ID   KCMA1_CHICK             Reviewed;        1137 AA.
AC   Q8AYS8; O12942; O13110; O93569; Q98951; Q9PS76;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Calcium-activated potassium channel subunit alpha-1;
DE   AltName: Full=BK channel;
DE   AltName: Full=BKCA alpha;
DE   AltName: Full=Calcium-activated potassium channel, subfamily M subunit alpha-1;
DE   AltName: Full=K(VCA)alpha;
DE   AltName: Full=KCa1.1;
DE   AltName: Full=Maxi K channel;
DE            Short=MaxiK;
DE   AltName: Full=Slo-alpha;
DE   AltName: Full=Slo1;
DE   AltName: Full=Slowpoke homolog;
DE            Short=Slo homolog;
DE            Short=cSlo;
GN   Name=KCNMA1; Synonyms=KCNMA;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE OF 398-1137
RP   (ISOFORM 4).
RC   STRAIN=Leghorn; TISSUE=Cochlear duct;
RX   PubMed=9178544; DOI=10.1098/rspb.1997.0104;
RA   Jiang G.J., Zidanic M., Michaels R.L., Michael T.H., Griguer C.,
RA   Fuchs P.A.;
RT   "CSlo encodes calcium-activated potassium channels in the chick's
RT   cochlea.";
RL   Proc. R. Soc. B 264:731-737(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9 AND 10).
RC   STRAIN=White leghorn; TISSUE=Brain;
RX   PubMed=9390519; DOI=10.1016/s0896-6273(00)80397-9;
RA   Rosenblatt K.P., Sun Z.-P., Heller S., Hudspeth A.J.;
RT   "Distribution of Ca2+-activated K+ channel isoforms along the tonotopic
RT   gradient of the chicken's cochlea.";
RL   Neuron 19:1061-1075(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=White leghorn; TISSUE=Lens epithelium;
RX   PubMed=9543635; DOI=10.1076/ceyr.17.3.264.5224;
RA   Rae J.L., Shepard A.R.;
RT   "Molecular biology and electrophysiology of calcium-activated potassium
RT   channels from lens epithelium.";
RL   Curr. Eye Res. 17:264-275(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 24-1137 (ISOFORM 3).
RX   PubMed=10362660; DOI=10.1152/ajpheart.1999.276.6.h1827;
RA   Kawakubo T., Naruse K., Matsubara T., Hotta N., Sokabe M.;
RT   "Characterization of a newly found stretch-activated KCa,ATP channel in
RT   cultured chick ventricular myocytes.";
RL   Am. J. Physiol. 276:H1827-H1838(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 710-973 (ISOFORM 5).
RX   PubMed=8755483; DOI=10.1016/s0896-6273(00)80285-8;
RA   Subramony P., Raucher S., Dryer L., Dryer S.E.;
RT   "Posttranslational regulation of Ca(2+)-activated K+ currents by a target-
RT   derived factor in developing parasympathetic neurons.";
RL   Neuron 17:115-124(1996).
RN   [6]
RP   FUNCTION.
RX   PubMed=9880252; DOI=10.1126/science.283.5399.215;
RA   Ramanathan K., Michael T.H., Jiang G.-J., Hiel H., Fuchs P.A.;
RT   "A molecular mechanism for electrical tuning of cochlear hair cells.";
RL   Science 283:215-217(1999).
CC   -!- FUNCTION: Potassium channel activated by both membrane depolarization
CC       or increase in cytosolic Ca(2+) that mediates export of K(+). It is
CC       also activated by the concentration of cytosolic Mg(2+). Its activation
CC       dampens the excitatory events that elevate the cytosolic Ca(2+)
CC       concentration and/or depolarize the cell membrane. It therefore
CC       contributes to repolarization of the membrane potential. Plays a key
CC       role in controlling excitability in a number of systems, such as
CC       regulation of the contraction of smooth muscle, the tuning of hair
CC       cells in the cochlea, regulation of transmitter release, and innate
CC       immunity. In smooth muscles, its activation by high level of Ca(2+),
CC       caused by ryanodine receptors in the sarcoplasmic reticulum, regulates
CC       the membrane potential. In cochlea cells, its number and kinetic
CC       properties partly determine the characteristic frequency of each hair
CC       cell and thereby helps to establish a tonotopic map. Highly sensitive
CC       to both iberiotoxin (IbTx) and charybdotoxin (CTX).
CC       {ECO:0000269|PubMed:9880252}.
