ID GNAL_HUMAN Reviewed; 381 AA. AC P38405; B7ZA26; Q86XU3; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 27-MAR-2024, entry version 205. DE RecName: Full=Guanine nucleotide-binding protein G(olf) subunit alpha; DE AltName: Full=Adenylate cyclase-stimulating G alpha protein, olfactory type; GN Name=GNAL; 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 1). RC TISSUE=Insulinoma; RX PubMed=8243272; DOI=10.1210/endo.133.6.8243272; RA Zigman J.M., Westermark G.T., Lamendola J., Boel E., Steiner D.F.; RT "Human G(olf) alpha: complementary deoxyribonucleic acid structure and RT expression in pancreatic islets and other tissues outside the olfactory RT neuroepithelium and central nervous system."; RL Endocrinology 133:2508-2514(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Vuoristo J.T., Berrettini W.H., Overhauser J., Prockop D.J., Ferraro T.N., RA Ala-Kokko L.; RT "The gene for the human G protein Golf alpha."; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Tongue; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16177791; DOI=10.1038/nature03983; RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J., RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.; RT "DNA sequence and analysis of human chromosome 18."; RL Nature 437:551-555(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction sequenced by RT the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [8] RP INTERACTION WITH GAS2L2. RX PubMed=23994616; DOI=10.1016/j.bbamcr.2013.08.009; RA Wu Y.C., Lai H.L., Chang W.C., Lin J.T., Liu Y.J., Chern Y.; RT "A novel Galphas-binding protein, Gas-2 like 2, facilitates the signaling RT of the A2A adenosine receptor."; RL Biochim. Biophys. Acta 1833:3145-3154(2013). RN [9] RP VARIANTS DYT25 102-PRO--VAL-104 DEL; MET-137 AND LYS-155, VARIANT PHE-16, RP AND CHARACTERIZATION OF VARIANTS DYT25 MET-137 AND LYS-155. RX PubMed=23222958; DOI=10.1038/ng.2496; RA Fuchs T., Saunders-Pullman R., Masuho I., Luciano M.S., Raymond D., RA Factor S., Lang A.E., Liang T.W., Trosch R.M., White S., Ainehsazan E., RA Herve D., Sharma N., Ehrlich M.E., Martemyanov K.A., Bressman S.B., RA Ozelius L.J.; RT "Mutations in GNAL cause primary torsion dystonia."; RL Nat. Genet. 45:88-92(2013). CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved CC as modulators or transducers in various transmembrane signaling CC systems. G(olf) alpha mediates signal transduction within the olfactory CC neuroepithelium and the basal ganglia. May be involved in some aspect CC of visual transduction, and in mediating the effect of one or more CC hormones/neurotransmitters. CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The CC alpha chain contains the guanine nucleotide binding site. Interacts CC with GAS2L2 (PubMed:23994616). {ECO:0000269|PubMed:23994616}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P38405-1; Sequence=Displayed; CC Name=2; CC IsoId=P38405-2; Sequence=VSP_043050; CC Name=3; CC IsoId=P38405-3; Sequence=VSP_045130; CC -!- TISSUE SPECIFICITY: Detected in olfactory neuroepithelium, brain, CC testis, and to a lower extent in retina, lung alveoli, spleen. Trace CC amounts where seen in kidney, adrenal gland and liver. Found to be CC expressed in all the insulinomas examined. CC -!- DISEASE: Dystonia 25 (DYT25) [MIM:615073]: A form of dystonia, a CC disorder defined by the presence of sustained involuntary muscle CC contraction, often leading to abnormal postures. DYT25 is an autosomal CC dominant neurologic disorder characterized by adult onset of focal CC dystonia, usually involving the neck. The dystonia most often CC progresses to involve other regions, particularly the face and CC laryngeal muscles, and less commonly the trunk and limbs. CC {ECO:0000269|PubMed:23222958}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L10665; AAC37535.1; -; mRNA. DR EMBL; U55184; AAD00085.1; -; Genomic_DNA. DR EMBL; U55180; AAD00085.1; JOINED; Genomic_DNA. DR EMBL; U55181; AAD00085.1; JOINED; Genomic_DNA. DR