KCMA1_RAT
ID KCMA1_RAT Reviewed; 1209 AA.
AC Q62976; O08626; O55180; O88659; Q7TMZ7; Q7TMZ8; Q7TQ55; Q7TQ56; Q7TQ57;
AC Q9WUI3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 181.
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;
GN Name=Kcnma1; Synonyms=Kcnma;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Sprague-Dawley; TISSUE=Aortic smooth muscle;
RX PubMed=9403560; DOI=10.1161/01.hyp.30.6.1403;
RA Liu Y., Pleyte K., Knaus H.-G., Rusch N.J.;
RT "Increased expression of Ca2+-sensitive K+ channels in aorta of
RT hypertensive rats.";
RL Hypertension 30:1403-1409(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10651830; DOI=10.1046/j.1432-1327.2000.01076.x;
RA Ha T.S., Jeong S.Y., Cho S.-W., Jeon H.-K., Roh G.S., Choi W.S.,
RA Park C.-S.;
RT "Functional characteristics of two BKCa channel variants differentially
RT expressed in rat brain tissues.";
RL Eur. J. Biochem. 267:910-918(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC STRAIN=Sprague-Dawley; TISSUE=Brain cortex;
RA Reimann F.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=Wistar HsdOla; TISSUE=Myometrium;
RA Lawrence K.M., Fenech C.J., Zhang H., Bolton T.B.;
RT "Cloning and expression of smooth muscle specific isoforms of a rat
RT calcium-activated potassium channel.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1028 (ISOFORM 6).
RC STRAIN=Sprague-Dawley;
RX PubMed=10384881;
RX DOI=10.1002/(sici)1098-1136(199904)26:2<166::aid-glia7>3.0.co;2-q;
RA Mi H., Harris-Warrick R.M., Deerinck T.J., Inman I., Ellisman M.H.,
RA Schwarz T.L.;
RT "Identification and localization of Ca(2+)-activated K+ channels in rat
RT sciatic nerve.";
RL Glia 26:166-175(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 62-1209 (ISOFORM 2), ACTIVITY REGULATION, AND
RP MUTAGENESIS OF 685-CYS-HIS-686.
RC STRAIN=Sprague-Dawley; TISSUE=Cerebral artery;
RX PubMed=16166559; DOI=10.1161/01.res.0000186180.47148.7b;
RA Jaggar J.H., Li A., Parfenova H., Liu J., Umstot E.S., Dopico A.M.,
RA Leffler C.W.;
RT "Heme is a carbon monoxide receptor for large-conductance Ca2+-activated K+
RT channels.";
RL Circ. Res. 97:805-812(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 62-1209 (ISOFORMS 2 AND 5).
RC STRAIN=Sprague-Dawley; TISSUE=Aorta, and Cerebral artery;
RA Liu J., Asuncion-Chin M.T., Liu P., Dopico A.M.;
RT "Slo subunits cloned from freshly isolated rat cerebral artery myocytes.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP ALTERNATIVE SPLICING (ISOFORM 7).
RX PubMed=11278440; DOI=10.1074/jbc.m008852200;
RA Zarei M.M., Zhu N., Alioua A., Eghbali M., Stefani E., Toro L.;
RT "A novel MaxiK splice variant exhibits dominant-negative properties for
RT surface expression.";
RL J. Biol. Chem. 276:16232-16239(2001).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-712; SER-925 AND SER-929, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. 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).
CC -!- ACTIVITY REGULATION: Ethanol and carbon monoxide-bound heme increase
CC channel activation. Heme inhibits channel activation.
CC {ECO:0000269|PubMed:16166559}.
