ANO2_HUMAN
ID ANO2_HUMAN Reviewed; 1003 AA.
AC Q9NQ90; C4N787; Q9H847;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Anoctamin-2;
DE AltName: Full=Transmembrane protein 16B;
GN Name=ANO2; Synonyms=C12orf3, TMEM16B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Retina;
RA Lorenz B., White K.E., Econs M.J., Strom T.M.;
RT "Transcripts in 12p13.3.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, GLYCOSYLATION, SUBUNIT,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=19474308; DOI=10.1523/jneurosci.5546-08.2009;
RA Stoehr H., Heisig J.B., Benz P.M., Schoeberl S., Milenkovic V.M.,
RA Strauss O., Aartsen W.M., Wijnholds J., Weber B.H.F., Schulz H.L.;
RT "TMEM16B, a novel protein with calcium-dependent chloride channel activity,
RT associates with a presynaptic protein complex in photoreceptor terminals.";
RL J. Neurosci. 29:6809-6818(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 556-999 (ISOFORMS 1/2).
RC TISSUE=Retinoblastoma;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20056604; DOI=10.1074/jbc.m109.065367;
RA Schreiber R., Uliyakina I., Kongsuphol P., Warth R., Mirza M.,
RA Martins J.R., Kunzelmann K.;
RT "Expression and function of epithelial anoctamins.";
RL J. Biol. Chem. 285:7838-7845(2010).
RN [6]
RP REVIEW.
RX PubMed=21642943; DOI=10.1038/aps.2011.48;
RA Duran C., Hartzell H.C.;
RT "Physiological roles and diseases of Tmem16/Anoctamin proteins: are they
RT all chloride channels?";
RL Acta Pharmacol. Sin. 32:685-692(2011).
RN [7]
RP REVIEW.
RX PubMed=21607626; DOI=10.1007/s00424-011-0975-9;
RA Kunzelmann K., Tian Y., Martins J.R., Faria D., Kongsuphol P.,
RA Ousingsawat J., Thevenod F., Roussa E., Rock J., Schreiber R.;
RT "Anoctamins.";
RL Pflugers Arch. 462:195-208(2011).
RN [8]
RP REVIEW.
RX PubMed=22302790; DOI=10.1113/expphysiol.2011.058214;
RA Winpenny J.P., Gray M.A.;
RT "The anoctamin (TMEM16) gene family: calcium-activated chloride channels
RT come of age.";
RL Exp. Physiol. 97:175-176(2012).
RN [9]
RP REVIEW, AND FUNCTION.
RX PubMed=21984732; DOI=10.1113/expphysiol.2011.058198;
RA Scudieri P., Sondo E., Ferrera L., Galietta L.J.;
RT "The anoctamin family: TMEM16A and TMEM16B as calcium-activated chloride
RT channels.";
RL Exp. Physiol. 97:177-183(2012).
RN [10]
RP REVIEW, AND FUNCTION.
RX PubMed=21890523; DOI=10.1113/expphysiol.2011.058230;
RA Pifferi S., Cenedese V., Menini A.;
RT "Anoctamin 2/TMEM16B: a calcium-activated chloride channel in olfactory
RT transduction.";
RL Exp. Physiol. 97:193-199(2012).
CC -!- FUNCTION: Calcium-activated chloride channel (CaCC) which may play a
CC role in olfactory signal transduction. Odorant molecules bind to odor-
CC sensing receptors (OSRs), leading to an increase in calcium entry that
CC activates CaCC current which amplifies the depolarization of the OSR
CC cells, ANO2 seems to be the underlying chloride channel involved in
CC this process. May mediate light perception amplification in retina.
CC {ECO:0000269|PubMed:19474308, ECO:0000269|PubMed:20056604,
CC ECO:0000269|PubMed:21890523, ECO:0000269|PubMed:21984732}.
CC -!- ACTIVITY REGULATION: Channel activity is repressed by chloride
CC inhibitors; strongly by niflumic acid (NFA), partially by flufenamic
CC acid (FFA), and only slightly by meclofenamic acid (MFA), 5-Nitro-2-(3-
CC phenylpropylamino)benzoic acid (NPPB), 4-acetamido-4'-isothiocyanato-
CC stilben-2,2'-disulfonate (SITS), and 4,4'-diisothiocyanatostilbene-
CC 2,2'-disulfonic acid (DIDS). {ECO:0000250}.
