ID CNGA1_HUMAN Reviewed; 690 AA.
AC P29973; A8K7K6; J3KPZ2; Q16279; Q16485; Q4W5E3;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 10-MAY-2017, entry version 177.
DE RecName: Full=cGMP-gated cation channel alpha-1;
DE AltName: Full=Cyclic nucleotide-gated cation channel 1;
DE AltName: Full=Cyclic nucleotide-gated channel alpha-1;
DE Short=CNG channel alpha-1;
DE Short=CNG-1;
DE Short=CNG1;
DE AltName: Full=Cyclic nucleotide-gated channel, photoreceptor;
DE AltName: Full=Rod photoreceptor cGMP-gated channel subunit alpha;
GN Name=CNGA1; Synonyms=CNCG, CNCG1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=1372902;
RA Pittler S.J., Lee A.K., Altherr M.R., Howard T.A., Seldin M.F.,
RA Hurwitz R.L., Wasmuth J.J., Baehr W.;
RT "Primary structure and chromosomal localization of human and mouse rod
RT photoreceptor cGMP-gated cation channel.";
RL J. Biol. Chem. 267:6257-6262(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Retina;
RX PubMed=1379636;
RA Dhallan R.S., Macke J.P., Eddy R.L., Shows T.B., Reed R.R., Yau K.-W.,
RA Nathans J.;
RT "Human rod photoreceptor cGMP-gated channel: amino acid sequence, gene
RT structure, and functional expression.";
RL J. Neurosci. 12:3248-3256(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 317-577.
RX PubMed=7532814; DOI=10.1016/0028-3908(94)90027-2;
RA Distler M., Biel M., Flockerzi V., Hofmann F.;
RT "Expression of cyclic nucleotide-gated cation channels in non-sensory
RT tissues and cells.";
RL Neuropharmacology 33:1275-1282(1994).
RN [7]
RP VARIANT RP49 PHE-320, AND VARIANTS GLN-32 AND ASN-118.
RX PubMed=7479749; DOI=10.1073/pnas.92.22.10177;
RA Dryja T.P., Finn J.T., Peng Y.-W., McGee T.L., Berson E.L., Yau K.-W.;
RT "Mutations in the gene encoding the alpha subunit of the rod cGMP-
RT gated channel in autosomal recessive retinitis pigmentosa.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10177-10181(1995).
RN [8]
RP INVOLVEMENT IN RP49.
RX PubMed=15570217;
RA Zhang Q., Zulfiqar F., Riazuddin S.A., Xiao X., Ahmad Z.,
RA Riazuddin S., Hejtmancik J.F.;
RT "Autosomal recessive retinitis pigmentosa in a Pakistani family mapped
RT to CNGA1 with identification of a novel mutation.";
RL Mol. Vis. 10:884-889(2004).
CC -!- FUNCTION: Visual signal transduction is mediated by a G-protein
CC coupled cascade using cGMP as second messenger. This protein can
CC be activated by cyclic GMP which leads to an opening of the cation
CC channel and thereby causing a depolarization of rod
CC photoreceptors.
CC -!- SUBUNIT: Tetramer formed of three CNGA1 and one CNGB1 modulatory
CC subunits. {ECO:0000250}.
CC -!- INTERACTION:
CC Q5ICW4:GRB14 (xeno); NbExp=4; IntAct=EBI-8417095, EBI-7639273;
CC Q9JLM9:Grb14 (xeno); NbExp=2; IntAct=EBI-8417095, EBI-8347358;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P29973-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P29973-2; Sequence=VSP_047170;
CC Note=No experimental confirmation available.;
CC -!- TISSUE SPECIFICITY: Rod cells in the retina.
CC -!- DOMAIN: The C-terminal coiled-coil domain mediates
CC homotrimerization of CNGA subunits. {ECO:0000250}.
CC -!- DISEASE: Retinitis pigmentosa 49 (RP49) [MIM:613756]: A retinal
CC dystrophy belonging to the group of pigmentary retinopathies.
CC Retinitis pigmentosa is characterized by retinal pigment deposits
CC visible on fundus examination and primary loss of rod
CC photoreceptor cells followed by secondary loss of cone
CC photoreceptors. Patients typically have night vision blindness and
CC loss of midperipheral visual field. As their condition progresses,
CC they lose their far peripheral visual field and eventually central
CC vision as well. {ECO:0000269|PubMed:15570217,
CC ECO:0000269|PubMed:7479749}. Note=The disease is caused by
CC mutations affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel
CC (TC 1.A.1.5) family. CNGA1 subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB22778.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Mutations of the CNGA1 gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="http://www.retina-international.org/files/sci-news/cnga1mut.htm";
CC -----------------------------------------------------------------------
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DR EMBL; M84741; AAA52010.1; -; mRNA.
DR EMBL; S42457; AAB22778.1; ALT_INIT; mRNA.
DR EMBL; AK292021; BAF84710.1; -; mRNA.