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 -!- INTERACTION:
CC Q62976; P02688: Mbp; NbExp=4; IntAct=EBI-1638146, EBI-1638296;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Endoplasmic reticulum membrane;
CC Multi-pass membrane protein. Note=Has a dominant-negative effect on
CC other isoforms, preventing their localization to the cell membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=May be partially controlled by hormonal stress. Additional
CC isoforms seem to exist.;
CC Name=1;
CC IsoId=Q62976-1; Sequence=Displayed;
CC Name=2; Synonyms=B, C, cvb1, cvb2;
CC IsoId=Q62976-2; Sequence=VSP_009970, VSP_009973, VSP_009976;
CC Name=3;
CC IsoId=Q62976-3; Sequence=VSP_009970, VSP_009973, VSP_009976,
CC VSP_009982;
CC Name=4; Synonyms=STTEX;
CC IsoId=Q62976-8; Sequence=VSP_009974, VSP_009976;
CC Name=5; Synonyms=A;
CC IsoId=Q62976-9; Sequence=VSP_009973, VSP_009976, VSP_009978,
CC VSP_009979;
CC Name=6; Synonyms=SLON-1;
CC IsoId=Q62976-10; Sequence=VSP_009970, VSP_009976;
CC Name=7; Synonyms=SV1;
CC IsoId=Q62976-11; Sequence=VSP_009971;
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.
CC -!- PTM: Phosphorylated (Probable). Phosphorylation by kinases such as PKA
CC and/or PKG. In smooth muscles, phosphorylation affects its activity (By
CC similarity). {ECO:0000250, ECO:0000305}.
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 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 -!- SEQUENCE CAUTION:
CC Sequence=AAB51398.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U93052; AAB51398.1; ALT_FRAME; mRNA.
DR EMBL; AF135265; AAD34786.1; -; mRNA.
DR EMBL; U40603; AAB96356.1; -; mRNA.
DR EMBL; U55995; AAA99161.1; -; mRNA.
DR EMBL; AF083341; AAC32866.1; -; mRNA.
DR EMBL; AY330290; AAP82450.1; -; mRNA.
DR EMBL; AY330291; AAP82451.1; -; mRNA.
DR EMBL; AY330292; AAP82452.1; -; mRNA.
DR EMBL; AY330293; AAP82453.2; -; mRNA.
DR EMBL; AY330294; AAP82454.1; -; mRNA.
DR RefSeq; NP_114016.1; NM_031828.1.
DR AlphaFoldDB; Q62976; -.
DR SMR; Q62976; -.
DR BioGRID; 249823; 5.
DR CORUM; Q62976; -.
DR DIP; DIP-40510N; -.
DR IntAct; Q62976; 41.
DR MINT; Q62976; -.
DR STRING; 10116.ENSRNOP00000058962; -.
DR BindingDB; Q62976; -.
DR ChEMBL; CHEMBL5505; -.
DR GuidetoPHARMACOLOGY; 380; -.
DR TCDB; 1.A.1.3.2; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q62976; -.
DR PhosphoSitePlus; Q62976; -.
DR SwissPalm; Q62976; -.
DR PRIDE; Q62976; -.
DR ABCD; Q62976; 3 sequenced antibodies.
DR Ensembl; ENSRNOT00000066928; ENSRNOP00000061684; ENSRNOG00000005985. [Q62976-3]
DR GeneID; 83731; -.
DR KEGG; rno:83731; -.
DR CTD; 3778; -.
DR RGD; 620715; Kcnma1.
DR VEuPathDB; HostDB:ENSRNOG00000005985; -.
DR GeneTree; ENSGT00940000154935; -.
DR InParanoid; Q62976; -.
DR OrthoDB; 124461at2759; -.
DR PhylomeDB; Q62976; -.
DR Reactome; R-RNO-1296052; Ca2+ activated K+ channels.
DR PRO; PR:Q62976; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000005985; Expressed in frontal cortex and 14 other tissues.
DR ExpressionAtlas; Q62976; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0005901; C:caveola; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0048787; C:presynaptic active zone membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; ISO:RGD.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0060072; F:large conductance calcium-activated potassium channel activity; IDA:RGD.
