopus oocytes of a human
RT insulinoma and islet potassium channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:53-57(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-575.
RX PubMed=1373731; DOI=10.1016/s0021-9258(18)42492-1;
RA Attali B., Romey G., Honore E., Schmid-Alliana A., Mattei M.-G., Lesage F.,
RA Ricard P., Barhanin J., Lazdunski M.;
RT "Cloning, functional expression, and regulation of two K+ channels in human
RT T lymphocytes.";
RL J. Biol. Chem. 267:8650-8657(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 47-575.
RC TISSUE=Lymphocyte;
RX PubMed=1547020; DOI=10.1089/dna.1992.11.163;
RA Cai Y.-C., Osborne P.B., North R.A., Dooley D.C., Douglass J.;
RT "Characterization and functional expression of genomic DNA encoding the
RT human lymphocyte type n potassium channel.";
RL DNA Cell Biol. 11:163-172(1992).
CC -!- FUNCTION: Mediates the voltage-dependent potassium ion permeability of
CC excitable membranes. Assuming opened or closed conformations in
CC response to the voltage difference across the membrane, the protein
CC forms a potassium-selective channel through which potassium ions may
CC pass in accordance with their electrochemical gradient.
CC -!- SUBUNIT: Heterotetramer of potassium channel proteins. Binds PDZ
CC domains of DLG1, DLG2 and DLG4 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P22001; Q07812: BAX; NbExp=2; IntAct=EBI-8627664, EBI-516580;
CC P22001; Q9UPQ8: DOLK; NbExp=6; IntAct=EBI-8627664, EBI-8645574;
CC P22001; Q09470: KCNA1; NbExp=3; IntAct=EBI-8627664, EBI-8286599;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein.
CC -!- DOMAIN: The N-terminus may be important in determining the rate of
CC inactivation of the channel while the tail may play a role in
CC modulation of channel activity and/or targeting of the channel to
CC specific subcellular compartments.
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.
CC -!- PTM: N-glycosylation promotes the cell surface expression.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC
CC 1.A.1.2) subfamily. Kv1.3/KCNA3 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-53 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36425.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA36425.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA59457.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA59457.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAB88073.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAC31761.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC31761.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L23499; AAC31761.1; ALT_SEQ; mRNA.
DR EMBL; AL365361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56457.1; -; Genomic_DNA.
DR EMBL; BC035059; AAH35059.2; -; mRNA.
DR EMBL; M55515; AAA36425.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M85217; AAA59457.1; ALT_SEQ; mRNA.
DR EMBL; M38217; AAB88073.1; ALT_INIT; Genomic_DNA.
DR CCDS; CCDS828.2; -.
DR PIR; A38101; A38101.
DR RefSeq; NP_002223.3; NM_002232.4.
DR PDB; 4BGC; X-ray; 1.20 A; A=104-204.
DR PDB; 7EJ1; EM; 3.20 A; B/D/F/H=1-575.
DR PDB; 7EJ2; EM; 3.30 A; B/D/F/H=1-575.
DR PDBsum; 4BGC; -.
DR PDBsum; 7EJ1; -.
DR PDBsum; 7EJ2; -.
DR AlphaFoldDB; P22001; -.
DR SMR; P22001; -.
DR BioGRID; 109941; 28.
DR DIP; DIP-44822N; -.
DR IntAct; P22001; 5.
DR MINT; P22001; -.
DR STRING; 9606.ENSP00000358784; -.
DR BindingDB; P22001; -.
DR ChEMBL; CHEMBL4633; -.
DR DrugBank; DB00845; Clofazimine.
DR DrugBank; DB06637; Dalfampridine.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB01110; Miconazole.
DR DrugBank; DB01069; Promethazine.
DR DrugCentral; P22001; -.
DR GuidetoPHARMACOLOGY; 540; -.
DR TCDB; 1.A.1.2.4; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; P22001; 1 site.
DR iPTMnet; P22001; -.
DR PhosphoSitePlus; P22001; -.
DR BioMuta; KCNA3; -.
DR DMDM; 215274135; -.
DR jPOST; P22001; -.
DR MassIVE; P22001; -.
DR MaxQB; P22001; -.
DR PaxDb; P22001; -.
DR PeptideAtlas; P22001; -.
DR PRIDE; P22001; -.
DR ProteomicsDB; 53950; -.
DR ABCD; P22001; 70 sequenced antibodies.
DR Antibodypedia; 33788; 380 antibodies from 37 providers.
DR DNASU; 3738; -.
DR Ensembl; ENST00000369769.4; ENSP00000358784.2; ENSG00000177272.9.
DR GeneID; 3738; -.
DR KEGG; hsa:3738; -.
DR MANE-Select; ENST00000369769.4; ENSP00000358784.2; NM_002232.5; NP_002223.3.
DR UCSC; uc001dzv.3; human.
DR CTD; 3738; -.
DR DisGeNET; 3738; -.
DR GeneCards; KCNA3; -.
DR HGNC; HGNC:6221; KCNA3.