CC -!- SUBUNIT: Component of a presynaptic protein complex recruited to
CC specialized plasma membrane domains of photoreceptors. Interacts with
CC DLG4 by its C-terminal region (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9NQ90; Q12959: DLG1; NbExp=2; IntAct=EBI-20731422, EBI-357481;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20056604};
CC Multi-pass membrane protein {ECO:0000269|PubMed:20056604}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NQ90-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQ90-2; Sequence=VSP_040493, VSP_040494;
CC -!- TISSUE SPECIFICITY: Retina, especially in the photoreceptor synaptic
CC terminals. {ECO:0000269|PubMed:19474308}.
CC -!- MISCELLANEOUS: The term 'anoctamin' was coined because these channels
CC are anion selective and have eight (OCT) transmembrane segments. There
CC is some dissatisfaction in the field with the Ano nomenclature because
CC it is not certain that all the members of this family are anion
CC channels or have the 8-transmembrane topology.
CC -!- MISCELLANEOUS: [Isoform 1]: Splice site between exons 4 and 5 is non-
CC canonical.
CC -!- MISCELLANEOUS: [Isoform 2]: Splice site between exons 4 and 5 is non-
CC canonical. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the anoctamin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14773.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ272204; CAC01125.1; -; mRNA.
DR EMBL; FJ384095; ACL36050.1; -; mRNA.
DR EMBL; AC006431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC137627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK024010; BAB14773.1; ALT_INIT; mRNA.
DR CCDS; CCDS44807.2; -. [Q9NQ90-2]
DR RefSeq; NP_001265525.1; NM_001278596.1. [Q9NQ90-1]
DR RefSeq; NP_001265526.1; NM_001278597.1. [Q9NQ90-2]
DR AlphaFoldDB; Q9NQ90; -.
DR SMR; Q9NQ90; -.
DR BioGRID; 121367; 2.
DR IntAct; Q9NQ90; 1.
DR STRING; 9606.ENSP00000348453; -.
DR BindingDB; Q9NQ90; -.
DR ChEMBL; CHEMBL4105767; -.
DR TCDB; 1.A.17.1.3; the calcium-dependent chloride channel (ca-clc) family.
DR GlyGen; Q9NQ90; 4 sites.
DR iPTMnet; Q9NQ90; -.
DR PhosphoSitePlus; Q9NQ90; -.
DR BioMuta; ANO2; -.
DR DMDM; 262527528; -.
DR MassIVE; Q9NQ90; -.
DR PaxDb; Q9NQ90; -.
DR PeptideAtlas; Q9NQ90; -.
DR PRIDE; Q9NQ90; -.
DR ProteomicsDB; 82108; -. [Q9NQ90-1]
DR ProteomicsDB; 82109; -. [Q9NQ90-2]
DR Antibodypedia; 41841; 137 antibodies from 28 providers.
DR DNASU; 57101; -.
DR Ensembl; ENST00000327087.12; ENSP00000314048.9; ENSG00000047617.17. [Q9NQ90-2]
DR Ensembl; ENST00000356134.9; ENSP00000348453.5; ENSG00000047617.17. [Q9NQ90-2]
DR Ensembl; ENST00000650848.1; ENSP00000498903.1; ENSG00000047617.17. [Q9NQ90-1]
DR GeneID; 57101; -.
DR KEGG; hsa:57101; -.
DR UCSC; uc058kbk.1; human. [Q9NQ90-1]
DR CTD; 57101; -.
DR DisGeNET; 57101; -.
DR GeneCards; ANO2; -.
DR HGNC; HGNC:1183; ANO2.
DR HPA; ENSG00000047617; Tissue enriched (retina).
DR MIM; 610109; gene.
DR neXtProt; NX_Q9NQ90; -.
DR OpenTargets; ENSG00000047617; -.
DR PharmGKB; PA25504; -.
DR VEuPathDB; HostDB:ENSG00000047617; -.
DR eggNOG; KOG2514; Eukaryota.
DR GeneTree; ENSGT00940000155840; -.
DR HOGENOM; CLU_006685_1_2_1; -.
DR InParanoid; Q9NQ90; -.
DR PhylomeDB; Q9NQ90; -.
DR TreeFam; TF314265; -.
DR PathwayCommons; Q9NQ90; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR Reactome; R-HSA-381753; Olfactory Signaling Pathway.
DR SignaLink; Q9NQ90; -.
DR BioGRID-ORCS; 57101; 5 hits in 240 CRISPR screens.
DR ChiTaRS; ANO2; human.
