KCMA1_BOVIN
ID KCMA1_BOVIN Reviewed; 1166 AA.
AC Q28204; Q95J89; Q95J90; Q95J91;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 166.
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 AltName: Full=bSlo;
GN Name=KCNMA1; Synonyms=KCNMA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE SPLICING,
RP PHOSPHORYLATION AT SER-1151 AND SER-1154, AND MUTAGENESIS OF SER-1151 AND
RP SER-1154.
RC TISSUE=Trachea smooth muscle;
RX PubMed=11514553; DOI=10.1074/jbc.m104202200;
RA Zhou X.-B., Arntz C., Kamm S., Motejlek K., Sausbier U., Wang G.-X.,
RA Ruth P., Korth M.;
RT "A molecular switch for specific stimulation of the BKCa channel by cGMP
RT and cAMP kinase.";
RL J. Biol. Chem. 276:43239-43245(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-1166 (ISOFORM 1).
RC TISSUE=Aortic smooth muscle;
RX PubMed=8973172; DOI=10.1021/bi961452k;
RA Moss G.W.J., Marshall J., Morabito M., Howe J.R., Moczydlowski E.;
RT "An evolutionarily conserved binding site for serine proteinase inhibitors
RT in large conductance calcium-activated potassium channels.";
RL Biochemistry 35:16024-16035(1996).
RN [3]
RP ACTIVITY REGULATION, PHOSPHORYLATION AT THR-139, AND MUTAGENESIS OF
RP THR-139.
RX PubMed=16341213; DOI=10.1038/nn1602;
RA Liu J., Asuncion-Chin M., Liu P., Dopico A.M.;
RT "CaM kinase II phosphorylation of slo Thr107 regulates activity and ethanol
RT responses of BK channels.";
RL Nat. Neurosci. 9:41-49(2006).
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 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. Kinetics of KCNMA1
CC channels are determined by alternative splicing, phosphorylation status
CC and its combination with modulating beta subunits. Highly sensitive to
CC both iberiotoxin (IbTx) and charybdotoxin (CTX) (By similarity).
CC {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Ethanol and carbon monoxide-bound heme increase
CC channel activation. Heme inhibits channel activation (By similarity).
CC Phosphorylation of Thr-139 leads to inhibition of channel activity by
CC ethanol. {ECO:0000250, ECO:0000269|PubMed:16341213}.
CC -!- SUBUNIT: Homotetramer; which constitutes the calcium-activated
CC potassium channel. Interacts with beta subunits KCNMB1, KCNMB2, KCNMB3
CC and KCNMB4. Interacts with gamma subunits LRRC26, LRRC38, LRRC52 and
CC LRRC55. Beta and gamma subunits are accessory, and modulate its
CC activity. Interacts with RAB11B (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=May be partially controlled by hormonal stress. Additional
CC isoforms seem to exist.;
CC Name=1; Synonyms=A, BKA;
CC IsoId=Q28204-1; Sequence=Displayed;
CC Name=2; Synonyms=B, BKB;
CC IsoId=Q28204-2; Sequence=VSP_009951;
CC Name=3; Synonyms=C, BKC;
CC IsoId=Q28204-3; Sequence=VSP_009950;
CC -!- DOMAIN: The S0 segment is essential for the modulation by the accessory
CC beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4. {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 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 sensors regions required for activation of the channel (By similarity).
CC {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 -!- PTM: Phosphorylated. Isoform 1 and isoform 2 are stimulated by PKG, but
CC not by PKA. In contrast, isoform 3 is exclusively stimulated by PKA. In
CC smooth muscles, phosphorylation affects its activity.
CC {ECO:0000269|PubMed:11514553}.
CC -!- PTM: Incremental phosphorylation of Thr-139 of the KCNMA1 tetramer
CC changes the response to ethanol from increased activation to inhibition
CC of channel activity. {ECO:0000269|PubMed:16341213,
CC ECO:0000269|PubMed:8973172}.
CC -!- PTM: Palmitoylation by ZDHHC22 and ZDHHC23 within the intracellular
CC linker between the S0 and S1 transmembrane domains regulates
CC localization to the plasma membrane. Depalmitoylated by LYPLA1 and
CC LYPLAL1, leading to retard exit from the trans-Golgi network (By
CC similarity). {ECO:0000250}.
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 also 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY033472; AAK54352.1; -; mRNA.
DR EMBL; AY033473; AAK54353.1; -; mRNA.
DR EMBL; AY033474; AAK54354.1; -; mRNA.
DR EMBL; U60105; AAB03663.1; -; mRNA.
DR PIR; B53145; B53145.
DR RefSeq; NP_777105.1; NM_174680.2. [Q28204-1]
DR AlphaFoldDB; Q28204; -.
DR BMRB; Q28204; -.
