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Database: UniProt
Entry: CAC1A_RABIT
LinkDB: CAC1A_RABIT
Original site: CAC1A_RABIT 
ID   CAC1A_RABIT             Reviewed;        2424 AA.
AC   P27884; P27883;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   27-SEP-2017, entry version 132.
DE   RecName: Full=Voltage-dependent P/Q-type calcium channel subunit alpha-1A;
DE   AltName: Full=Brain calcium channel I;
DE            Short=BI;
DE   AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 4;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.1;
GN   Name=CACNA1A; Synonyms=CACH4, CACN3, CACNL1A4;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC   TISSUE=Brain;
RX   PubMed=1849233; DOI=10.1038/350398a0;
RA   Mori Y., Friedrich T., Kim M.-S., Mikami A., Nakai J., Ruth P.,
RA   Bosse E., Hofmann F., Flockerzi V., Furuichi T., Mikoshiba K.,
RA   Imoto K., Tanabe T., Numa S.;
RT   "Primary structure and functional expression from complementary DNA of
RT   a brain calcium channel.";
RL   Nature 350:398-402(1991).
RN   [2]
RP   BETA-SUBUNIT BINDING DOMAIN, AND MUTAGENESIS OF GLU-386; LEU-389;
RP   TYR-392 AND GLU-400.
RX   PubMed=7509046; DOI=10.1038/368067a0;
RA   Pragnell M., de Waard M., Mori Y., Tanabe T., Snutch T.P.,
RA   Campbell K.P.;
RT   "Calcium channel beta-subunit binds to a conserved motif in the I-II
RT   cytoplasmic linker of the alpha 1-subunit.";
RL   Nature 368:67-70(1994).
RN   [3]
RP   FUNCTION, AND MUTAGENESIS OF GLU-188 AND GLU-1658.
RX   PubMed=11055992; DOI=10.1085/jgp.116.5.637;
RA   Winterfield J.R., Swartz K.J.;
RT   "A hot spot for the interaction of gating modifier toxins with
RT   voltage-dependent ion channels.";
RL   J. Gen. Physiol. 116:637-644(2000).
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
CC       entry of calcium ions into excitable cells and are also involved
CC       in a variety of calcium-dependent processes, including muscle
CC       contraction, hormone or neurotransmitter release, gene expression,
CC       cell motility, cell division and cell death. The isoform alpha-1A
CC       gives rise to P and/or Q-type calcium currents. P/Q-type calcium
CC       channels belong to the 'high-voltage activated' (HVA) group and
CC       are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-
CC       IVA (omega-Aga-IVA). They are however insensitive to
CC       dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).
CC       {ECO:0000269|PubMed:11055992}.
CC   -!- SUBUNIT: Voltage-dependent calcium channels are multisubunit
CC       complexes, consisting of alpha-1, alpha-2, beta and delta subunits
CC       in a 1:1:1:1 ratio. The channel activity is directed by the pore-
CC       forming and voltage-sensitive alpha-1 subunit. In many cases, this
CC       subunit is sufficient to generate voltage-sensitive calcium
CC       channel activity. The auxiliary subunits beta and alpha-2/delta
CC       linked by a disulfide bridge regulate the channel activity.
CC       Interacts with CABP1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:O00555}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=BI-2; Synonyms=1A-2;
CC         IsoId=P27884-1; Sequence=Displayed;
CC       Name=BI-1; Synonyms=1A-1;
CC         IsoId=P27884-2; Sequence=VSP_000879, VSP_000880;
CC       Name=CBP101; Synonyms=CBP109;
CC         IsoId=P27884-3; Sequence=VSP_000878;
CC       Name=CBP103;
CC         IsoId=P27884-4; Sequence=VSP_000877;
CC       Name=CBP107;
CC         IsoId=P27884-5; Sequence=VSP_000876;
CC   -!- TISSUE SPECIFICITY: Brain specific. Purkinje cells contain
CC       predominantly P-type VSCC, the Q-type being a prominent calcium
CC       current in cerebellar granule cells.
CC   -!- DOMAIN: Each of the four internal repeats contains five
CC       hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one
CC       positively charged transmembrane segment (S4). S4 segments
CC       probably represent the voltage-sensor and are characterized by a
CC       series of positively charged amino acids at every third position.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC       1.A.1.11) family. CACNA1A subfamily. {ECO:0000305}.
DR   EMBL; X57477; CAA40715.1; -; mRNA.
DR   EMBL; X57689; CAA40872.1; -; mRNA.
