ID ANXA8_HUMAN Reviewed; 327 AA. AC P13928; A6NDE6; A6NLM1; B4DKI1; B4DTC9; Q5T2P8; Q5VTM4; Q6GMY3; Q9BT34; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 3. DT 24-JAN-2024, entry version 207. DE RecName: Full=Annexin A8 {ECO:0000312|HGNC:HGNC:546}; DE AltName: Full=Annexin VIII {ECO:0000303|PubMed:1313714}; DE AltName: Full=Annexin-8 {ECO:0000303|PubMed:2530088}; DE AltName: Full=Vascular anticoagulant-beta {ECO:0000303|PubMed:2530088}; DE Short=VAC-beta {ECO:0000303|PubMed:2530088}; GN Name=ANXA8 {ECO:0000312|HGNC:HGNC:546}; Synonyms=ANX8; 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), AND VARIANTS ALA-6 AND ALA-177. RC TISSUE=Placenta; RX PubMed=2530088; DOI=10.1111/j.1432-1033.1989.tb15082.x; RA Hauptmann R., Maurer-Fogy I., Krystek E., Bodo G., Andree H., RA Reutelingsperger C.P.M.; RT "Vascular anticoagulant beta: a novel human Ca2+/phospholipid binding RT protein that inhibits coagulation and phospholipase A2 activity. Its RT molecular cloning, expression and comparison with VAC-alpha."; RL Eur. J. Biochem. 185:63-71(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1313714; RA Chang K.S., Wang G., Freireich E.J., Daly M., Naylor S.L., Trujillo J.M., RA Stass S.A.; RT "Specific expression of the annexin VIII gene in acute promyelocytic RT leukemia."; RL Blood 79:1802-1810(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Cervix, and Placenta; 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=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-177. RC TISSUE=Lung, and Pancreas; 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 [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS), AND CALCIUM-BINDING SITES. RX PubMed=15644210; DOI=10.1016/j.jmb.2004.11.015; RA Rety S., Sopkova-de Oliveira Santos J., Dreyfuss L., Blondeau K., RA Hofbauerova K., Raguenes-Nicol C., Kerboeuf D., Renouard M., RA Russo-Marie F., Lewit-Bentley A.; RT "The crystal structure of annexin A8 is similar to that of annexin A3."; RL J. Mol. Biol. 345:1131-1139(2005). CC -!- FUNCTION: This protein is an anticoagulant protein that acts as an CC indirect inhibitor of the thromboplastin-specific complex, which is CC involved in the blood coagulation cascade. CC -!- INTERACTION: CC P13928; P54253: ATXN1; NbExp=6; IntAct=EBI-2556915, EBI-930964; CC P13928; P46379-2: BAG6; NbExp=3; IntAct=EBI-2556915, EBI-10988864; CC P13928; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-2556915, EBI-21553822; CC P13928; O14645: DNALI1; NbExp=3; IntAct=EBI-2556915, EBI-395638; CC P13928; Q01658: DR1; NbExp=3; IntAct=EBI-2556915, EBI-750300; CC P13928; Q00403: GTF2B; NbExp=3; IntAct=EBI-2556915, EBI-389564; CC P13928; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-2556915, EBI-1054873; CC P13928; P04792: HSPB1; NbExp=3; IntAct=EBI-2556915, EBI-352682; CC P13928; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2556915, EBI-10975473; CC P13928; O14901: KLF11; NbExp=3; IntAct=EBI-2556915, EBI-948266; CC P13928; P07196: NEFL; NbExp=3; IntAct=EBI-2556915, EBI-475646; CC P13928; O43933: PEX1; NbExp=3; IntAct=EBI-2556915, EBI-988601; CC P13928; D3DTS7: PMP22; NbExp=3; IntAct=EBI-2556915, EBI-25882629; CC P13928; P60891: PRPS1; NbExp=3; IntAct=EBI-2556915, EBI-749195; CC