DR SMR; Q28204; -.
DR BioGRID; 159786; 1.
DR STRING; 9913.ENSBTAP00000047743; -.
DR ChEMBL; CHEMBL2111364; -.
DR iPTMnet; Q28204; -.
DR PaxDb; Q28204; -.
DR Ensembl; ENSBTAT00000054334; ENSBTAP00000047743; ENSBTAG00000013300. [Q28204-1]
DR GeneID; 282573; -.
DR KEGG; bta:282573; -.
DR CTD; 3778; -.
DR VEuPathDB; HostDB:ENSBTAG00000013300; -.
DR eggNOG; KOG1420; Eukaryota.
DR GeneTree; ENSGT00940000154935; -.
DR InParanoid; Q28204; -.
DR OrthoDB; 124461at2759; -.
DR TreeFam; TF314283; -.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000013300; Expressed in myometrium and 99 other tissues.
DR ExpressionAtlas; Q28204; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; ISA:AgBase.
DR GO; GO:0005901; C:caveola; ISA:AgBase.
DR GO; GO:0005737; C:cytoplasm; ISA:AgBase.
DR GO; GO:0005783; C:endoplasmic reticulum; ISA:AgBase.
DR GO; GO:0009897; C:external side of plasma membrane; ISA:AgBase.
DR GO; GO:0070062; C:extracellular exosome; ISA:AgBase.
DR GO; GO:0016021; C:integral component of membrane; ISA:AgBase.
DR GO; GO:0005886; C:plasma membrane; ISA:AgBase.
DR GO; GO:0045211; C:postsynaptic membrane; ISA:AgBase.
DR GO; GO:0043195; C:terminal bouton; ISA:AgBase.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISA:AgBase.
DR GO; GO:0003779; F:actin binding; ISA:AgBase.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; IDA:AgBase.
DR GO; GO:0060072; F:large conductance calcium-activated potassium channel activity; ISA:AgBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005267; F:potassium channel activity; ISA:AgBase.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISA:AgBase.
DR GO; GO:0007628; P:adult walking behavior; ISA:AgBase.
DR GO; GO:0048469; P:cell maturation; ISA:AgBase.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; ISA:AgBase.
DR GO; GO:0007268; P:chemical synaptic transmission; ISA:AgBase.
DR GO; GO:0007623; P:circadian rhythm; ISA:AgBase.
DR GO; GO:0060082; P:eye blink reflex; ISA:AgBase.
DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; ISA:AgBase.
DR GO; GO:0045475; P:locomotor rhythm; ISA:AgBase.
DR GO; GO:0060073; P:micturition; ISA:AgBase.
DR GO; GO:0045794; P:negative regulation of cell volume; ISA:AgBase.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISA:AgBase.
DR GO; GO:0019228; P:neuronal action potential; ISA:AgBase.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISA:AgBase.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISA:AgBase.
DR GO; GO:0006813; P:potassium ion transport; ISA:AgBase.
DR GO; GO:0051260; P:protein homooligomerization; ISA:AgBase.
DR GO; GO:0032344; P:regulation of aldosterone metabolic process; ISA:AgBase.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; ISA:AgBase.
DR GO; GO:0060087; P:relaxation of vascular associated smooth muscle; ISA:AgBase.
DR GO; GO:0051592; P:response to calcium ion; ISA:AgBase.
DR GO; GO:0034465; P:response to carbon monoxide; ISA:AgBase.
DR GO; GO:0001666; P:response to hypoxia; ISA:AgBase.
DR GO; GO:0006970; P:response to osmotic stress; ISA:AgBase.
DR GO; GO:0046541; P:saliva secretion; ISA:AgBase.
DR GO; GO:0007605; P:sensory perception of sound; ISA:AgBase.
DR GO; GO:0060083; P:smooth muscle contraction involved in micturition; ISA:AgBase.
DR GO; GO:0042311; P:vasodilation; ISA:AgBase.
DR InterPro; IPR024939; Ca-act_K_channel_Slo-1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003929; K_chnl_BK_asu.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10027:SF28; PTHR10027:SF28; 2.