DR   EMBL; X57476; CAA40714.1; -; mRNA.
DR   EMBL; X57688; CAA40871.1; -; mRNA.
DR   PIR; I46477; I46477.
DR   PIR; I46480; I46480.
DR   RefSeq; NP_001095163.1; NM_001101693.1. [P27884-2]
DR   UniGene; Ocu.2123; -.
DR   PDB; 3DVM; X-ray; 2.60 A; B=1963-1982.
DR   PDBsum; 3DVM; -.
DR   ProteinModelPortal; P27884; -.
DR   SMR; P27884; -.
DR   DIP; DIP-29591N; -.
DR   PRIDE; P27884; -.
DR   GeneID; 100009265; -.
DR   KEGG; ocu:100009265; -.
DR   CTD; 773; -.
DR   HOVERGEN; HBG050763; -.
DR   InParanoid; P27884; -.
DR   KO; K04344; -.
DR   EvolutionaryTrace; P27884; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IC:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IEA:GOC.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR   InterPro; IPR005448; CACNA1A.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF249; PTHR10037:SF249; 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; PR01632; PQVDCCALPHA1.
DR   SMART; SM01062; Ca_chan_IQ; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Calcium channel;
KW   Calcium transport; Cell membrane; Complete proteome; Disulfide bond;
KW   Glycoprotein; Ion channel; Ion transport; Membrane; Metal-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1   2424       Voltage-dependent P/Q-type calcium
FT                                channel subunit alpha-1A.
FT                                /FTId=PRO_0000053918.
FT   TOPO_DOM      1     98       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     99    117       Helical; Name=S1 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    118    135       Extracellular. {ECO:0000255}.
FT   TRANSMEM    136    155       Helical; Name=S2 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    156    167       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    168    185       Helical; Name=S3 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    186    190       Extracellular. {ECO:0000255}.
FT   TRANSMEM    191    209       Helical; Name=S4 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    210    228       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    229    248       Helical; Name=S5 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    249    335       Extracellular. {ECO:0000255}.
FT   TRANSMEM    336    360       Helical; Name=S6 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    361    487       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    488    506       Helical; Name=S1 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    507    521       Extracellular. {ECO:0000255}.
FT   TRANSMEM    522    541       Helical; Name=S2 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    542    549       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    550    568       Helical; Name=S3 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    569    578       Extracellular. {ECO:0000255}.
FT   TRANSMEM    579    597       Helical; Name=S4 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    598    616       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    617    636       Helical; Name=S5 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    637    689       Extracellular. {ECO:0000255}.
FT   TRANSMEM    690    714       Helical; Name=S6 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    715   1253       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1254   1272       Helical; Name=S1 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1273   1288       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1289   1308       Helical; Name=S2 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1309   1320       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1321   1339       Helical; Name=S3 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1340   1350       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1351   1369       Helical; Name=S4 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1370   1388       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1389   1408       Helical; Name=S5 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1409   1495       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1496   1520       Helical; Name=S6 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1521   1575       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1576   1604       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1605   1609       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1610   1629       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1630   1637       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1638   1656       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1657   1665       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1666   1684       Helical; Name=S4 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1685   1703       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1704   1723       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1724   1795       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1796   1820       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1821   2424       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       85    363       I.
FT   REPEAT      473    717       II.
FT   REPEAT     1240   1523       III.
FT   REPEAT     1560   1823       IV.
FT   CA_BIND    1849   1860       {ECO:0000250}.
FT   REGION      383    400       Binding to the beta subunit.
FT   COMPBIAS     13     18       Poly-Gly.
FT   COMPBIAS    727    732       Poly-Glu.
FT   COMPBIAS   1004   1010       Poly-Gly.
FT   COMPBIAS   1012   1017       Poly-Arg.
FT   COMPBIAS   2219   2227       Poly-His.
FT   COMPBIAS   2242   2246       Poly-Arg.
FT   COMPBIAS   2288   2297       Poly-Arg.
FT   COMPBIAS   2298   2301       Poly-Gly.
FT   COMPBIAS   2372   2377       Poly-Pro.
FT   COMPBIAS   2411   2416       Poly-Gly.
FT   SITE        318    318       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE        668    668       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE       1469   1469       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE       1658   1658       Binds to omega-Aga-IVA.
FT   SITE       1765   1765       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   MOD_RES     409    409       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P97445}.
FT   MOD_RES     448    448       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P97445}.
FT   MOD_RES     451    451       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P97445}.
FT   MOD_RES     750    750       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P97445}.