DR GO; GO:0099507; F:ligand-gated ion channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005267; F:potassium channel activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:RGD.
DR GO; GO:0007628; P:adult walking behavior; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IDA:RGD.
DR GO; GO:0048469; P:cell maturation; ISO:RGD.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR GO; GO:0060082; P:eye blink reflex; ISO:RGD.
DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; ISO:RGD.
DR GO; GO:0045475; P:locomotor rhythm; ISO:RGD.
DR GO; GO:0060073; P:micturition; ISO:RGD.
DR GO; GO:0045794; P:negative regulation of cell volume; ISO:RGD.
DR GO; GO:1904348; P:negative regulation of small intestine smooth muscle contraction; IMP:RGD.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:0019228; P:neuronal action potential; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0006813; P:potassium ion transport; ISO:RGD.
DR GO; GO:0032344; P:regulation of aldosterone metabolic process; ISO:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0060087; P:relaxation of vascular associated smooth muscle; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; IDA:RGD.
DR GO; GO:0034465; P:response to carbon monoxide; ISO:RGD.
DR GO; GO:0031960; P:response to corticosteroid; IDA:RGD.
DR GO; GO:0043627; P:response to estrogen; IDA:RGD.
DR GO; GO:0001666; P:response to hypoxia; IDA:RGD.
DR GO; GO:0006970; P:response to osmotic stress; ISO:RGD.
DR GO; GO:0009268; P:response to pH; IDA:RGD.
DR GO; GO:0046541; P:saliva secretion; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0060083; P:smooth muscle contraction involved in micturition; ISO:RGD.
DR GO; GO:0042311; P:vasodilation; IMP:RGD.
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; Endoplasmic reticulum;
KW Ion channel; Ion transport; Lipoprotein; Magnesium; Membrane;
KW Metal-binding; Palmitate; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..1209
FT /note="Calcium-activated potassium channel subunit alpha-1"
FT /id="PRO_0000054137"
FT TOPO_DOM 1..87
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical; Name=Segment S0"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..336
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 337..359
FT /note="Pore-forming; Name=P region"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..368
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..1209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 416..559
FT /note="RCK N-terminal"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..577
FT /note="Segment S7"
FT REGION 614..634
FT /note="Segment S8"
FT REGION 682..686
FT /note="Heme-binding motif"
FT REGION 704..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..804
FT /note="Segment S9"
FT REGION 1006..1026
FT /note="Segment S10"
FT REGION 1160..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 353..356
FT /note="Selectivity for potassium"
FT MOTIF 977..999
FT /note="Calcium bowl"
FT COMPBIAS 713..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 440
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 986
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 989
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 992
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 994
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 710
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08460"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 725
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08460"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08460"
FT MOD_RES 917
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08460"
FT MOD_RES 925
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28204"
FT MOD_RES 1198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28204"
FT LIPID 119
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 120
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 122
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..30
FT /note="Missing (in isoform 2, isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10384881,
FT ECO:0000303|PubMed:16166559, ECO:0000303|PubMed:9403560,
FT ECO:0000303|Ref.4, ECO:0000303|Ref.7"
FT /id="VSP_009970"
FT VAR_SEQ 181
FT /note="L -> AFERSSLLARISIQKDGCQCVLFSSHFMPRLLM (in isoform
FT 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_009971"
FT VAR_SEQ 644..647
FT /note="Missing (in isoform 2, isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16166559,
FT ECO:0000303|PubMed:9403560, ECO:0000303|Ref.4,
FT ECO:0000303|Ref.7"
FT /id="VSP_009973"
FT VAR_SEQ 703
FT /note="L -> LIYSKMSIYKRMSRACCFDCGRSERDCSCMSGRVRGNVDTLERNFPL
FT SSVSVNDCSTSFRAF (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_009974"
FT VAR_SEQ 949..975
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10384881,
FT ECO:0000303|PubMed:16166559, ECO:0000303|PubMed:9403560,
FT ECO:0000303|Ref.3, ECO:0000303|Ref.4, ECO:0000303|Ref.7"
FT /id="VSP_009976"
FT VAR_SEQ 1128..1165
FT /note="RYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSH -> SNRRCWWFSK
FT RQDIHQQKRNGLQMRRIMPIPETFKSSP (in isoform 5)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_009978"
FT VAR_SEQ 1166..1209
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_009979"
FT VAR_SEQ 1203..1209
FT /note="KKEMVYR -> NNRRCWWFSKRQDIHQQKRNGLQMRRIMPIPETFKSSP
FT (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_009982"
FT MUTAGEN 685..686
FT /note="CH->SR: Loss of heme-induced channel inhibition as
FT well as carbon monoxide-induced channel activation."
