ID   A2AIS0_MOUSE            Unreviewed;      2288 AA.
AC   A2AIS0;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   02-SEP-2026, entry version 149.
DE   RecName: Full=Voltage-dependent N-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=Cacna1b {ECO:0000313|Ensembl:ENSMUSP00000063236.8,
GN   ECO:0000313|MGI:MGI:88296};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000063236.8, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0007829|PubMed:16452087}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [2] {ECO:0007829|PubMed:17114649}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000063236.8, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000063236.8,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RG   Mouse Genome Sequencing Consortium;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5] {ECO:0000313|Ensembl:ENSMUSP00000063236.8, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000063236.8,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=21750661;
RA   Church D.M., Schneider V.A., Graves T., Auger K., Cunningham F., Bouk N.,
RA   Chen H.C., Agarwala R., McLaren W.M., Ritchie G.R., Albracht D.,
RA   Kremitzki M., Rock S., Kotkiewicz H., Kremitzki C., Wollam A., Trani L.,
RA   Fulton L., Fulton R., Matthews L., Whitehead S., Chow W., Torrance J.,
RA   Dunn M., Harden G., Threadgold G., Wood J., Collins J., Heath P.,
RA   Griffiths G., Pelan S., Grafham D., Eichler E.E., Weinstock G.,
RA   Mardis E.R., Wilson R.K., Howe K., Flicek P., Hubbard T.;
RT   "Modernizing reference genome assemblies.";
RL   PLoS Biol. 9:e1001091-e1001091(2011).
RN   [6] {ECO:0007829|PubMed:24129315}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24129315;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [7] {ECO:0000313|Ensembl:ENSMUSP00000063236.8}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000063236.8};
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC       of calcium ions into excitable cells and are also involved in a variety
CC       of calcium-dependent processes, including muscle contraction, hormone
CC       or neurotransmitter release, gene expression, cell motility, cell
CC       division and cell death. This alpha-1B subunit gives rise to N-type
CC       calcium currents. N-type calcium channels belong to the 'high-voltage
CC       activated' (HVA) group. They are involved in pain signaling. Calcium
CC       channels containing alpha-1B subunit may play a role in directed
CC       migration of immature neurons. Mediates Ca(2+) release probability at
CC       hippocampal neuronal soma and synaptic terminals.
CC       {ECO:0000256|ARBA:ARBA00049617}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671,
CC         ChEBI:CHEBI:29108; Evidence={ECO:0000256|ARBA:ARBA00036634};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. CACNA1B subfamily.
CC       {ECO:0000256|ARBA:ARBA00005685}.
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DR   RefSeq; NP_031605.2; NM_007579.4.
DR   SMR; A2AIS0; -.
DR   iPTMnet; A2AIS0; -.
DR   SwissPalm; A2AIS0; -.
DR   ProteomicsDB; 318524; -.
DR   Antibodypedia; 32538; 150 antibodies from 29 providers.
DR   DNASU; 12287; -.
DR   Ensembl; ENSMUST00000070864.14; ENSMUSP00000063236.8; ENSMUSG00000004113.20.
DR   GeneID; 12287; -.
DR   UCSC; uc008ipf.2; mouse.
DR   AGR; MGI:88296; -.
DR   CTD; 774; -.
DR   MGI; MGI:88296; Cacna1b.
DR   VEuPathDB; HostDB:ENSMUSG00000004113; -.
DR   GeneTree; ENSGT00940000155275; -.
DR   HOGENOM; CLU_000540_1_0_1; -.
DR   BioGRID-ORCS; 12287; 2 hits in 79 CRISPR screens.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000004113; Expressed in supraoptic nucleus and 134 other cell types or tissues.
DR   ExpressionAtlas; A2AIS0; baseline and differential.
DR   GO; GO:0098793; C:presynapse; IEA:UniProtKB-ARBA.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR   GO; GO:0007626; P:locomotory behavior; IEA:UniProtKB-ARBA.
DR   GO; GO:0051049; P:regulation of transport; IEA:UniProtKB-ARBA.