CC   -!- ACTIVITY REGULATION: Ethanol and carbon monoxide-bound heme increase
CC       channel activation. Heme inhibits channel activation (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer; which constitutes the calcium-activated
CC       potassium channel. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8AYS8; O57513: akt1; NbExp=2; IntAct=EBI-1635766, EBI-4306384;
CC       Q8AYS8; P17153: ANXA5; NbExp=3; IntAct=EBI-1635766, EBI-1635947;
CC       Q8AYS8; P08251: ATP1B1; NbExp=3; IntAct=EBI-1635766, EBI-7206371;
CC       Q8AYS8; Q01406: CTTN1; NbExp=2; IntAct=EBI-1635766, EBI-2530463;
CC       Q8AYS8; F1NPL8: GSK3A; NbExp=2; IntAct=EBI-1635766, EBI-4306413;
CC       Q8AYS8; P42324: HPCAL1; NbExp=3; IntAct=EBI-1635766, EBI-1636399;
CC       Q8AYS8; Q90593: HSPA5; NbExp=3; IntAct=EBI-1635766, EBI-1635886;
CC       Q8AYS8; Q5ZL72: HSPD1; NbExp=3; IntAct=EBI-1635766, EBI-1635874;
CC       Q8AYS8; Q5F425: LIN7C; NbExp=3; IntAct=EBI-1635766, EBI-1636456;
CC       Q8AYS8; F1NLP2: PDK1; NbExp=2; IntAct=EBI-1635766, EBI-4306427;
CC       Q8AYS8; P84173: PHB1; NbExp=3; IntAct=EBI-1635766, EBI-1636878;
CC       Q8AYS8; F1NSA8: RAP1A; NbExp=2; IntAct=EBI-1635766, EBI-4306330;
CC       Q8AYS8; P60878: SNAP25; NbExp=3; IntAct=EBI-1635766, EBI-1637031;
CC       Q8AYS8; P80566: SOD1; NbExp=3; IntAct=EBI-1635766, EBI-1637015;
CC       Q8AYS8; P31395: STMN1; NbExp=3; IntAct=EBI-1635766, EBI-1636998;
CC       Q8AYS8; Q5ZMU9: vcp; NbExp=3; IntAct=EBI-1635766, EBI-1637127;
CC       Q8AYS8; Q5F3W6: YWHAG; NbExp=3; IntAct=EBI-1635766, EBI-1635853;
CC       Q8AYS8; P08106; NbExp=3; IntAct=EBI-1635766, EBI-1636307;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=10;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1;
CC         IsoId=Q8AYS8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8AYS8-2; Sequence=VSP_009985;
CC       Name=3;
CC         IsoId=Q8AYS8-3; Sequence=VSP_009987;
CC       Name=4;
CC         IsoId=Q8AYS8-4; Sequence=VSP_009991;
CC       Name=5; Synonyms=IK;
CC         IsoId=Q8AYS8-5; Sequence=VSP_009990;
CC       Name=6;
CC         IsoId=Q8AYS8-6; Sequence=VSP_009988;
CC       Name=7;
CC         IsoId=Q8AYS8-7; Sequence=VSP_009983;
CC       Name=8;
CC         IsoId=Q8AYS8-8; Sequence=VSP_009984;
CC       Name=9;
CC         IsoId=Q8AYS8-9; Sequence=VSP_009986;
CC       Name=10;
CC         IsoId=Q8AYS8-10; Sequence=VSP_009989;
CC   -!- DOMAIN: The S0 segment is essential for the modulation by the accessory
CC       beta subunits. {ECO:0000250}.
CC   -!- DOMAIN: The S4 segment, which is characterized by a series of
CC       positively charged amino acids at every third position, is part of the
CC       voltage-sensor. {ECO:0000250}.
CC   -!- DOMAIN: The pore-forming domain (also referred as P region) is imbedded
CC       into the membrane, and forms the selectivity filter of the pore. It
CC       contains the signature sequence of potassium channels that displays
CC       selectivity to potassium (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The RCK N-terminal domain mediates the homotetramerization,
CC       thereby promoting the assembly of monomers into functional potassium
CC       channel. It includes binding sites for Ca(2+) and Mg(2+) (By
CC       similarity). {ECO:0000250}.
CC   -!- DOMAIN: The heme-binding motif mediates inhibition of channel
CC       activation by heme. Carbon monoxide-bound heme leads to increased
CC       channel activation (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The calcium bowl constitutes one of the Ca(2+) sensors and
CC       probably acts as a Ca(2+)-binding site. There are however other Ca(2+)
CC       sensor regions required for activation of the channel.
CC       {ECO:0000250|UniProtKB:B7ZC96}.
CC   -!- MISCELLANEOUS: The protein was initially thought to contain two
CC       functionally distinct parts: The core channel (from the N-terminus to
CC       the S9 segment) that mediates the channel activity, and the cytoplasmic
CC       tail (from the S9 segment to the C-terminus) that mediates the calcium
CC       sensing. The situation is however more complex, since the core channel
CC       contains binding sites for Ca(2+) and Mg(2+).