FT /evidence="ECO:0000269|PubMed:16166559"
FT CONFLICT 33
FT /note="Missing (in Ref. 1; AAB51398 and 4; AAA99161)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="I -> V (in Ref. 7; AAP82452)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="G -> V (in Ref. 5; AAC32866)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="K -> E (in Ref. 1; AAB51398)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="L -> P (in Ref. 7; AAP82451)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="E -> Q (in Ref. 5; AAC32866)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="N -> K (in Ref. 7; AAP82451)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="N -> D (in Ref. 7; AAP82451)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="R -> I (in Ref. 7; AAP82451)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="I -> V (in Ref. 7; AAP82452)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="I -> S (in Ref. 7; AAP82452)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="S -> N (in Ref. 7; AAP82450)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="L -> P (in Ref. 4; AAA99161)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="T -> A (in Ref. 7; AAP82452)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="T -> S (in Ref. 4; AAA99161)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="T -> TLGT (in Ref. 7; AAP82452)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="N -> S (in Ref. 7; AAP82451)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="N -> D (in Ref. 7; AAP82451)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="Q -> K (in Ref. 1; AAB51398)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="S -> P (in Ref. 7; AAP82452)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="R -> T (in Ref. 4; AAA99161)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="A -> S (in Ref. 5; AAC32866)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="L -> H (in Ref. 7; AAP82452)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="A -> V (in Ref. 6; AAP82454)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="N -> T (in Ref. 1; AAB51398)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="E -> G (in Ref. 4; AAA99161)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="K -> R (in Ref. 7; AAP82452)"
FT /evidence="ECO:0000305"
FT CONFLICT 659
FT /note="I -> T (in Ref. 3; AAB96356)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="Q -> R (in Ref. 1; AAB51398)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="R -> K (in Ref. 1; AAB51398)"
FT /evidence="ECO:0000305"
FT CONFLICT 685..687
