CAC1D_CHICK
ID CAC1D_CHICK Reviewed; 2190 AA.
AC O73700; O73701; O73702; O73703; O73704;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1D;
DE AltName: Full=CHCACHA1D;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.3;
GN Name=CACNA1D;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 5 AND 6).
RC TISSUE=Brain;
RX PubMed=9405708; DOI=10.1073/pnas.94.26.14883;
RA Kollmar R., Montgomery L.G., Fak J., Henry L.J., Hudspeth A.J.;
RT "Predominance of the alpha1D subunit in L-type voltage-gated Ca2+ channels
RT of hair cells in the chicken's cochlea.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14883-14888(1997).
RN [2]
RP ALTERNATIVE SPLICING.
RX PubMed=9405709; DOI=10.1073/pnas.94.26.14889;
RA Kollmar R., Fak J., Montgomery L.G., Hudspeth A.J.;
RT "Hair cell-specific splicing of mRNA for the alpha1D subunit of voltage-
RT gated Ca2+ channels in the chicken's cochlea.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14889-14893(1997).
CC -!- FUNCTION: The isoform alpha-1D gives rise to L-type calcium currents.
CC Long-lasting (L-type) calcium channels belong to the 'high-voltage
CC activated' (HVA) group.
CC -!- SUBUNIT: Voltage-dependent calcium channels are multisubunit complexes,
CC consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1
CC ratio. The channel activity is directed by the pore-forming and
CC voltage-sensitive alpha-1 subunit. In many cases, this subunit is
CC sufficient to generate voltage-sensitive calcium channel activity. The
CC auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge
CC regulate the channel activity (By similarity). Interacts with RIMBP2.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=O73700-1; Sequence=Displayed;
CC Name=2; Synonyms=IIIS2;
CC IsoId=O73700-2; Sequence=VSP_000928;
CC Name=3; Synonyms=IVS3;
CC IsoId=O73700-3; Sequence=VSP_000930;
CC Name=4; Synonyms=IVS2-IVS3;
CC IsoId=O73700-4; Sequence=VSP_000929;
CC Name=5; Synonyms=PSE29-31-2;
CC IsoId=O73700-5; Sequence=VSP_000931, VSP_000932;
CC Name=6; Synonyms=PSE29-31-1;
CC IsoId=O73700-6; Sequence=VSP_000933, VSP_000934;
CC Name=7; Synonyms=PSE48, 154-1;
CC IsoId=O73700-7; Sequence=VSP_000935, VSP_000936;
CC Name=8; Synonyms=I-II-loop;
CC IsoId=O73700-8; Sequence=VSP_000927;
CC -!- TISSUE SPECIFICITY: Expressed in the basilar papilla of the cochlea.
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 -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1D subfamily. {ECO:0000305}.
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DR EMBL; AF027602; AAC08304.1; -; mRNA.
DR EMBL; AF027603; AAC08305.1; -; mRNA.
DR EMBL; AF027604; AAC08306.1; -; mRNA.
DR EMBL; AF027605; AAC08307.1; -; mRNA.
DR EMBL; AF027606; AAC08308.1; -; mRNA.
DR RefSeq; NP_990365.1; NM_205034.2. [O73700-1]
DR AlphaFoldDB; O73700; -.
DR SMR; O73700; -.
DR STRING; 9031.ENSGALP00000035486; -.
DR PaxDb; O73700; -.
DR PRIDE; O73700; -.
DR Ensembl; ENSGALT00000036264; ENSGALP00000035486; ENSGALG00000005332. [O73700-1]
DR Ensembl; ENSGALT00000055249; ENSGALP00000043621; ENSGALG00000005332. [O73700-5]
DR Ensembl; ENSGALT00000073762; ENSGALP00000043479; ENSGALG00000005332. [O73700-3]
DR Ensembl; ENSGALT00000099292; ENSGALP00000070410; ENSGALG00000005332. [O73700-7]
DR GeneID; 395895; -.
DR KEGG; gga:395895; -.
DR CTD; 776; -.
DR VEuPathDB; HostDB:geneid_395895; -.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000154839; -.
DR InParanoid; O73700; -.
DR OMA; YEIADAC; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; O73700; -.
DR Reactome; R-GGA-422356; Regulation of insulin secretion.
DR PRO; PR:O73700; -.
DR Proteomes; UP000000539; Chromosome 12.