EMBL; U55182; AAD00085.1; JOINED; Genomic_DNA. DR EMBL; U55183; AAD00085.1; JOINED; Genomic_DNA. DR EMBL; AF493893; AAM12607.1; -; mRNA. DR EMBL; AK316141; BAH14512.1; -; mRNA. DR EMBL; AP001120; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP001269; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP005137; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471113; EAX01573.1; -; Genomic_DNA. DR EMBL; BC050021; AAH50021.1; -; mRNA. DR CCDS; CCDS11851.1; -. [P38405-2] DR CCDS; CCDS11852.1; -. [P38405-1] DR CCDS; CCDS58614.1; -. [P38405-3] DR PIR; I53271; I53271. DR RefSeq; NP_001135811.1; NM_001142339.2. [P38405-1] DR RefSeq; NP_001248372.1; NM_001261443.1. [P38405-1] DR RefSeq; NP_001248373.1; NM_001261444.1. [P38405-3] DR RefSeq; NP_892023.1; NM_182978.3. [P38405-2] DR PDB; 8EL8; EM; 3.20 A; A=1-381. DR PDB; 8KGK; EM; 3.16 A; B=7-14, B=191-197. DR PDB; 8KH4; EM; 3.10 A; B=7-14, B=191-197. DR PDBsum; 8EL8; -. DR PDBsum; 8KGK; -. DR PDBsum; 8KH4; -. DR AlphaFoldDB; P38405; -. DR EMDB; EMD-28224; -. DR EMDB; EMD-35761; -. DR SMR; P38405; -. DR BioGRID; 109036; 21. DR IntAct; P38405; 15. DR STRING; 9606.ENSP00000334051; -. DR iPTMnet; P38405; -. DR PhosphoSitePlus; P38405; -. DR SwissPalm; P38405; -. DR BioMuta; GNAL; -. DR DMDM; 585178; -. DR EPD; P38405; -. DR jPOST; P38405; -. DR MassIVE; P38405; -. DR MaxQB; P38405; -. DR PaxDb; 9606-ENSP00000334051; -. DR PeptideAtlas; P38405; -. DR ProteomicsDB; 55293; -. [P38405-1] DR ProteomicsDB; 55294; -. [P38405-2] DR ProteomicsDB; 7052; -. DR Antibodypedia; 4227; 214 antibodies from 27 providers. DR DNASU; 2774; -. DR Ensembl; ENST00000269162.9; ENSP00000269162.4; ENSG00000141404.17. [P38405-1] DR Ensembl; ENST00000334049.11; ENSP00000334051.5; ENSG00000141404.17. [P38405-2] DR Ensembl; ENST00000423027.8; ENSP00000408489.2; ENSG00000141404.17. [P38405-1] DR Ensembl; ENST00000535121.5; ENSP00000439023.1; ENSG00000141404.17. [P38405-1] DR Ensembl; ENST00000602628.1; ENSP00000473600.1; ENSG00000141404.17. [P38405-3] DR GeneID; 2774; -. DR KEGG; hsa:2774; -. DR MANE-Select; ENST00000334049.11; ENSP00000334051.5; NM_182978.4; NP_892023.1. [P38405-2] DR UCSC; uc002kqc.4; human. [P38405-1] DR AGR; HGNC:4388; -. DR CTD; 2774; -. DR DisGeNET; 2774; -. DR GeneCards; GNAL; -. DR GeneReviews; GNAL; -. DR HGNC; HGNC:4388; GNAL. DR HPA; ENSG00000141404; Tissue enhanced (brain). DR MalaCards; GNAL; -. DR MIM; 139312; gene. DR MIM; 615073; phenotype. DR neXtProt; NX_P38405; -. DR OpenTargets; ENSG00000141404; -. DR Orphanet; 329466; Autosomal dominant focal dystonia, DYT25 type. DR PharmGKB; PA28770; -. DR VEuPathDB; HostDB:ENSG00000141404; -. DR eggNOG; KOG0099; Eukaryota. DR GeneTree; ENSGT00940000155271; -. DR HOGENOM; CLU_014184_3_0_1; -. DR InParanoid; P38405; -. DR OMA; KEFFEHA; -. DR OrthoDB; 2897309at2759; -. DR PhylomeDB; P38405; -. DR TreeFam; TF300673; -. DR PathwayCommons; P38405; -. DR Reactome; R-HSA-170660; Adenylate cyclase activating pathway. DR Reactome; R-HSA-170670; Adenylate cyclase inhibitory pathway. DR Reactome; R-HSA-381753; Olfactory Signaling Pathway. DR SignaLink; P38405; -. DR SIGNOR; P38405; -. DR BioGRID-ORCS; 2774; 10 hits in 1150 CRISPR screens. DR ChiTaRS; GNAL; human. DR GeneWiki; GNAL; -. DR GenomeRNAi; 2774; -. DR Pharos; P38405; Tbio. DR PRO; PR:P38405; -. DR Proteomes; UP000005640; Chromosome 18. DR RNAct; P38405; Protein. DR Bgee; ENSG00000141404; Expressed in lateral globus pallidus and 195 other cell types or tissues. DR ExpressionAtlas; P38405; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central. DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd00066; G-alpha; 1. DR Gene3D; 1.10.400.10; GI Alpha 1, domain 2-like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR000367; Gprotein_alpha_S. DR InterPro; IPR001019; Gprotein_alpha_su. DR InterPro; IPR011025; GproteinA_insert. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1. DR PANTHER; PTHR10218:SF233; GUANINE NUCLEOTIDE-BINDING PROTEIN G(OLF) SUBUNIT ALPHA; 1. DR Pfam; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR PRINTS; PR00443; GPROTEINAS. DR SMART; SM00275; G_alpha; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1. DR PROSITE; PS51882; G_ALPHA; 1. DR Genevisible; P38405; HS. PE 1: Evidence at protein level; KW 3D-structure; ADP-ribosylation; Alternative splicing; Disease variant; KW Dystonia; GTP-binding; Lipoprotein; Magnesium; Metal-binding; KW Nucleotide-binding; Palmitate; Phosphoprotein; Reference proteome; KW Transducer. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..381 FT /note="Guanine nucleotide-binding protein G(olf) subunit FT alpha" FT /id="PRO_0000203732" FT DOMAIN 41..381 FT /note="G-alpha" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 44..57 FT /note="G1 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 183..191 FT /note="G2 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 206..215 FT /note="G3 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 275..282 FT /note="G4 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 351..356 FT /note="G5 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT BINDING 49..56 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 56 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 185..191 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 191 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 210..214 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 279..282 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 353 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT MOD_RES 178 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8CGK7" FT MOD_RES 188 FT /note="ADP-ribosylarginine; by cholera toxin" FT /evidence="ECO:0000250" FT LIPID 2 FT /note="N-palmitoyl glycine" FT /evidence="ECO:0000250|UniProtKB:P04896" FT LIPID 3 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT VAR_SEQ 1..207 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045130" FT VAR_SEQ 1..41 FT /note="MGCLGGNSKTTEDQGVDEKERREANKKIEKQLQKERLAYKA -> MGLCYSL FT RPLLFGGPGDDPCAASEPPVEDAQPAPAPALAPVRAAARDTARTLLPRGGEGSPACARP FT KADKPKEKRQRTEQLSAEEREAAKEREAVKEARKVSRGIDRMLRDQKRDLQQ (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043050" FT VARIANT 16 FT /note="V -> F (in dbSNP:rs1039372506)" FT /evidence="ECO:0000269|PubMed:23222958" FT /id="VAR_069329" FT VARIANT 102..104 FT /note="Missing (in DYT25)" FT /evidence="ECO:0000269|PubMed:23222958" FT /id="VAR_069330" FT VARIANT 137 FT /note="V -> M (in DYT25; loss of function mutation; FT dbSNP:rs398122923)" FT /evidence="ECO:0000269|PubMed:23222958" FT /id="VAR_069331" FT VARIANT 155 FT /note="E -> K (in DYT25; loss of function mutation; FT dbSNP:rs398122925)" FT /evidence="ECO:0000269|PubMed:23222958" FT /id="VAR_069332" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:8EL8" FT STRAND 208..210 FT /evidence="ECO:0007829|PDB:8EL8" FT STRAND 230..234 FT /evidence="ECO:0007829|PDB:8EL8" FT HELIX 252..264 FT /evidence="ECO:0007829|PDB:8EL8" FT STRAND 267..271 FT /evidence="ECO:0007829|PDB:8EL8" FT STRAND 273..278 FT /evidence="ECO:0007829|PDB:8EL8" FT HELIX 281..290 FT /evidence="ECO:0007829|PDB:8EL8" FT HELIX 295..297 FT /evidence="ECO:0007829|PDB:8EL8" FT HELIX 300..302 FT /evidence="ECO:0007829|PDB:8EL8" FT HELIX 319..337 FT /evidence="ECO:0007829|PDB:8EL8" FT TURN 341..343 FT /evidence="ECO:0007829|PDB:8EL8" FT STRAND 346..350 FT /evidence="ECO:0007829|PDB:8EL8" FT HELIX 365..377 FT /evidence="ECO:0007829|PDB:8EL8" SQ SEQUENCE 381 AA; 44308 MW; 9A73D2982FF9C9A3 CRC64; MGCLGGNSKT TEDQGVDEKE RREANKKIEK QLQKERLAYK ATHRLLLLGA GESGKSTIVK QMRILHVNGF NPEEKKQKIL DIRKNVKDAI VTIVSAMSTI IPPVPLANPE NQFRSDYIKS IAPITDFEYS QEFFDHVKKL WDDEGVKACF ERSNEYQLID CAQYFLERID SVSLVDYTPT DQDLLRCRVL TSGIFETRFQ VDKVNFHMFD VGGQRDERRK WIQCFNDVTA IIYVAACSSY NMVIREDNNT NRLRESLDLF ESIWNNRWLR TISIILFLNK QDMLAEKVLA GKSKIEDYFP EYANYTVPED ATPDAGEDPK VTRAKFFIRD LFLRISTATG DGKHYCYPHF TCAVDTENIR RVFNDCRDII QRMHLKQYEL L //