DR HPA; ENSG00000177272; Tissue enriched (lymphoid).
DR MIM; 176263; gene.
DR neXtProt; NX_P22001; -.
DR OpenTargets; ENSG00000177272; -.
DR PharmGKB; PA30021; -.
DR VEuPathDB; HostDB:ENSG00000177272; -.
DR eggNOG; KOG1545; Eukaryota.
DR GeneTree; ENSGT00940000160210; -.
DR HOGENOM; CLU_011722_4_0_1; -.
DR InParanoid; P22001; -.
DR OMA; GMNSAFK; -.
DR OrthoDB; 695337at2759; -.
DR PhylomeDB; P22001; -.
DR TreeFam; TF313103; -.
DR PathwayCommons; P22001; -.
DR Reactome; R-HSA-1296072; Voltage gated Potassium channels.
DR SignaLink; P22001; -.
DR SIGNOR; P22001; -.
DR BioGRID-ORCS; 3738; 13 hits in 1061 CRISPR screens.
DR GeneWiki; KCNA3; -.
DR GenomeRNAi; 3738; -.
DR Pharos; P22001; Tclin.
DR PRO; PR:P22001; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P22001; protein.
DR Bgee; ENSG00000177272; Expressed in bone marrow cell and 91 other tissues.
DR Genevisible; P22001; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IEA:Ensembl.
DR GO; GO:0005244; F:voltage-gated ion channel activity; TAS:ProtInc.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003972; K_chnl_volt-dep_Kv1.
DR InterPro; IPR004050; K_chnl_volt-dep_Kv1.3.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01510; KV13CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01496; SHAKERCHANEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Glycoprotein; Ion channel; Ion transport;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..575
FT /note="Potassium voltage-gated channel subfamily A member
FT 3"
FT /id="PRO_0000053977"
FT TOPO_DOM 1..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..253
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..294
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..316
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..362
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..381
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..417
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..458
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..481
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..575
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 444..449
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOTIF 573..575
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 520
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT LIPID 317
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 72
FT /note="A -> G (in Ref. 5; AAA36425)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="L -> V (in Ref. 5; AAA36425)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="L -> V (in Ref. 6; AAA59457)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="L -> V (in Ref. 5; AAA36425)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="E -> K (in Ref. 1; AAC31761)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="T -> S (in Ref. 5; AAA36425)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="T -> S (in Ref. 5; AAA36425)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="S -> T (in Ref. 5; AAA36425)"
FT /evidence="ECO:0000305"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:4BGC"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:4BGC"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:4BGC"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:4BGC"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:4BGC"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:4BGC"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:4BGC"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:4BGC"
FT HELIX 153..164
FT /evidence="ECO:0007829|PDB:4BGC"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:4BGC"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:4BGC"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 231..254
FT /evidence="ECO:0007829|PDB:7EJ1"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 296..314
FT /evidence="ECO:0007829|PDB:7EJ1"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 337..346
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 360..368
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 369..380
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 382..392
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 395..420
FT /evidence="ECO:0007829|PDB:7EJ1"
FT TURN 431..434
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 435..442
FT /evidence="ECO:0007829|PDB:7EJ1"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 455..470
FT /evidence="ECO:0007829|PDB:7EJ1"
FT TURN 471..476
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 477..491
FT /evidence="ECO:0007829|PDB:7EJ1"
FT TURN 494..496
FT /evidence="ECO:0007829|PDB:7EJ1"
FT TURN 498..501
FT /evidence="ECO:0007829|PDB:7EJ1"
SQ SEQUENCE 575 AA; 63842 MW; 0E98905187A85F48 CRC64;
MDERLSLLRS PPPPSARHRA HPPQRPASSG GAHTLVNHGY AEPAAGRELP PDMTVVPGDH
LLEPEVADGG GAPPQGGCGG GGCDRYEPLP PSLPAAGEQD CCGERVVINI SGLRFETQLK
TLCQFPETLL GDPKRRMRYF DPLRNEYFFD RNRPSFDAIL YYYQSGGRIR RPVNVPIDIF
SEEIRFYQLG EEAMEKFRED EGFLREEERP LPRRDFQRQV WLLFEYPESS GPARGIAIVS
VLVILISIVI FCLETLPEFR DEKDYPASTS QDSFEAAGNS TSGSRAGASS FSDPFFVVET
LCIIWFSFEL LVRFFACPSK ATFSRNIMNL IDIVAIIPYF ITLGTELAER QGNGQQAMSL
AILRVIRLVR VFRIFKLSRH SKGLQILGQT LKASMRELGL LIFFLFIGVI LFSSAVYFAE
ADDPTSGFSS IPDAFWWAVV TMTTVGYGDM HPVTIGGKIV GSLCAIAGVL TIALPVPVIV
SNFNYFYHRE TEGEEQSQYM HVGSCQHLSS SAEELRKARS NSTLSKSEYM VIEEGGMNHS
AFPQTPFKTG NSTATCTTNN NPNSCVNIKK IFTDV