FT /note="CHD -> YHE (in Ref. 7; AAP82452)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="R -> K (in Ref. 2; AAD34786)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="L -> S (in Ref. 6; AAP82454)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="F -> L (in Ref. 4; AAA99161)"
FT /evidence="ECO:0000305"
FT CONFLICT 780
FT /note="A -> V (in Ref. 6; AAP82454)"
FT /evidence="ECO:0000305"
FT CONFLICT 806
FT /note="N -> NRN (in Ref. 7; AAP82451)"
FT /evidence="ECO:0000305"
FT CONFLICT 864
FT /note="I -> L (in Ref. 5; AAC32866)"
FT /evidence="ECO:0000305"
FT CONFLICT 885
FT /note="L -> V (in Ref. 5; AAC32866)"
FT /evidence="ECO:0000305"
FT CONFLICT 940
FT /note="I -> T (in Ref. 6; AAP82453)"
FT /evidence="ECO:0000305"
FT CONFLICT 989
FT /note="D -> G (in Ref. 7; AAP82451)"
FT /evidence="ECO:0000305"
FT CONFLICT 1005
FT /note="P -> L (in Ref. 4; AAA99161)"
FT /evidence="ECO:0000305"
FT CONFLICT 1012
FT /note="F -> S (in Ref. 5; AAC32866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1093
FT /note="Y -> C (in Ref. 7; AAP82452)"
FT /evidence="ECO:0000305"
FT CONFLICT 1107
FT /note="L -> F (in Ref. 7; AAP82451)"
FT /evidence="ECO:0000305"
FT CONFLICT 1173
FT /note="S -> P (in Ref. 6; AAP82453)"
FT /evidence="ECO:0000305"
FT CONFLICT 1188
FT /note="N -> S (in Ref. 6; AAP82454)"
FT /evidence="ECO:0000305"
FT CONFLICT 1203
FT /note="K -> NR (in Ref. 1; AAB51398, 2; AAD34786, 6;
FT AAP82454 and 7; AAP82451)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1209 AA; 134374 MW; 14F19072DA7F22FE CRC64;
MANGGGGGGG GSSGSSGGGG GGGGGETALR MSSNIHANHL SLDASSSSSS SSSSSSSSSS
SVHEPKMDAL IIPVTMEVPC DSRGQRMWWA FLASSMVTFF GGLFIILLWR TLKYLWTVCC
HCGGKTKEAQ KINNGSSQAD GTLKPVDEKE EVVAAEVGWM TSVKDWAGVM ISAQTLTGRV
LVVLVFALSI GALVIYFIDS SNPIESCQNF YKDFTLQIDM AFNVFFLLYF GLRFIAANDK
LWFWLEVNSV VDFFTVPPVF VSVYLNRSWL GLRFLRALRL IQFSEILQFL NILKTSNSIK
LVNLLSIFIS TWLTAAGFIH LVENSGDPWE NFQNNQALTY WECVYLLMVT MSTVGYGDVY
AKTTLGRLFM VFFILGGLAM FASYVPEIIE LIGNRKKYGG SYSAVSGRKH IVVCGHITLE
SVSNFLKDFL HKDRDDVNVE IVFLHNISPN LELEALFKRH FTQVEFYQGS VLNPHDLARV
KIESADACLI LANKYCADPD AEDASNIMRV ISIKNYHPKI RIITQMLQYH NKAHLLNIPS
WNWKEGDDAI CLAELKLGFI AQSCLAQGLS TMLANLFSMR SFIKIEEDTW QKYYLEGVSN
EMYTEYLSSA FVGLSFPTVC ELCFVKLKLL MIAIEYKSAN RESRSRKRIL INPGNHLKIQ
EGTLGFFIAS DAKEVKRAFF YCKACHDDVT DPKRIKKCGC RRLEDEQPPT LSPKKKQRNG
GMRNSPNTSP KLMRHDPLLI PGNDQIDNMD SNVKKYDSTG MFHWCAPKEI EKVILTRSEA
AMTVLSGHVV VCIFGDVSSA LIGLRNLVMP LRASNFHYHE LKHIVFVGSI EYLKREWETL
HNFPKVSILP GTPLSRADLR AVNINLCDMC VILSANQNNI DDTSLQDKEC ILASLNIKSM
QFDDSIGVLQ ANSQGFTPPG MDRSSPDNSP VHGMLRQPSI TTGVNIPIIT ELAKPGKLPL
VSVNQEKNSG THILMITELV NDTNVQFLDQ DDDDDPDTEL YLTQPFACGT AFAVSVLDSL
MSATYFNDNI LTLIRTLVTG GATPELEALI AEENALRGGY STPQTLANRD RCRVAQLALL
DGPFADLGDG GCYGDLFCKA LKTYNMLCFG IYRLRDAHLS TPSQCTKRYV ITNPPYEFEL
VPTDLIFCLM QFDHNAGQSR ASLSHSSHSS QSSSKKSSSV HSIPSTANRP NRPKSRESRD
KQKKEMVYR