DR EMBL; AC096749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107068; AAY40919.1; -; Genomic_DNA.
DR EMBL; CH471069; EAW93048.1; -; Genomic_DNA.
DR EMBL; S76062; AAD14206.1; -; Genomic_DNA.
DR CCDS; CCDS43226.1; -. [P29973-1]
DR CCDS; CCDS47050.1; -. [P29973-2]
DR PIR; A42161; A42161.
DR RefSeq; NP_000078.2; NM_000087.3. [P29973-1]
DR RefSeq; NP_001136036.1; NM_001142564.1. [P29973-2]
DR RefSeq; XP_011511925.1; XM_011513623.2. [P29973-1]
DR RefSeq; XP_016863201.1; XM_017007712.1. [P29973-1]
DR UniGene; Hs.1323; -.
DR ProteinModelPortal; P29973; -.
DR SMR; P29973; -.
DR BioGrid; 107659; 1.
DR IntAct; P29973; 2.
DR MINT; MINT-7004260; -.
DR STRING; 9606.ENSP00000384264; -.
DR GuidetoPHARMACOLOGY; 394; -.
DR TCDB; 1.A.1.5.3; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; P29973; -.
DR PhosphoSitePlus; P29973; -.
DR BioMuta; CNGA1; -.
DR DMDM; 239938910; -.
DR EPD; P29973; -.
DR PaxDb; P29973; -.
DR PeptideAtlas; P29973; -.
DR PRIDE; P29973; -.
DR DNASU; 1259; -.
DR Ensembl; ENST00000358519; ENSP00000351320; ENSG00000198515. [P29973-1]
DR Ensembl; ENST00000402813; ENSP00000384264; ENSG00000198515. [P29973-2]
DR Ensembl; ENST00000420489; ENSP00000389881; ENSG00000198515. [P29973-1]
DR Ensembl; ENST00000514170; ENSP00000426862; ENSG00000198515. [P29973-1]
DR Ensembl; ENST00000544810; ENSP00000443401; ENSG00000198515. [P29973-2]
DR GeneID; 1259; -.
DR KEGG; hsa:1259; -.
DR UCSC; uc003gxt.5; human. [P29973-1]
DR CTD; 1259; -.
DR DisGeNET; 1259; -.
DR GeneCards; CNGA1; -.
DR GeneReviews; CNGA1; -.
DR H-InvDB; HIX0031530; -.
DR H-InvDB; HIX0031590; -.
DR HGNC; HGNC:2148; CNGA1.
DR HPA; HPA076168; -.
DR MalaCards; CNGA1; -.
DR MIM; 123825; gene.
DR MIM; 613756; phenotype.
DR neXtProt; NX_P29973; -.
DR OpenTargets; ENSG00000198515; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA26658; -.
DR eggNOG; KOG0500; Eukaryota.
DR eggNOG; ENOG410YWWI; LUCA.
DR GeneTree; ENSGT00760000118772; -.
DR HOGENOM; HOG000007898; -.
DR HOVERGEN; HBG000281; -.
DR InParanoid; P29973; -.
DR KO; K04948; -.
DR OMA; YLEYWLI; -.
DR OrthoDB; EOG091G03EW; -.
DR PhylomeDB; P29973; -.
DR TreeFam; TF319048; -.
DR Reactome; R-HSA-2485179; Activation of the phototransduction cascade.
DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR GeneWiki; Cyclic_nucleotide-gated_channel_alpha_1; -.
DR GenomeRNAi; 1259; -.
DR PRO; PR:P29973; -.
DR Proteomes; UP000005640; Chromosome 4.
DR Bgee; ENSG00000198515; -.
DR CleanEx; HS_CNGA1; -.
DR ExpressionAtlas; P29973; baseline and differential.
DR Genevisible; P29973; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0005221; F:intracellular cyclic nucleotide activated cation channel activity; IEA:InterPro.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; TAS:Reactome.
DR GO; GO:0006810; P:transport; TAS:ProtInc.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR032406; CLZ_dom.
DR InterPro; IPR032945; CNGA1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR10217:SF608; PTHR10217:SF608; 1.
DR Pfam; PF16526; CLZ; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; cGMP; cGMP-binding; Coiled coil;
KW Complete proteome; Disease mutation; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane; Nucleotide-binding;
KW Polymorphism; Reference proteome; Retinitis pigmentosa;
KW Sensory transduction; Transmembrane; Transmembrane helix; Transport;
KW Vision.
FT CHAIN 1 690 cGMP-gated cation channel alpha-1.
FT /FTId=PRO_0000219308.
FT TOPO_DOM 1 164 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 165 185 Helical; Name=H1. {ECO:0000255}.
FT TOPO_DOM 186 198 Extracellular. {ECO:0000255}.
FT TRANSMEM 199 217 Helical; Name=H2. {ECO:0000255}.