CC   -!- SIMILARITY: Belongs to the potassium channel family. Calcium-activated
CC       (TC 1.A.1.3) subfamily. KCa1.1/KCNMA1 sub-subfamily. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 is the initiator or if the
CC       sequence starts further upstream. {ECO:0000305}.
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DR   EMBL; U23821; AAC60378.1; -; mRNA.
DR   EMBL; U23823; AAC60125.1; -; mRNA.
DR   EMBL; U73189; AAB17873.1; -; mRNA.
DR   EMBL; AF087663; AAC35370.1; -; mRNA.
DR   EMBL; AB072618; BAC20639.1; -; mRNA.
DR   RefSeq; NP_989555.1; NM_204224.1.
DR   AlphaFoldDB; Q8AYS8; -.
DR   SMR; Q8AYS8; -.
DR   BioGRID; 675104; 111.
DR   IntAct; Q8AYS8; 106.
DR   MINT; Q8AYS8; -.
DR   STRING; 9031.ENSGALP00000063286; -.
DR   iPTMnet; Q8AYS8; -.
DR   PaxDb; 9031-ENSGALP00000039705; -.
DR   GeneID; 374065; -.
DR   KEGG; gga:374065; -.
DR   CTD; 3778; -.
DR   VEuPathDB; HostDB:geneid_374065; -.
DR   eggNOG; KOG1420; Eukaryota.
DR   InParanoid; Q8AYS8; -.
DR   Reactome; R-GGA-1296052; Ca2+ activated K+ channels.
DR   PRO; PR:Q8AYS8; -.
DR   Proteomes; UP000000539; Chromosome 6.
DR   Bgee; ENSGALG00000004980; Expressed in colon and 9 other cell types or tissues.
DR   ExpressionAtlas; Q8AYS8; baseline and differential.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR   GO; GO:0060072; F:large conductance calcium-activated potassium channel activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003929; K_chnl_BK_asu.
DR   InterPro; IPR047871; K_chnl_Slo-like.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR048735; Slowpoke-like_C.
DR   PANTHER; PTHR10027; CALCIUM-ACTIVATED POTASSIUM CHANNEL ALPHA CHAIN; 1.
DR   PANTHER; PTHR10027:SF33; CALCIUM-ACTIVATED POTASSIUM CHANNEL SUBUNIT ALPHA-1; 1.
DR   Pfam; PF03493; BK_channel_a; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF21014; Slowpoke_C; 1.
DR   PRINTS; PR01449; BKCHANNELA.
DR   PRINTS; PR00169; KCHANNEL.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Ion channel; Ion transport; Magnesium;
KW   Membrane; Metal-binding; Potassium; Potassium channel; Potassium transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN           1..1137
FT                   /note="Calcium-activated potassium channel subunit alpha-1"
FT                   /id="PRO_0000054138"
FT   TOPO_DOM        1..44
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical; Name=Segment S0"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        66..137
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..173
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        195..198
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..223
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        224..244
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        245..259
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        281..294
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        295..317
FT                   /note="Pore-forming; Name=P region"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        318..326
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..347
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        348..1137
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          374..517
FT                   /note="RCK N-terminal"
FT   REGION          515..535
FT                   /note="Segment S7"
FT   REGION          572..592
FT                   /note="Segment S8"
FT   REGION          636..640
FT                   /note="Heme-binding motif"
FT   REGION          660..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..758
FT                   /note="Segment S9"
FT   REGION          933..953
FT                   /note="Segment S10"
FT   REGION          1088..1137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           311..314
FT                   /note="Selectivity for potassium"
FT   MOTIF           904..926
FT                   /note="Calcium bowl"
FT   COMPBIAS        667..685
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1088..1118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1119..1137
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         398
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000305"
FT   BINDING         421
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000305"
FT   BINDING         423
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000305"
FT   BINDING         913
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:B7ZC96"