DR Bgee; ENSGALG00000005332; Expressed in brain and 6 other tissues.
DR ExpressionAtlas; O73700; baseline and differential.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IBA:GO_Central.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR031688; CAC1F_C.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR005452; LVDCC_a1dsu.
DR InterPro; IPR014873; VDCC_a1su_IQ.
DR InterPro; IPR005446; VDCC_L_a1su.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16885; CAC1F_C; 2.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01630; LVDCCALPHA1.
DR PRINTS; PR01636; LVDCCALPHA1D.
DR SMART; SM01062; Ca_chan_IQ; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..2190
FT /note="Voltage-dependent L-type calcium channel subunit
FT alpha-1D"
FT /id="PRO_0000053937"
FT TOPO_DOM 1..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..140
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..158
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..178
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..209
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..249
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..288
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..376
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..401
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..544
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..564
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..579
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 580..598
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..606
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 607..625
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..635
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..654
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 655..673
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 674..694
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 695..748
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 749..773
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 774..907
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 908..926
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 927..942
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 943..962
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 963..974
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 975..993
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 994..999
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1000..1019
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1020..1038
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1039..1058
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1059..1148
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1149..1169
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1170..1226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1227..1245
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1246..1260
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1261..1280
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1281..1297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1298..1319
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1320..1342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1343..1362
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1363..1381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1382..1401
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1402..1468
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1469..1493
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1494..2190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 108..404
FT /note="I"
FT REPEAT 530..776
FT /note="II"
FT REPEAT 894..1176
FT /note="III"
FT REPEAT 1213..1496
FT /note="IV"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..441
FT /note="Binding to the beta subunit"
FT /evidence="ECO:0000250"
FT REGION 478..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1186
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250"
FT REGION 1449..1515
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250"
FT REGION 1461..1504
FT /note="Phenylalkylamine binding"
FT /evidence="ECO:0000250"