DR Pfam; PF03493; BK_channel_a; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Ion channel; Ion transport;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Palmitate; Phosphoprotein;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..1166
FT /note="Calcium-activated potassium channel subunit alpha-1"
FT /id="PRO_0000054130"
FT TOPO_DOM 1..74
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical; Name=Segment S0"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..252
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..323
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 324..346
FT /note="Pore-forming; Name=P region"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..355
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..1166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 403..546
FT /note="RCK N-terminal"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..564
FT /note="Segment S7"
FT REGION 601..621
FT /note="Segment S8"
FT REGION 665..669
FT /note="Heme-binding motif"
FT REGION 689..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..787
FT /note="Segment S9"
FT REGION 962..982
FT /note="Segment S10"
FT REGION 1116..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 340..343
FT /note="Selectivity for potassium"
FT MOTIF 933..955
FT /note="Calcium bowl"
FT COMPBIAS 696..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 427
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 452
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 942
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 945
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 948
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 950
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 139
FT /note="Phosphothreonine; by CamK2"
FT /evidence="ECO:0000269|PubMed:16341213"
FT MOD_RES 693
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08460"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08460"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08460"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08460"
FT MOD_RES 900
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08460"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08460"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08460"
FT MOD_RES 1151
FT /note="Phosphoserine; by PKG"
FT /evidence="ECO:0000305|PubMed:11514553"
FT MOD_RES 1154
FT /note="Phosphoserine; by PKG"
FT /evidence="ECO:0000305|PubMed:11514553"
FT LIPID 106
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 107
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 109
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1141..1166
FT /note="STANRQNRPKSRESRDKQKYVQEERL -> PQT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11514553"
FT /id="VSP_009950"
FT VAR_SEQ 1160..1166
FT /note="YVQEERL -> KEMVYL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11514553"
FT /id="VSP_009951"
FT MUTAGEN 139
FT /note="T->V: Loss of phosphorylation by CaMK2 and,
FT therefore, inhibition of channel activity in response to
FT ethanol."
FT /evidence="ECO:0000269|PubMed:16341213"
FT MUTAGEN 1151
FT /note="S->A: Induces a stimulation by PKA instead of PKG;
FT when associated with A-1154."
FT /evidence="ECO:0000269|PubMed:8973172"
FT MUTAGEN 1154
FT /note="S->A: Induces a stimulation by PKA instead of PKG;
FT when associated with A-1151."
FT /evidence="ECO:0000269|PubMed:8973172"
FT CONFLICT 33..35
FT /note="SSS -> GST (in Ref. 2; AAB03663)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1166 AA; 130063 MW; 5E7DE4845D94743F CRC64;
MANGGGGGGG GGGGSSLRMS SNIHANHLSL DASSSSSSSS SSSSSSSSVH EPKMDALIIP
VTMEVPCDSR GQRMWWAFLA SSMVTFFGGL FIILLWRTLK YLWTVCCHCG GKTKEAQKIN
NGSSQADGTL KPVDEKEETV AAEVGWMTSV KDWAGVMISA QTLTGRVLVV LVFALSIGAL
VIYFIDSSNP IESCQNFYKD FTLQIDMAFN VFFLLYFGLR FIAANDKLWF WLEVNSVVDF
FTVPPVFVSV YLNRSWLGLR FLRALRLIQF SEILQFLNIL KTSNSIKLVN LLSIFISTWL
TAAGFIHLVE NSGDPWENFQ NNQALTYWEC VYLLMVTMST VGYGDVYAKT TLGRLFMVFF
ILGGLAMFAS YVPEIIELIG NRKKYGGSYS AVSGRKHIVV CGHITLESVS NFLKDFLHKD
RDDVNVEIVF LHNISPNLEL EALFKRHFTQ VEFYQGSVLN PHDLARVKIE SADACLILAN
KYCADPDAED ASNIMRVISI KNYHPKIRII TQMLQYHNKA HLLNIPSWNW KEGDDAICLA
ELKLGFIAQS CLAQGLSTML ANLFSMRSFI KIEEDTWQKY YLEGVSNEMY TEYLSSAFVG
LSFPTVCELC FVKLKLLMIA IEYKSANRES RILINPGNHL KIQEGTLGFF IASDAKEVKR
AFFYCKACHD DITDPKRIKK CGCKRLEDEQ PSTLSPKKKQ RNGGMRNSPS SSPKLMRHDP
LLIPGNDQID NMDSNVKKYD STGMFHWCAP KEIEKVILTR SEAAMTVLSG HVVVCIFGDV
SSALIGLRNL VMPLRASNFH YHELKHIVFV GSIEYLKREW ETLHNFPKVS ILPGTPLSRA
DLRAVNINLC DMCVILSANQ NNIDDTSLQD KECILASLNI KSMQFDDSIG VLQANSQGFT
PPGMDRSSPD NSPVHGMLRQ PSITTGVNIP IITELVNDTN VQFLDQDDDD DPDTELYLTQ
PFACGTAFAV SVLDSLMSAT YFNDNILTLI RTLVTGGATP ELEALIAEEN ALRGGYSTPQ
TLANRDRCRV AQLALLDGPF ADLGDGGCYG DLFCKALKTY NMLCFGIYRL RDAHLSTPSQ
CTKRYVITNP PYEFELVPTD LIFCLMQFDH NAGQSRASLS HSSHSSQSSS KKSSSVHSIP
STANRQNRPK SRESRDKQKY VQEERL
