CAC1B_RABIT
ID CAC1B_RABIT Reviewed; 2339 AA.
AC Q05152;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Voltage-dependent N-type calcium channel subunit alpha-1B;
DE AltName: Full=Brain calcium channel III;
DE Short=BIII;
DE AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 5;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.2;
GN Name=CACNA1B; Synonyms=CACH5, CACNL1A5;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8386525; DOI=10.1016/0896-6273(93)90162-k;
RA Fujita Y., Mynlieff M., Dirksen R.T., Kim M.-S., Niidome T., Nakai J.,
RA Friedrich T., Iwabe N., Miyata T., Furuichi T., Furutama D., Mikoshiba K.,
RA Mori Y., Beam K.G.;
RT "Primary structure and functional expression of the omega-conotoxin-
RT sensitive N-type calcium channel from rabbit brain.";
RL Neuron 10:585-598(1993).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q02294}.
CC -!- ACTIVITY REGULATION: Is specifically blocked by omega-conotoxin GVIA
CC (By similarity). Is specifically blocked by omega-conotoxin MVIIA
CC (ziconotide) (By similarity). Is insensitive to dihydropyridines (DHP).
CC {ECO:0000250|UniProtKB:Q00975, ECO:0000250|UniProtKB:Q02294}.
CC -!- SUBUNIT: Multisubunit complex consisting of alpha-1, alpha-2, beta and
CC delta subunits in a 1:1:1:1 ratio. The channel activity is directed by
CC the pore-forming and voltage-sensitive alpha-1 subunit. In many cases,
CC this subunit is sufficient to generate voltage-sensitive calcium
CC channel activity. The auxiliary subunits beta and alpha-2/delta linked
CC by a disulfide bridge regulate the channel activity. Interacts with
CC RIMS1. Interacts with FMR1 (via C-terminus); this interaction induces a
CC decrease in the number of presynaptic functional CACNA1B channels at
CC the cell surface. {ECO:0000250|UniProtKB:O55017}.
CC -!- INTERACTION:
CC Q05152; P62158: CALM3; Xeno; NbExp=2; IntAct=EBI-15685496, EBI-397435;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q00975}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q00975}.
CC -!- TISSUE SPECIFICITY: Widespread expression throughout the brain. Highest
CC levels in corpus striatum and midbrain.
CC -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments probably represent the voltage-
CC sensor and are characterized by a series of positively charged amino
CC acids at every third position.
CC -!- PTM: Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1B subfamily. {ECO:0000305}.
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DR EMBL; D14157; BAA03202.1; -; mRNA.
DR RefSeq; NP_001075660.1; NM_001082191.1.
DR PDB; 3DVE; X-ray; 2.35 A; B=1855-1875.
DR PDB; 3DVJ; X-ray; 2.80 A; B=1853-1873.
DR PDBsum; 3DVE; -.
DR PDBsum; 3DVJ; -.
DR AlphaFoldDB; Q05152; -.
DR SMR; Q05152; -.
DR BioGRID; 1172002; 2.
DR DIP; DIP-29592N; -.
DR IntAct; Q05152; 2.
DR STRING; 9986.ENSOCUP00000010930; -.
DR iPTMnet; Q05152; -.
DR PRIDE; Q05152; -.
DR GeneID; 100008979; -.
DR KEGG; ocu:100008979; -.
DR CTD; 774; -.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; Q05152; -.
DR OrthoDB; 172471at2759; -.
DR EvolutionaryTrace; Q05152; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006816; P:calcium ion transport; IDA:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 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; IPR005447; VDCC_N_a1su.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
DR PANTHER; PTHR10037:SF289; PTHR10037:SF289; 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 PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Calcium; Calcium channel; Calcium transport;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Metal-binding; Methylation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..2339
FT /note="Voltage-dependent N-type calcium channel subunit
FT alpha-1B"
FT /id="PRO_0000053923"
FT TOPO_DOM 1..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 91..114
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 115..131
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 132..152
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 153..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 164..182
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 183..187
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 188..211
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 212..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 222..244
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 245..331
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 332..356
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 357..483
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 484..502
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 503..512
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 513..535
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 536..545
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 546..567
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 568..574
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 575..587
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 588..605
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 606..631
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 632..683
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 684..710
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 711..1156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1157..1175
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1176..1183
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1184..1208
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1209..1222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1223..1243
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1244..1249
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1250..1270