DR GenomeRNAi; 57101; -.
DR Pharos; Q9NQ90; Tchem.
DR PRO; PR:Q9NQ90; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9NQ90; protein.
DR Bgee; ENSG00000047617; Expressed in sural nerve and 93 other tissues.
DR ExpressionAtlas; Q9NQ90; baseline and differential.
DR Genevisible; Q9NQ90; HS.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005254; F:chloride channel activity; IBA:GO_Central.
DR GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR032394; Anoct_dimer.
DR InterPro; IPR007632; Anoctamin.
DR InterPro; IPR031288; Anoctamin-2.
DR PANTHER; PTHR12308; PTHR12308; 1.
DR PANTHER; PTHR12308:SF20; PTHR12308:SF20; 1.
DR Pfam; PF16178; Anoct_dimer; 1.
DR Pfam; PF04547; Anoctamin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Chloride; Chloride channel;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1003
FT /note="Anoctamin-2"
FT /id="PRO_0000072564"
FT TOPO_DOM 1..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..434
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..559
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 560..582
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604..623
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 624..644
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 645..748
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 749..769
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 770..801
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 802..822
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 823..907
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 908..928
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 929..1003
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1001..1003
FT /note="DLG4 binding (PDZ)"
FT COMPBIAS 978..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 841
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 849
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 856
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..4
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_040493"
FT VAR_SEQ 5..7
FT /note="GPR -> MPE (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_040494"
FT VARIANT 112
FT /note="V -> A (in dbSNP:rs3741903)"
FT /id="VAR_021932"
FT VARIANT 147
FT /note="P -> S (in dbSNP:rs3741901)"
FT /id="VAR_057286"
FT VARIANT 401
FT /note="M -> I (in dbSNP:rs17788563)"
FT /id="VAR_061853"
FT VARIANT 505
FT /note="S -> A (in dbSNP:rs1860961)"
FT /id="VAR_020331"
SQ SEQUENCE 1003 AA; 113969 MW; 32939EADC8AFE5C8 CRC64;
MATPGPRDIP LLPGSPRRLS PQAGSRGGQG PKHGQQCLKM PGPRAPGLQG GSNRDPGQPC
GGESTRSSSV INNYLDANEP VSLEARLSRM HFHDSQRKVD YVLAYHYRKR GVHLAQGFPG
HSLAIVSNGE TGKEPHAGGP GDIELGPLDA LEEERKEQRE EFEHNLMEAG LELEKDLENK
SQGSIFVRIH APWQVLAREA EFLKIKVPTK KEMYEIKAGG SIAKKFSAAL QKLSSHLQPR
VPEHSNNKMK NLSYPFSREK MYLYNIQEKD TFFDNATRSR IVHEILKRTA CSRANNTMGI
NSLIANNIYE AAYPLHDGEY DSPEDDMNDR KLLYQEWARY GVFYKFQPID LIRKYFGEKI
GLYFAWLGLY TSFLIPSSVI GVIVFLYGCA TIEEDIPSRE MCDQQNAFTM CPLCDKSCDY
WNLSSACGTA QASHLFDNPA TVFFSIFMAL WATMFLENWK RLQMRLGYFW DLTGIEEEEE
RAQEHSRPEY ETKVREKMLK ESNQSAVQKL ETNTTECGDE DDEDKLTWKD RFPGYLMNFA
SILFMIALTF SIVFGVIVYR ITTAAALSLN KATRSNVRVT VTATAVIINL VVILILDEIY
GAVAKWLTKI EVPKTEQTFE ERLILKAFLL KFVNAYSPIF YVAFFKGRFV GRPGSYVYVF
DGYRMEECAP GGCLMELCIQ LSIIMLGKQL IQNNIFEIGV PKLKKLFRKL KDETEAGETD
SAHSKHPEQW DLDYSLEPYT GLTPEYMEMI IQFGFVTLFV ASFPLAPVFA LLNNVIEVRL
DAKKFVTELR RPDAVRTKDI GIWFDILSGI GKFSVISNAF VIAITSDFIP RLVYQYSYSH
NGTLHGFVNH TLSFFNVSQL KEGTQPENSQ FDQEVQFCRF KDYREPPWAP NPYEFSKQYW
FILSARLAFV IIFQNLVMFL SVLVDWMIPD IPTDISDQIK KEKSLLVDFF LKEEHEKLKL
MDEPALRSPG GGDRSRSRAA SSAPSGQSQL GSMMSSGSQH TNV
