ID DOC2A_HUMAN Reviewed; 400 AA. AC Q14183; B4DEJ2; H3BNH6; Q6P4G4; Q7Z5G0; Q8IVX0; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 5. DT 24-JAN-2024, entry version 186. DE RecName: Full=Double C2-like domain-containing protein alpha; DE Short=Doc2; DE Short=Doc2-alpha; GN Name=DOC2A; 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), VARIANT SER-48, AND TISSUE RP SPECIFICITY. RC TISSUE=Brain; RX PubMed=7826360; DOI=10.1006/bbrc.1995.1062; RA Orita S., Sasaki T., Naito A., Maeda M., Igarashi H., Takai Y.; RT "Doc2, a novel synaptic vesicle protein with two repeated C2-like RT domains."; RL Biochem. Biophys. Res. Commun. 206:439-448(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Cerebellum; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-48. RC TISSUE=Brain, and Mammary gland; 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 [5] RP TISSUE SPECIFICITY. RX PubMed=8554557; DOI=10.1006/bbrc.1995.2876; RA Sakaguchi G., Orita S., Maeda M., Igarashi H., Takai Y.; RT "Molecular cloning of an isoform of Doc2 having two C2-like domains."; RL Biochem. Biophys. Res. Commun. 217:1053-1061(1995). RN [6] RP FUNCTION, AND INTERACTION WITH UNC13A. RX PubMed=9736751; DOI=10.1073/pnas.95.19.11418; RA Mochida S., Orita S., Sakaguchi G., Sasaki T., Takai Y.; RT "Role of the Doc2 alpha-Munc13-1 interaction in the neurotransmitter RT release process."; RL Proc. Natl. Acad. Sci. U.S.A. 95:11418-11422(1998). RN [7] RP FUNCTION, AND INTERACTION WITH DYNLT1. RX PubMed=9804756; DOI=10.1074/jbc.273.46.30065; RA Nagano F., Orita S., Sasaki T., Naito A., Sakaguchi G., Maeda M., RA Watanabe T., Kominami E., Uchiyama Y., Takai Y.; RT "Interaction of Doc2 with tctex-1, a light chain of cytoplasmic dynein. RT Implication in dynein-dependent vesicle transport."; RL J. Biol. Chem. 273:30065-30068(1998). RN [8] RP FUNCTION, AND INTERACTION WITH UNC13D. RX PubMed=18354201; DOI=10.4049/jimmunol.180.7.4774; RA Higashio H., Nishimura N., Ishizaki H., Miyoshi J., Orita S., Sakane A., RA Sasaki T.; RT "Doc2 alpha and Munc13-4 regulate Ca(2+) -dependent secretory lysosome RT exocytosis in mast cells."; RL J. Immunol. 180:4774-4784(2008). CC -!- FUNCTION: Calcium sensor which most probably regulates fusion of CC vesicles with membranes. Binds calcium and phospholipids. May be CC involved in calcium dependent neurotransmitter release through the CC interaction with UNC13A. May be involved in calcium-dependent CC spontaneous release of neurotransmitter in absence of action potentials CC in neuronal cells. Regulates Ca(2+)-dependent secretory lysosome CC exocytosis in mast cells. {ECO:0000269|PubMed:18354201, CC ECO:0000269|PubMed:9736751, ECO:0000269|PubMed:9804756}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00041}; CC -!- SUBUNIT: Interacts (via N-terminus) with UNC13A. Interacts with CC cytoplasmic dynein light chain DYNLT1. Interacts with UNC13D. CC {ECO:0000269|PubMed:18354201, ECO:0000269|PubMed:9736751, CC ECO:0000269|PubMed:9804756}. CC -!- INTERACTION: CC Q14183; Q8TF42: UBASH3B; NbExp=5; IntAct=EBI-20861623, EBI-1380492; CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. Cytoplasmic vesicle, CC secretory vesicle, synaptic vesicle membrane {ECO:0000305}; Peripheral CC membrane protein {ECO:0000305}. Synapse, synaptosome. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q14183-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14183-2; Sequence=VSP_056977, VSP_056978, VSP_056979; CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain. Also expressed in CC testis. {ECO:0000269|PubMed:7826360, ECO:0000269|PubMed:8554557}. CC -!- DOMAIN: C2 domain 1 is involved in binding calcium and phospholipids. CC {ECO:0000250}. 