DR   GO; GO:0048265; P:response to pain; IEA:UniProtKB-ARBA.
DR   GO; GO:0003008; P:system process; IEA:UniProtKB-ARBA.
DR   FunFam; 1.20.120.350:FF:000001; Voltage-dependent L-type calcium channel subunit alpha; 1.
DR   FunFam; 1.10.238.10:FF:000063; Voltage-dependent N-type calcium channel subunit alpha; 1.
DR   FunFam; 1.20.120.350:FF:000011; Voltage-dependent N-type calcium channel subunit alpha; 1.
DR   FunFam; 1.20.120.350:FF:000013; Voltage-dependent N-type calcium channel subunit alpha; 1.
DR   FunFam; 1.20.120.350:FF:000015; Voltage-dependent N-type calcium channel subunit alpha; 1.
DR   FunFam; 1.10.287.70:FF:000023; Voltage-dependent R-type calcium channel subunit alpha; 1.
DR   FunFam; 1.10.287.70:FF:000025; Voltage-dependent R-type calcium channel subunit alpha; 1.
DR   Gene3D; 1.10.287.70; -; 4.
DR   Gene3D; 6.10.250.2180; -; 1.
DR   Gene3D; 6.10.250.2500; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR050599; VDCC_alpha-1_subunit.
DR   InterPro; IPR005447; VDCC_N_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR45628; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A SUBUNIT ALPHA-1; 1.
DR   PANTHER; PTHR45628:SF6; VOLTAGE-DEPENDENT N-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1B; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01631; NVDCCALPHA1.
DR   SMART; SM01062; Ca_chan_IQ; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   1: Evidence at protein level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR602077-1};
KW   Calcium channel {ECO:0000256|ARBA:ARBA00022673,
KW   ECO:0000256|RuleBase:RU003808};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW   ECO:0000256|RuleBase:RU003808};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602077-1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A2AIS0,
KW   ECO:0007829|ProteomicsDB:A2AIS0};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW   ECO:0000256|RuleBase:RU003808}.
FT   TRANSMEM        97..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        135..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        223..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        300..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        333..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        484..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        510..527
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        548..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        609..631
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        687..709
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1139..1157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1177..1197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1209..1227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1270..1292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1382..1407
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1463..1481
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1493..1519
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1586..1604
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1673..1696
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1712..1747
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          798..1014
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1041..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1933..2154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2191..2210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..37
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        804..825
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        868..884