FT REGION 1736..1787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1803..1833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1917..1952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1995..2025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..859
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1917..1937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 359
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 726
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 1122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 459..484
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_000927"
FT VAR_SEQ 939..958
FT /note="ILGYADYVFTSMFTFEIILK -> ILGYFDYAFTAIFTVEILLK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:9405708"
FT /id="VSP_000928"
FT VAR_SEQ 1284..1293
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_000929"
FT VAR_SEQ 1294..1321
FT /note="GYFSDAWNTFDSLIVIGSIVDVVLSEAD -> HYFTDAWNTFDALIVVGSVV
FT DIAITEVN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9405708"
FT /id="VSP_000930"
FT VAR_SEQ 1671..1705
FT /note="AGLRTLHDIGPEIRRAISCDLQDDEPEENNPDEEE -> VLIAHTAQTPFCS
FT PASKLFPFGAEAWLQRAAGVA (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9405708"
FT /id="VSP_000931"
FT VAR_SEQ 1706..2190
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9405708"
FT /id="VSP_000932"
FT VAR_SEQ 1710..1728
FT /note="RNGALFGNHINHISSDRRD -> VMSEHGYVIFLLCNMSFIE (in
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:9405708"
FT /id="VSP_000933"
FT VAR_SEQ 1729..2190
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:9405708"
FT /id="VSP_000934"
FT VAR_SEQ 1892..1894
FT /note="HVY -> NGP (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_000935"
FT VAR_SEQ 1895..2190
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_000936"
SQ SEQUENCE 2190 AA; 249344 MW; 10680C1CB7708651 CRC64;
MQHHQQQQPE QHPEEANYAS STRIPLPGDG PTTQSNSSAP SKQTVLSWQA AIDAARQAKA
AQNMNTTTAQ PVGSLSQRKR QQYAKSKKQG NTSNSRPPRA LFCLSLNNPI RRACISLVEW
KPFDIFILLS IFANCVALAV YIPFPEDDSN STNHNLEKVE YAFLIIFTVE TFLKIIAYGL
LLHPNAYVRN GWNLLDFVIV VVGLFSVILE QLTKETEGGS HSGGKPGGFD VKALRAFRVL
RPLRLVSGVP SLQVVLNSII KAMVPLLHIA LLVLFVIIIY AIIGLELFIG KMHKSCFLID
SDILVEEDPA PCAFSGNGRQ CVMNGTECKG GWVGPNGGIT NFDNFAFAML TVFQCITMEG
WTDVLYWVND AIGCEWPWIY FVSLIILGSF FVLNLVLGVL SGEFSKEREK AKARGDFQKL
REKQQLEEDL KGYLDWITQA EDIDPENDEE ADEEGKRNRV TLADLMEEKK KSRLSCFGRS
SNKHASMPTS ETESVNTENV SGEGENPACC GSLCQTISKS KFSRRWRRWN RFNRRKCRAA
VKSVTFYWLV IVLVFLNTLT ISSEHYNQPD WLTQIQDIAN KVLLALFTCE MLVKMYSLGL
QAYFVSLFNR FDCFVVCGGI VETILVELEI MSPLGISVFR CVRLLRIFKV TRHWASLSNL
VASLLNSMKS IASLLLLLFL FIIIFSLLGM QLFGGKFNFD ETQTKRSTFD NFPQALLTVF
QILTGEDWNA VMYDGIMAYG GPSSSGMIVC IYFIILFICG NYILLNVFLA IAVDNLADAE
SLNTAQKEEA EEKERKKNAR KESLENKKSE KSEGDQKKPK DSKVTIAEYG EGEDEDKDPY
PPCDVPVGED EEDEEDEPEV PAGPRPRRIS ELNMKEKITP IPEGSAFFIF SSTNPIRVGC
HRLINHHIFT NLILVFIMLS SVSLAAEDPI RSHSFRNNIL GYADYVFTSM FTFEIILKMT
AFGAFLHKGS FCRNYFNLLD LLVVGVSLVS FGIQSSAISV VKILRVLRVL RPLRAINRAK
GLKHVVQCVF VAIRTIGNIM IVTTLLQFMF ACIGVQLFKG KFYKCTDEAK QNPEECRGIY
IVYKDGDVDN PMVKERVWQN SDFNFDNVLS AMMALFTVST FEGWPALLYK AIDSNGENVG
PVYNYRVEIS IFFIIYIIII AFFMMNIFVG FVIVTFQEQG EQEYKNCELD KNQRQCVEYA
LKARPLRRYI PKNPYQYKFW YVVNSTGFEY IMFVLIMLNT LCLAMQHYGQ SKLFNDAMDI
MNMVFTGVFT VEMVLKLIAF KPKIFVRKKE RWLGYFSDAW NTFDSLIVIG SIVDVVLSEA
DPKPTETVTT DESGNSEDSA RISITFFRLF RVMRLVKLLS RGEGIRTLLW TFIKSFQALP
YVALLIAMLF FIYAVIGMQV FGKVAMRDNN QINRNNNFQT FPQAVLLLFR CATGEAWQEI
MLACLPGKRC DPESDYNPGE EYTCGSNFAI IYFISFYMLC AFLIINLFVA VIMDNFDYLT
RDWSILGPHH LDEFKRIWSE YDPEAKGRIK HLDVVTLLRR IQPPLGFGKL CPHRVACKRL
VAMNMPLNSD GTVMFNATLF ALVRTALKIK TEGNLEQANE ELRAVIKKIW KKTSMKLLDQ
VVPPAGDDEV TVGKFYATFL IQDYFRKFKK RKEQGLVGKY PAKNTTIALQ AGLRTLHDIG
PEIRRAISCD LQDDEPEENN PDEEEEVYKR NGALFGNHIN HISSDRRDSF QQINTTHRPL
HVQRPSIPSA SDTEKNIYPH TGNSVYHNHH NHNSVGKQVP NSTNANLNNA NVSKVVHGKH
ANFGSHEHRS ENGYHSYSRA DHEKRRRPSS RRTRYYETYI RSDSGDGRRP TICREERDIR
DYCNDDHYLG EQEYYSGEEY YEEDSMLSGN RHVYDYHCRH HCHDSDFERP KGYHHPHGFF
EEDDSQTCYD TKRSPRRRLL PPTPASNRRS SFNFECLRRQ SSQDDIPLSP NFHHRTALPL
HLMQQQVMAV AGLDSSKAHK HSPSRSTRSW ATPPATPPNR DHTPYYTPLI QVDRAESTEH
MNGSLPSLHR SSWYTDDPDI SYRTFTPANL TVPNDFRHKH SDKQRSADSL VEAVLISEGL
GRYAKDPKFV SATKHEIADA CDMTIDEMES AASNLLNGNI SNGTNGDMFP ILSRQDYELQ
DFGPGYSDEE PEPGRYEEDL ADEMICITSL