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; D31897; BAA06695.1; -; mRNA. DR EMBL; AK293651; BAG57103.1; -; mRNA. DR EMBL; AC093512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC041769; AAH41769.2; -; mRNA. DR EMBL; BC055284; AAH55284.1; -; mRNA. DR EMBL; BC063436; AAH63436.1; -; mRNA. DR CCDS; CCDS10666.1; -. [Q14183-1] DR PIR; JC2473; JC2473. DR RefSeq; NP_001268991.1; NM_001282062.1. [Q14183-1] DR RefSeq; NP_001268992.1; NM_001282063.1. [Q14183-1] DR RefSeq; NP_001268997.1; NM_001282068.1. [Q14183-1] DR RefSeq; NP_003577.2; NM_003586.2. [Q14183-1] DR RefSeq; XP_011544277.1; XM_011545975.1. DR RefSeq; XP_016879265.1; XM_017023776.1. DR RefSeq; XP_016879266.1; XM_017023777.1. DR PDB; 4MJJ; X-ray; 2.00 A; A=81-217. DR PDBsum; 4MJJ; -. DR AlphaFoldDB; Q14183; -. DR SMR; Q14183; -. DR BioGRID; 114026; 15. DR IntAct; Q14183; 9. DR STRING; 9606.ENSP00000482870; -. DR iPTMnet; Q14183; -. DR PhosphoSitePlus; Q14183; -. DR SwissPalm; Q14183; -. DR BioMuta; DOC2A; -. DR DMDM; 150421541; -. DR jPOST; Q14183; -. DR MassIVE; Q14183; -. DR MaxQB; Q14183; -. DR PaxDb; 9606-ENSP00000340017; -. DR PeptideAtlas; Q14183; -. DR ProteomicsDB; 3964; -. DR ProteomicsDB; 59901; -. [Q14183-1] DR Antibodypedia; 26947; 155 antibodies from 24 providers. DR DNASU; 8448; -. DR Ensembl; ENST00000350119.9; ENSP00000340017.4; ENSG00000149927.18. [Q14183-1] DR Ensembl; ENST00000564944.5; ENSP00000455196.1; ENSG00000149927.18. [Q14183-1] DR Ensembl; ENST00000564979.5; ENSP00000455624.1; ENSG00000149927.18. [Q14183-1] DR Ensembl; ENST00000566310.5; ENSP00000454857.1; ENSG00000149927.18. [Q14183-2] DR Ensembl; ENST00000616445.4; ENSP00000482870.1; ENSG00000149927.18. [Q14183-1] DR GeneID; 8448; -. DR KEGG; hsa:8448; -. DR MANE-Select; ENST00000350119.9; ENSP00000340017.4; NM_003586.3; NP_003577.2. DR UCSC; uc002dvn.4; human. [Q14183-1] DR AGR; HGNC:2985; -. DR CTD; 8448; -. DR DisGeNET; 8448; -. DR GeneCards; DOC2A; -. DR HGNC; HGNC:2985; DOC2A. DR HPA; ENSG00000149927; Group enriched (brain, testis). DR MIM; 604567; gene. DR neXtProt; NX_Q14183; -. DR OpenTargets; ENSG00000149927; -. DR PharmGKB; PA27451; -. DR VEuPathDB; HostDB:ENSG00000149927; -. DR eggNOG; KOG1013; Eukaryota. DR GeneTree; ENSGT00940000159141; -. DR HOGENOM; CLU_023008_3_0_1; -. DR InParanoid; Q14183; -. DR OMA; SPMTVRK; -. DR OrthoDB; 590187at2759; -. DR PhylomeDB; Q14183; -. DR TreeFam; TF351844; -. DR PathwayCommons; Q14183; -. DR SignaLink; Q14183; -. DR BioGRID-ORCS; 8448; 16 hits in 1152 CRISPR screens. DR ChiTaRS; DOC2A; human. DR GeneWiki; DOC2A; -. DR GenomeRNAi; 8448; -. DR Pharos; Q14183; Tbio. DR PRO; PR:Q14183; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q14183; Protein. DR Bgee; ENSG00000149927; Expressed in right frontal lobe and 107 other cell types or tissues. DR ExpressionAtlas; Q14183; baseline and differential. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IBA:GO_Central. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0045202; C:synapse; IBA:GO_Central. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0099502; P:calcium-dependent activation of synaptic vesicle fusion; IEA:Ensembl. DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc. DR GO; GO:0006887; P:exocytosis; IBA:GO_Central. DR GO; GO:0007399; P:nervous system development; TAS:ProtInc. DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IMP:UniProtKB. DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; IBA:GO_Central. DR CDD; cd04035; C2A_Rabphilin_Doc2; 1. DR CDD; cd08384; C2B_Rabphilin_Doc2; 1. DR Gene3D; 2.60.40.150; C2 domain; 2. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR014638; Doc2. DR InterPro; IPR043566; Rabphilin/DOC2/Noc2. DR InterPro; IPR047022; Rabphilin_Doc2_C2A. DR InterPro; IPR001565; Synaptotagmin. DR PANTHER; PTHR45729:SF1; DOUBLE C2-LIKE DOMAIN-CONTAINING PROTEIN ALPHA; 1. DR PANTHER; PTHR45729; RABPHILIN, ISOFORM A; 1. DR Pfam; PF00168; C2; 2. DR PIRSF; PIRSF036931; Doc2; 1. DR PRINTS; PR00360; C2DOMAIN. DR PRINTS; PR00399; SYNAPTOTAGMN. DR SMART; SM00239; C2; 2. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2. DR PROSITE; PS50004; C2; 2. DR Genevisible; Q14183; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Calcium/phospholipid-binding; KW Cytoplasmic vesicle; Exocytosis; Lysosome; Membrane; Metal-binding; KW Reference proteome; Repeat; Synapse; Synaptosome. FT CHAIN 1..400 FT /note="Double C2-like domain-containing protein alpha" FT /id="PRO_0000079965" FT DOMAIN 89..211 FT /note="C2 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 251..384 FT /note="C2 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT REGION 1..89 FT /note="Interaction with UNC13D and DYNLT1" FT /evidence="ECO:0000269|PubMed:18354201, FT ECO:0000269|PubMed:9804756" FT REGION 215..400 FT /note="Interaction with UNC13D" FT /evidence="ECO:0000269|PubMed:18354201" FT BINDING 120 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 126 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 181 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 183 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 282 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 282 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 288 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 342 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 342 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 344 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 344 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 350 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT VAR_SEQ 1..118 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056977" FT VAR_SEQ 271..281 FT /note="GILRCAHLAAM -> PEARCGQEIQA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056978" FT VAR_SEQ 282..400 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056979" FT VARIANT 48 FT /note="G -> S (in dbSNP:rs1140239)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:7826360" FT /id="VAR_019656" FT CONFLICT 92 FT /note="T -> K (in Ref. 1; BAA06695)" FT /evidence="ECO:0000305" FT CONFLICT 108..109 FT /note="CS -> VC (in Ref. 1; BAA06695)" FT /evidence="ECO:0000305" FT CONFLICT 238 FT /note="E -> D (in Ref. 1; BAA06695)" FT /evidence="ECO:0000305" FT CONFLICT 376 FT /note="P -> R (in Ref. 1; BAA06695)" FT /evidence="ECO:0000305" FT STRAND 92..100 FT /evidence="ECO:0007829|PDB:4MJJ" FT TURN 101..104 FT /evidence="ECO:0007829|PDB:4MJJ" FT STRAND 105..115 FT /evidence="ECO:0007829|PDB:4MJJ" FT STRAND 127..135 FT /evidence="ECO:0007829|PDB:4MJJ" FT HELIX 139..141 FT /evidence="ECO:0007829|PDB:4MJJ" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:4MJJ" FT STRAND 155..162 FT /evidence="ECO:0007829|PDB:4MJJ" FT HELIX 167..172 FT /evidence="ECO:0007829|PDB:4MJJ" FT STRAND 174..181 FT /evidence="ECO:0007829|PDB:4MJJ" FT STRAND 190..197 FT /evidence="ECO:0007829|PDB:4MJJ" FT HELIX 198..200 FT /evidence="ECO:0007829|PDB:4MJJ" FT STRAND 207..212 FT /evidence="ECO:0007829|PDB:4MJJ" SQ SEQUENCE 400 AA; 43959 MW; 2E61A459AC373C6C CRC64; MRGRRGDRMT INIQEHMAIN VCPGPIRPIR QISDYFPRGP GPEGGGGGGG EAPAHLVPLA LAPPAALLGA TTPEDGAEVD SYDSDDATAL GTLEFDLLYD RASCTLHCSI LRAKGLKPMD FNGLADPYVK LHLLPGACKA NKLKTKTQRN TLNPVWNEDL TYSGITDDDI THKVLRIAVC DEDKLSHNEF IGEIRVPLRR LKPSQKKHFN ICLERQVPLA SPSSMSAALR GISCYLKELE QAEQGQGLLE ERGRILLSLS YSSRRRGLLV GILRCAHLAA MDVNGYSDPY VKTYLRPDVD KKSKHKTCVK KKTLNPEFNE EFFYEIELST LATKTLEVTV WDYDIGKSND FIGGVSLGPG ARGEARKHWS DCLQQPDAAL ERWHTLTSEL PPAAGALSSA //