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1271..1288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1289..1308
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1309..1395
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1396..1421
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1422..1476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1477..1495
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1496..1503
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1504..1528
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1529..1538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1539..1560
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1561..1566
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1567..1585
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1586..1604
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1605..1624
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1625..1686
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1687..1710
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1711..2339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT REPEAT 82..359
FT /note="I"
FT REPEAT 469..713
FT /note="II"
FT REPEAT 1142..1424
FT /note="III"
FT REPEAT 1461..1714
FT /note="IV"
FT DOMAIN 1727..1762
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 15..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..396
FT /note="Binding to the beta subunit"
FT /evidence="ECO:0000250"
FT REGION 809..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1983..2312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..1026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2049..2065
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2097..2133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2169..2212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2284..2306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 452..459
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 545
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT BINDING 585
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT BINDING 588
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT BINDING 1740
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1746
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1751
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT SITE 314
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 663
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1370
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1658
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT MOD_RES 22
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 1074
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 2067
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 2224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 2233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 2256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT CARBOHYD 1566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 1855..1869
FT /evidence="ECO:0007829|PDB:3DVE"
SQ SEQUENCE 2339 AA; 261181 MW; 0413DA93794C8B34 CRC64;
MVRFGDELGG RYGGAGGAER ARGGGAGGAG GPGPGGLPPG QRVLYKQSIA QRARTMALYN
PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM ILATIIANCI VLALEQHLPD
GDKTPMSERL DDTEPYFIGI FCFEAGIKIL ALGFVLHKGS YLRNGWNVMD FVVVLTGILA
TAGTDFDLRT LRAVRVLRPL KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII
GLEFYMGKFH KACFPNSTDP DPVGDFPCGK EAPARLCEGD TECREYWAGP NFGITNFDNI
LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL VLGVLSGEFA
KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML AEEDRNAEEK SPLDAVLKRA
AAKKSRSDLI QAEEGEGRLT GLCAPGSPFA RASLKSGKTE SSSYFRRKEK MFRFFIRRMV
KAQSFYWTVL CVVALNTLCV AMVHYNQPQR LTTALYFAEF VFLGLFLTEM SLKMYGLGPR
SYFRSSFNCF DFGVIVGSIF EVVWAAVKPG TSFGISVLRA LRLLRIFKVT KYWNSLRNLV
VSLLNSMKSI ISLLFLLFLF IVVFALLGMQ LFGGQFNFKD ETPTTNFDTF PAAILTVFQI
LTGEDWNAVM YHGIESQGGV SRGMFSSFYF IVLTLFGNYT LLNVFLAIAV DNLANAQELT
KDEEEMEEAA NQKLALQKAK EVAEVSPMSA ANISIAARQQ NSAKARSVWE QRASQLRLQN
LRASCEALYS EMDPEERLRY ATARHLRPDV KTHLDRPLVV EPGRDAPRGP PGGKSRPDGS
EAPEGADPPR RHHRHRDKDK APATVPSAGE QDRAEALRAE GGELGPREER GRPRRSRSKE
APGAPEVRSD RGRGPCPEGG RRHHRRGSPE EAAEREPRRH RAHRHGPDPG KEGPASGTRG
ERRARHRTGP RACPREAESS EEPARRHRAR HKAPPTQETA EKDKEAAEKG GEATEAEKDK
EARNHQPKEL PCDLEAIGML GVGAVHTLPS TCLQKVEEQP EDADNQRNVT RMGSQPPDTS
TTVHIPVTLT GPPGETTVVP SGNVDLESQA EGKKEVETSD VMRSGPRPIV PYSSMFCLSP
TNLLRRCCHY IVTMRYFEMV ILVVIALSSI ALAAEDPVRT DSPRNNALKY MDYIFTGVFT
FEMVIKMIDL GLLLHPGAYF RDLWNILDFI VVSGALVAFA FSGSKGKDIS TIKSLRVLRV
LRPLKTIKRL PKLKAVFDCV VNSLKNVLNI LIVYMLFMFI FAVIAVQLFK GKFFYCTDES
KELERDCRGQ YLDYEKEEVE AQPRQWKKYD FHYDNVLWAL LTLFTVSTGE GWPMVLKHSV
DATYEEQGPS PGYRMELSIF YVVYFVVFPF FFVNIFVALI IITFQEQGDK VMSECSLEKN
ERACIDFAIS ARPLTRYMPQ NKQSFQYKTW TFVVSPPFEY FIMAMIALNT VVLMMKFYDA
PYEYELMLKC LNIVFTSMFS MECVLKIIAF GVLNYFRDAW NVFDFVTVLG SITDILVTEI
ANNFINLSFL RLFRAARLIK LLRQGYTIRI LLWTFVQSFK ALPYVCLLIA MLFFIYAIIG
MQVFGNIALD DDTSINRHNN FRTFLQALML LFRSATGEAW HEIMLSCLSS RACDEHSNAS
ECGSDFAYFY FVSFIFLCSF LMLNLFVAVI MDNFEYLTRD SSILGPHHLD EFIRVWAEYD
PAACGRISYS DMFEMLKHMS PPLGLGKKCP ARVAYKRLVR MNMPISSEDM TVHFTSTLMA
LIRTALDIKL APAGTKQHQC DAELRKEISC VWANLPQKTL DLLVPPHKPD EMTVGKVYAA
LMIFDFYKQN KTSRDQTQQA PGGLSQLGPV SLFHPLKATL EQTQPALRGA RAFLRQKSSA
SLSNGGAVQT QESGIKESVS WGTQRTQDVL CEARAPLERG HSAEIPVGQP GTLAVDVQMQ
NMTLSGPDAE PQPGLESQGR AASMPRLAAE TQPAPDASPM KRSISTLAPR PHTARLGSTA
LDRPAPSQAP HHHHHRCHRR RDRKQRSLEK GPSLSADTDG APDSTVGPGL PTGEGPPGCR
RERERRQERG RSQERRQPSS SSSEKHRFYS CDRFGGREPP QPKPSLSSHP TSPTAGQEPG
PHPQGSGSVH GSPLLSTSGA STPGRGRRQL PQTPLTPRPS VTYKTANSSP VHFAGAPSGL
PAFSPGRLSR GLSEHNALLQ RDPLSRPLAP GSRIGSDPYL GQRLDSEAPA RALPEDAPAF
EETAASNSGR SSRTSYVSSL TSQPPPLRRV PNGYHCTLGL GGGGRARRGC HHPDRDRRC