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        913..923
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        960..971
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        987..1014
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1049..1065
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2000..2014
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2049..2065
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2092..2102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2113..2129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         314
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         663
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         1353
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ   SEQUENCE   2288 AA;  257072 MW;  2847EB88FE600366 CRC64;
     MVRFGDELGG RYGGTGGGER ARGGGAGGAG GPGQGGLPPG QRVLYKQSIA QRARTMALYN
     PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM ILATIIANCI VLALEQHLPD
     GDKTPMSERL DDTEPYFIGI FCFEAGIKII ALGFVFHKGS YLRNGWNVMD FVVVLTGILA
     TAGTDFDLRT LRAVRVLRPL KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII
     GLEFYMGKFH KACFPNSTDT EPVGDFPCGK DPPARQCDGD TECREYWPGP NFGITNFDNI
     LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL VLGVLSGEFA
     KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML AEEDKNAEEK SPLDVLKRAA
     TKKSRNDLIH AEEGEDRFVD LCAVGSPFAR ASLKSGKTES SSYFRRKEKM FRFFIRRMVK
     AQSFYWVVLC VVALNTLCVA MVHYNQPQRL TTALYFAEFV FLGLFLTEMS LKMYGLGPRS
     YFRSSFNCFD FGVIVGSIFE VVWAAIKPGT SFGISVLRAL RLLRIFKVTK YWNSLRNLVV
     SLLNSMKSII SLLFLLFLFI VVFALLGMQL FGGQFNFQDE TPTTNFDTFP AAILTVFQIL
     TGEDWNAVMY HGIESQGGVS KGMFSSFYFI VLTLFGNYTL LNVFLAIAVD NLANAQELTK
     DEEEMEEAAN QKLALQKAKE VAEVSPMSAA NISIAAQQNS AKARSVWEQR ASQLRLQNLR
     ASCEALYSEM DPEERLRYAS TRHVRPDMKT HMDRPLVVEP GRDGLRGPVG SKSKPEGTEA
     TESADLPRRH HRHRDRDKTS ATAPAGGEQD RTESTETGAR EERARPRRSH SKETPGADTQ
     VRCERSRRHH RRGSPEEATE REPRRHRAHR HAQDSSKEGT APVLVPKGER RARHRGPRTG
     PREAENNEEP TRRHRARHKV PPTLQPPERE AAEKESNAVE GDKETRNHQP KEPHCDLEAI
     AVTGVGPLHM LPSTCLQKVD EQPEDADNQR NVTRMGSQPS DPSTTVHVPV TLTGPPGETP
     VVPSGNMNLE GQAEGKKEAE ADDVLRRGPR PIVPYSSMFC LSPTNLLRRF CHYIVTMRYF
     EMVILVVIAL SSIALAAEDP VRTDSFRNNA LKYMDYIFTG VFTFEMVIKM IDLGLLLHPG
     AYFRDLWNIL DFIVVSGALV AFAFSGSKGK DINTIKSLRV LRVLRPLKTI KRLPKLKAVF
     DCVVNSLKNV LNILIVYMLF MFIFAVIAVQ LFKGKFFYCT DESKELERDC RGQYLDYEKE
     EVEAQPRQWK KYDFHYDNVL WALLTLFTVS TGEGWPMVLK HSVDATYEEQ GPSPGFRMEL
     SIFYVVYFVV FPFFFVNIFV ALIIITFQEQ GDKVMSECSL EKNERACIDF AISAKPLTRY
     MPQNKQSFQY KTWTFVVSPP FEYFIMAMIA LNTVVLMMKF YDAPYEYELM LKCLNIVFTS
     MFSMECILKI IAFGVLNYFR DAWNVFDFVT VLGSITDILV TEIAETNNFI NLSFLRLFRA
     ARLIKLLRQG YTIRILLWTF VQSFKALPYV CLLIAMLFFI YAIIGMQVFG NIALDDDTSI
     NRHNNFRTFL QALMLLFRSA TGEAWHEIML SCLGNRACDP HANASECGSD FAYFYFVSFI
     FLCSFLMLNL FVAVIMDNFE YLTRDSSILG PHHLDEFIRV WAEYDPAACG RISYNDMFEM
     LKHMSPPLGL GKKCPARVAY KRLVRMNMPI SNEDMTVHFT STLMALIRTA LEIKLAPADE
     MTVGKVYAAL MIFDFYKQNK TTRDQTHQAP GGLSQMGPVS LFHPLKATLE QTQPAVLRGA
     RVFLRQKSAT SLSNGGAIQT QESGIKESLS WGTQRTQDAL YEARAPLERG HSAEIPVGQS
     GTLAVDVQMQ NMTLRGPDGE PQPGLESQGR AASMPRLAAE TQPAPNASPM KRSISTLAPR
     PHGTQLCSTV LDRPPPSQAS HHHHHRCHRR RDKKQRSLEK GPSLSVDPEG APSTAAGPGL
     PHGEGSTACR RDRKQERGRS QERRQPSSSS SEKQRFYSCD RFGSREPPQL MPSLSSHPTS
     PTAALEPAPH PQGSGSVNGS PLMSTSGAST PGRGGRRQLP QTPLTPRPSI TYKTANSSPV
     HFAEGQSGLP AFSPGRLSRG LSEHNALLQK EPLSQPLAPG SRIGSDPYLG QRLDSEASAH
     TLPEDTLTFE EAVATNSGRS SRTSYVSSLT SQSHPLRRVP NGYHCTLGLS TGVRARHSYH
     HPDQDHWC
//