FT   MOD_RES     753    753       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P97445}.
FT   MOD_RES     790    790       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P97445}.
FT   MOD_RES    1091   1091       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P97445}.
FT   MOD_RES    1104   1104       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P97445}.
FT   MOD_RES    1831   1831       Phosphoserine; by PKA. {ECO:0000255}.
FT   MOD_RES    1993   1993       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P97445}.
FT   MOD_RES    2054   2054       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P54282}.
FT   MOD_RES    2072   2072       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P97445}.
FT   MOD_RES    2084   2084       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P54282}.
FT   MOD_RES    2086   2086       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P54282}.
FT   MOD_RES    2127   2127       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P97445}.
FT   MOD_RES    2148   2148       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P54282}.
FT   CARBOHYD    283    283       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1665   1665       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VAR_SEQ     772   1120       Missing (in isoform CBP103).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_000877.
FT   VAR_SEQ     772   1051       Missing (in isoform CBP107).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_000876.
FT   VAR_SEQ    1857   1884       LYRDMYAMLRHMPPPLGLGKNCPARVAY -> HYKDMYSLL
FT                                RVISPPLGLGKKCPHRVAC (in isoform CBP101).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_000878.
FT   VAR_SEQ    2230   2273       RGPGRVSPGVSARRRRRGPVARVRPARAPALAHARARARAP
FT                                ARL -> PAAADKERYGPQDRPDHGHGRARARDQRWSRSPS
FT                                EGREHTTHRQ (in isoform BI-1).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_000879.
FT   VAR_SEQ    2274   2424       Missing (in isoform BI-1). {ECO:0000305}.
FT                                /FTId=VSP_000880.
FT   VARIANT     419    419       Missing (in isoform CBP315).
FT   VARIANT     877    877       A -> T (in isoform CBS).
FT   VARIANT    1104   1104       S -> N (in isoform CBS).
FT   MUTAGEN     188    188       E->K: No change in inhibition by omega-
FT                                Aga-IVA. {ECO:0000269|PubMed:11055992}.
FT   MUTAGEN     386    386       E->S: Reduced beta-subunit interaction.
FT                                {ECO:0000269|PubMed:7509046}.
FT   MUTAGEN     389    389       L->H: Reduced beta-subunit interaction.
FT                                {ECO:0000269|PubMed:7509046}.
FT   MUTAGEN     392    392       Y->S: Reduced beta-subunit interaction.
FT                                {ECO:0000269|PubMed:7509046}.
FT   MUTAGEN     400    400       E->A: No effect on beta-subunit
FT                                interaction.
FT                                {ECO:0000269|PubMed:7509046}.
FT   MUTAGEN    1658   1658       E->K: Loss of inhibition by omega-Aga-