FT   BINDING         916
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:B7ZC96"
FT   BINDING         919
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:B7ZC96"
FT   BINDING         921
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:B7ZC96"
FT   VAR_SEQ         1..17
FT                   /note="MSNNINANNLNTDSSSS -> MKPFEVSLPPPPPS (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:9390519"
FT                   /id="VSP_009983"
FT   VAR_SEQ         160
FT                   /note="N -> KSRTADSLI (in isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:9390519"
FT                   /id="VSP_009984"
FT   VAR_SEQ         602
FT                   /note="S -> RSRKR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9390519"
FT                   /id="VSP_009985"
FT   VAR_SEQ         602
FT                   /note="S -> RSRKRYALFVTFPSNLNPTST (in isoform 9)"
FT                   /evidence="ECO:0000303|PubMed:9390519"
FT                   /id="VSP_009986"
FT   VAR_SEQ         657
FT                   /note="L -> PKMSIYKRMKLACCFDCGRSERDCSCMSGSVHSNMDTLERAFPLSSV
FT                   SVNDCSTSLRAF (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10362660,
FT                   ECO:0000303|PubMed:9390519"
FT                   /id="VSP_009987"
FT   VAR_SEQ         657
FT                   /note="L -> IYF (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:9390519"
FT                   /id="VSP_009988"
FT   VAR_SEQ         687
FT                   /note="M -> MRFSCPFLP (in isoform 10)"
FT                   /evidence="ECO:0000303|PubMed:9390519"
FT                   /id="VSP_009989"
FT   VAR_SEQ         906
FT                   /note="L -> LAKPGKLLPLVSISQEKNSGTQILMITEL (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:8755483,
FT                   ECO:0000303|PubMed:9390519"
FT                   /id="VSP_009990"
FT   VAR_SEQ         1130..1137
FT                   /note="KYVQEDRL -> NSTRMNRMGQEKKWFTDEPDNAYPRNIQIKPMSTHMANQI
FT                   NQYKSTSSLIPPIREVEDEC (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:9390519"
FT                   /id="VSP_009991"
FT   CONFLICT        96
FT                   /note="Q -> R (in Ref. 1; AAC60378)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        397
FT                   /note="V -> I (in Ref. 1; AAC60378)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        409
FT                   /note="L -> P (in Ref. 4; AAC35370)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        522
FT                   /note="C -> S (in Ref. 1; AAC60378)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        712
FT                   /note="S -> W (in Ref. 5; BAC20639)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        937
FT                   /note="T -> P (in Ref. 5; BAC20639)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        941
FT                   /note="V -> D (in Ref. 5; BAC20639)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1034
FT                   /note="L -> F (in Ref. 4; AAC35370)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1137 AA;  127647 MW;  40A9735E586F0BD1 CRC64;
     MSNNINANNL NTDSSSSPVN VPKMDALIIP VTMEVPCDSR GQRMWWAFLA SSMVTFFGGL
     FIILLWRTLK YLWTVCCHCG VKNKEAQKIN GGGDTQADGA CKPTDEKEEN VAAEVGWMTS
     VKDWAGVMIS AQTLTGRVLV VLVFALSIGA LVIYFIDSSN PIESCQNFYK DFTLQIDMAF
     NVFFLLYFGL RFIAANDKLW FWLEVNSVVD FFTVPPVFVS VYLNRSWLGL RFLRALRLIQ
     FSEILQFLNI LKTSNSIKLV NLCSIFISTW LTAAGFIHLV ENSGDPWENF QNNQQLTYWE
     CVYLLMVTMS TVGYGDVYAK TTLGRLFMVF FILGGLAMFA SYVPEIIELI GNRKKYGGSY
     SAVSGRKHIV VCGHITLESV SNFLKDFLHK DRDDVNVEIV FLHNISPNLE LEALFKRHFT
     QVEFYQGSVL NPHDLARVKI ESADACLILA NKYCADPDAE DASNIMRVIS IKNYHPKIRI
     ITQMLQYHNK AHLLNIPSWN WKEGDDAICL AELKLGFIAQ SCLAPGLSTM LANLFSMRSF
     IKIEEDTWQK YYLEGVANEM YTEYLSSAFV GLSFPAVCEL VFAKLKLLMI AIEYKSEKRE
     SSILINPGNH VKIQEGTLGF FIASDAKEVK RAFFYCKACH DDITDPKRIK KCGCKRLEDE
     QPSTLSPKKK QRNGGMRNSP NSSPKLMRHD PLLIPGNEQI DNMDANVKKY DSTGMFHWCP
     AKDIEKVILT RSEAAMTVLS GHVVVCIFGD VKSALIGLRN LVMPLRASNF HYHELKHIVF
     VGSLEYLRRE WETLHNFPKV SILPGTPLSR ADLRAVNINL CDMCVILSAN QNNIDDASLQ
     DKECILASLN IKSMQFDDSI GVLQANSQGF TPPGMDRSSP DNSPVHGLLR QPSITTGANI
     PIITELVNDS NVQFLDQDDD DDPDTELYLT QPFACGTAFA VSVLDSLMSA TYFNDNILTL
     IRTLVTGGAT PELEALIAEE NALRGGYSTP QTLANRDRCR VAQLALYDGP FADLGDGGCY
     GDLFCKALKT YNMLCFGIYR LRDAHLSTPS QCTKRYVITN PPYEFELVPT DLIFCLMQFD
     HNAGQSRASL SHSSHSSYSS SKKSSSVHSI PSTANRPNRT KTRDSREKQK YVQEDRL
//