FT TOPO_DOM 218 241 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 242 261 Helical; Name=H3. {ECO:0000255}.
FT TOPO_DOM 262 299 Extracellular. {ECO:0000255}.
FT TRANSMEM 300 322 Helical; Name=H4. {ECO:0000255}.
FT TOPO_DOM 323 374 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 375 394 Helical; Name=H5. {ECO:0000255}.
FT TOPO_DOM 395 478 Extracellular. {ECO:0000255}.
FT TRANSMEM 479 499 Helical; Name=H6. {ECO:0000255}.
FT TOPO_DOM 500 690 Cytoplasmic. {ECO:0000255}.
FT NP_BIND 487 609 cGMP. {ECO:0000255}.
FT COILED 623 666 {ECO:0000250}.
FT BINDING 546 546 cGMP. {ECO:0000255}.
FT BINDING 561 561 cGMP. {ECO:0000255}.
FT CARBOHYD 425 425 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT VAR_SEQ 1 1 M -> MESRSSPRLECSGAISAHCSLHLPDSSDFQLIFVFL
FT VEMGFHHVGQAGLELLISSDLPTSASQSAGITDM (in
FT isoform 2). {ECO:0000303|PubMed:1379636}.
FT /FTId=VSP_047170.
FT VARIANT 32 32 R -> Q (in dbSNP:rs76537883).
FT {ECO:0000269|PubMed:7479749}.
FT /FTId=VAR_009295.
FT VARIANT 118 118 D -> N (in dbSNP:rs28642966).
FT {ECO:0000269|PubMed:7479749}.
FT /FTId=VAR_009296.
FT VARIANT 122 122 N -> D (in dbSNP:rs28642966).
FT /FTId=VAR_047385.
FT VARIANT 320 320 S -> F (in RP49; dbSNP:rs62625014).
FT {ECO:0000269|PubMed:7479749}.
FT /FTId=VAR_009297.
FT CONFLICT 35 35 E -> V (in Ref. 3; BAF84710).
FT {ECO:0000305}.
FT CONFLICT 50 50 S -> Y (in Ref. 1; AAA52010).
FT {ECO:0000305}.
FT CONFLICT 89 89 L -> I (in Ref. 1; AAA52010).
FT {ECO:0000305}.
FT CONFLICT 150 151 EE -> HH (in Ref. 1; AAA52010).
FT {ECO:0000305}.
FT CONFLICT 209 209 I -> V (in Ref. 3; BAF84710).
FT {ECO:0000305}.
FT CONFLICT 543 543 Y -> T (in Ref. 1; AAA52010).
FT {ECO:0000305}.
FT CONFLICT 681 682 GA -> WS (in Ref. 1; AAA52010).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 479 603 ismart:cNMP [T]
FT MYHIT 479 585 iprf:CNMP_BINDING_3 [T]
FT MYHIT 506 522 ipat:CNMP_BINDING_1 [T]
FT MYHIT 595 664 ipfam:CLZ [T]
FT MYHIT 167 406 ipfam:Ion_trans [T]
FT MYHIT 498 587 ipfam:cNMP_binding [T]
FT MYHIT 544 567 ipat:CNMP_BINDING_2 [T]
SQ SEQUENCE 690 AA; 79586 MW; F1045A210FE33DC0 CRC64;
MKLSMKNNII NTQQSFVTMP NVIVPDIEKE IRRMENGACS SFSEDDDSAS TSEESENENP
HARGSFSYKS LRKGGPSQRE QYLPGAIALF NVNNSSNKDQ EPEEKKKKKK EKKSKSDDKN
ENKNDPEKKK KKKDKEKKKK EEKSKDKKEE EKKEVVVIDP SGNTYYNWLF CITLPVMYNW
TMVIARACFD ELQSDYLEYW LILDYVSDIV YLIDMFVRTR TGYLEQGLLV KEELKLINKY
KSNLQFKLDV LSLIPTDLLY FKLGWNYPEI RLNRLLRFSR MFEFFQRTET RTNYPNIFRI
SNLVMYIVII IHWNACVFYS ISKAIGFGND TWVYPDINDP EFGRLARKYV YSLYWSTLTL
TTIGETPPPV RDSEYVFVVV DFLIGVLIFA TIVGNIGSMI SNMNAARAEF QARIDAIKQY
MHFRNVSKDM EKRVIKWFDY LWTNKKTVDE KEVLKYLPDK LRAEIAINVH LDTLKKVRIF
ADCEAGLLVE LVLKLQPQVY SPGDYICKKG DIGREMYIIK EGKLAVVADD GVTQFVVLSD
GSYFGEISIL NIKGSKAGNR RTANIKSIGY SDLFCLSKDD LMEALTEYPD AKTMLEEKGK
QILMKDGLLD LNIANAGSDP KDLEEKVTRM EGSVDLLQTR FARILAEYES MQQKLKQRLT
KVEKFLKPLI DTEFSSIEGP GAESGPIDST
//
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