FT                                IVA. {ECO:0000269|PubMed:11055992}.
FT   HELIX      1963   1979       {ECO:0000244|PDB:3DVM}.
SQ   SEQUENCE   2424 AA;  273231 MW;  F7CC4D0AB4B45604 CRC64;
     MARFGDEMPA RYGGGGAGAA AGVVVGAAGG RGAGGSRQGG QPGAQRMYKQ SMAQRARTMA
     LYNPIPVRQN CLTVNRSLFL FSEDNVVRKY AKKITEWPPF EYMILATIIA NCIVLALEQH
     LPDDDKTPMS ERLDDTEPYF IGIFCFEAGI KIIALGFAFH KGSYLRNGWN VMDFVVVLTG
     ILATVGTEFD LRTLRAVRVL RPLKLVSGIP SLQVVLKSIM KAMIPLLQIG LLLFFAILIF
     AIIGLEFYMG KFHTTCFEEG TDDIQGESPA PCGTEEPART CPNGTRCQPY WEGPNNGITQ
     FDNILFAVLT VFQCITMEGW TDLLYNSNDA SGNTWNWLYF IPLIIIGSFF MLNLVLGVLS
     GEFAKERERV ENRRAFLKLR RQQQIERELN GYMEWISKAE EVILAEDETD VEQRHPFDGA
     LRRATIKKSK TDLLHPEEAE DQLADIASVG SPFARASIKS AKLENSSFFH KKERRMRFYI
     RRMVKTQAFY WTVLSLVALN TLCVAIVHYN QPEWLSDFLY YAEFIFLGLF MSEMFIKMYG
     LGTRPYFHSS FNCFDCGVII GSIFEVIWAV IKPGTSFGIS VLRALRLLRI FKVTKYWASL
     RNLVVSLLNS MKSIISLLFL LFLFIVVFAL LGMQLFGGQF NFDEGTPPTN FDTFPAAIMT
     VFQILTGEDW NEVMYDGIKS QGGVQGGMVF SIYFIVLTLF GNYTLLNVFL AIAVDNLANA
     QELTKDEQEE EEAVNQKLAL QKAKEVAEVS PLSAANMSIA MKEQQKNQKP AKSVWEQRTS
     EMRKQNLLAS REALYSEMDP EERWKASYAR HLRPDMKTHL DRPLVVDPQE NRNNNTNKSR
     VAEPTVDQRL GQQRAEDFLR KQARHHDRAR DPSAHAAAGL DARRPWAGSQ EAELSREGPY
     GRESDHQARE GGLEPPGFWE GEAERGKAGD PHRRHAHRQG VGGSGGSRSG SPRTGTADGE
     PRRHRVHRRP GEDGPDDKAE RRGRHREGSR PARSGEGEAE GPDGGGGGGG ERRRRHRHGP
     PPAYDPDARR DDRERRHRRR KDTQGSGVPV SGPNLSTTRP IQQDLSRQEP PLAEDMDNLK
     NSRLATAEPV SPHENLSHAG LPQSPAKMGS STDPAGPTPA TAANPQNSTA SRRTPNNPGN
     PSNPGPPKTP ENSLIVTNPS TAQTNSAKTA RKPDHTTVEI PPACPPPLNH TVVQVNKNAN
     PDPLPKKEDE KKEEVDEGPG EDGPKPMPPY SSMFILSTTN PLRRLCHYIL NLRYFEMCIL
     MVIAMSSIAL AAEDPVQPNA PRNNVLRYFD YVFTGVFTFE MVIKMIDLGL VLHQGAYFRD
     LWNILDFIVV SGALVAFAFT GNSKGKDINT IKSLRVLRVL RPLKTIKRLP KLKAVFDCVV
     NSLKNVFNIL IVYMLFMFIF AVVAVQLFKG KFFHCTDESK EFEKDCRGKY LLYEKNEVKA
     RDREWKKYEF HYDNVLWALL TLFTVSTGEG WPQVLKHSVD ATFENQGPSP GYRMEMSIFY
     VVYFVVFPFF FVNIFVALII ITFQEQGDKM MEEYSLEKNE RACIDFAISA KPLTRHMPQN
     KQSFQYRMWQ FVVSPPFEYT IMAMIALNTI VLMMKFYGAS VAYDNALKVF NIVFTSLFSL
     ECLLKVLAFG ILNYFRDAWN IFDFVTVLGS ITDILVTEFG NNFINLSFLR LFRAARLIKL
     LRQGYTIRIL LWTFVQSFKA LPYVCLLIAM LFFIYAIIGM QVFGNIGIDM EDEDSDEDEF
     QITEHNNFRT FFQALMLLFR SATGEAWHNI MLSCLSGKPC DKNSGILTPE CGNEFAYFYF
     VSFIFLCSFL MLNLFVAVIM DNFEYLTRDS SILGPHHLDE YVRVWAEYDP AAWGRMLYRD
     MYAMLRHMPP PLGLGKNCPA RVAYKRLLRM DLPVADDNTV HFNSTLMALI RTALDIKIAK
     GGADKQQMDA ELRKEMMAIW PNLSQKTLDL LVTPHKSTDL TVGKIYAAMM IMEYYRQSKA
     KKLQAMREEQ NRTPLMFQRM EPPPDEGGAG QNALPSTQLD PAGGLMAHED GLKDSPSWVT
     QRAQEMFQKT GTWSPERAPP ADMADSQPKP QSVEMREMSQ DGYSDSEHCL PMEGQARAAS
     MPRLPAENQR RRGRPRGSDL STICDTSPMK RSASVLGPKA SRRLDDYSLE RVPPEENQRH
     HPRRRERAHR TSERSLGRYT DVDTGLGTDL SMTTQSGDLP SREREQERGR PKDRKHRPHH
     HHHHHHHPGR GPGRVSPGVS ARRRRRGPVA RVRPARAPAL AHARARARAP ARLLPELRLR
     RARRPRPRQR RRPRRRRGGG GRALRRAPGP REPLAQDSPG RGPSVCLARA ARPAGPQRLL
     PGPRTGQAPR ARLPQKPARS VQRERRGLVL SPPPPPPGEL APRAHPARTP RPGPGDSRSR
     RGGRRWTASA GKGGGGPRAS APSP
//
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