P13928; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-2556915, EBI-396669; CC P13928; P00441: SOD1; NbExp=3; IntAct=EBI-2556915, EBI-990792; CC P13928; Q13148: TARDBP; NbExp=6; IntAct=EBI-2556915, EBI-372899; CC P13928; O76024: WFS1; NbExp=3; IntAct=EBI-2556915, EBI-720609; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P13928-1; Sequence=Displayed; CC Name=2; CC IsoId=P13928-2; Sequence=VSP_056397, VSP_056398; CC Name=3; CC IsoId=P13928-3; Sequence=VSP_057805; CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium CC and phospholipid. CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE- CC ProRule:PRU01245, 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; X16662; CAA34650.1; -; mRNA. DR EMBL; M81844; AAB46383.1; -; mRNA. DR EMBL; AK296573; BAG59193.1; -; mRNA. DR EMBL; AK300158; BAG61941.1; -; mRNA. DR EMBL; AL391137; CAI12203.1; -; Genomic_DNA. DR EMBL; AL591684; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC004376; AAH04376.1; -; mRNA. DR EMBL; BC073755; AAH73755.1; -; mRNA. DR CCDS; CCDS73121.1; -. [P13928-3] DR CCDS; CCDS73122.1; -. [P13928-1] DR PIR; S06476; LUHU8. DR RefSeq; NP_001035173.1; NM_001040084.2. [P13928-1] DR RefSeq; NP_001092315.2; NM_001098845.2. DR RefSeq; NP_001258631.1; NM_001271702.1. DR RefSeq; NP_001258632.1; NM_001271703.1. [P13928-3] DR PDB; 1W3W; X-ray; 1.99 A; A=1-327. DR PDB; 1W45; X-ray; 2.51 A; A/B=1-327. DR PDBsum; 1W3W; -. DR PDBsum; 1W45; -. DR AlphaFoldDB; P13928; -. DR SMR; P13928; -. DR BioGRID; 575558; 73. DR BioGRID; 608549; 19. DR IntAct; P13928; 31. DR MINT; P13928; -. DR iPTMnet; P13928; -. DR PhosphoSitePlus; P13928; -. DR SwissPalm; P13928; -. DR BioMuta; ANXA8; -. DR DMDM; 215274181; -. DR EPD; P13928; -. DR jPOST; P13928; -. DR MassIVE; P13928; -. DR MaxQB; P13928; -. DR PeptideAtlas; P13928; -. DR ProteomicsDB; 5097; -. DR ProteomicsDB; 52998; -. [P13928-1] DR Antibodypedia; 72811; 178 antibodies from 27 providers. DR DNASU; 244; -. DR Ensembl; ENST00000577813.1; ENSP00000463244.1; ENSG00000265190.7. [P13928-2] DR Ensembl; ENST00000583911.5; ENSP00000463091.1; ENSG00000265190.7. [P13928-3] DR Ensembl; ENST00000585281.6; ENSP00000462880.1; ENSG00000265190.7. [P13928-1] DR GeneID; 653145; -. DR GeneID; 728113; -. DR KEGG; hsa:653145; -. DR KEGG; hsa:728113; -. DR MANE-Select; ENST00000585281.6; ENSP00000462880.1; NM_001040084.3; NP_001035173.1. DR UCSC; uc001jev.5; human. [P13928-1] DR AGR; HGNC:23334; -. DR AGR; HGNC:546; -. DR CTD; 653145; -. DR CTD; 728113; -. DR DisGeNET; 653145; -. DR DisGeNET; 728113; -. DR GeneCards; ANXA8; -. DR HGNC; HGNC:546; ANXA8. DR HPA; ENSG00000265190; Tissue enhanced (esophagus, skin, vagina). DR MIM; 602396; gene. DR neXtProt; NX_P13928; -. DR OpenTargets; ENSG00000265190; -. DR PharmGKB; PA134881914; -. DR PharmGKB; PA24836; -. DR VEuPathDB; HostDB:ENSG00000265190; -. DR GeneTree; ENSGT00940000161044; -. DR HOGENOM; CLU_025300_2_3_1; -. DR InParanoid; P13928; -. DR OMA; CGQFGKE; -. DR OrthoDB; 1500773at2759; -. DR PhylomeDB; P13928; -. DR TreeFam; TF105452; -. DR PathwayCommons; P13928; -. DR SignaLink; P13928; -. DR BioGRID-ORCS; 653145; 6 hits in 1022 CRISPR screens. DR BioGRID-ORCS; 728113; 45 hits in 1036 CRISPR screens. DR ChiTaRS; ANXA8; human. DR EvolutionaryTrace; P13928; -. DR Pharos; P13928; Tbio. DR PRO; PR:P13928; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; P13928; Protein. DR Bgee; ENSG00000265190; Expressed in skin of abdomen and 90 other cell types or tissues. DR ExpressionAtlas; P13928; baseline and differential. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0042383; C:sarcolemma; IBA:GO_Central. DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB. DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB. DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB. DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW. DR GO; GO:0016197; P:endosomal transport; IMP:UniProtKB. DR GO; GO:0007032; P:endosome organization; IMP:UniProtKB. DR GO; GO:1900138; P:negative regulation of phospholipase A2 activity; IDA:UniProtKB. DR GO; GO:1900004; P:negative regulation of serine-type endopeptidase activity; IDA:UniProtKB. DR Gene3D; 1.10.220.10; Annexin; 4. DR InterPro; IPR001464; Annexin. DR InterPro; IPR018502; Annexin_repeat. DR InterPro; IPR018252; Annexin_repeat_CS. DR InterPro; IPR037104; Annexin_sf. DR InterPro; IPR009115; ANX8. DR PANTHER; PTHR10502; ANNEXIN; 1. DR PANTHER; PTHR10502:SF133; ANNEXIN A8-RELATED; 1. DR Pfam; PF00191; Annexin; 4. DR PRINTS; PR00196; ANNEXIN. DR PRINTS; PR01808; ANNEXINVIII. DR SMART; SM00335; ANX; 4. DR SUPFAM; SSF47874; Annexin; 1. DR PROSITE; PS00223; ANNEXIN_1; 4. DR PROSITE; PS51897; ANNEXIN_2; 4. DR Genevisible; P13928; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Annexin; Blood coagulation; Calcium; KW Calcium/phospholipid-binding; Hemostasis; Metal-binding; KW Reference proteome; Repeat. FT CHAIN 1..327 FT /note="Annexin A8" FT /id="PRO_0000067503" FT REPEAT 21..92 FT /note="Annexin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245" FT REPEAT 93..164 FT /note="Annexin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245" FT REPEAT 177..249 FT /note="Annexin 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245" FT REPEAT 253..324 FT /note="Annexin 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245" FT BINDING 266 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 268 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 270 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 310 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT VAR_SEQ 8..69 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057805" FT VAR_SEQ 138..141 FT /note="DYGS -> GQQG (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056397" FT VAR_SEQ 142..327 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056398" FT VARIANT 6 FT /note="S -> A (in dbSNP:rs3870786)" FT /evidence="ECO:0000269|PubMed:2530088" FT /id="VAR_000604" FT VARIANT 177 FT /note="G -> A (in dbSNP:rs75345346)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:2530088" FT /id="VAR_030630" FT CONFLICT 32 FT /note="K -> Q (in Ref. 3; BAG59193 and 4; CAI12203)" FT /evidence="ECO:0000305" FT CONFLICT 58 FT /note="Q -> T (in Ref. 2; AAB46383)" FT /evidence="ECO:0000305" FT CONFLICT 83 FT /note="F -> L (in Ref. 2; AAB46383)" FT /evidence="ECO:0000305" FT CONFLICT 157 FT /note="R -> S (in Ref. 2; AAB46383)" FT /evidence="ECO:0000305" FT CONFLICT 313..314 FT /note="GD -> RY (in Ref. 2; AAB46383)" FT /evidence="ECO:0000305" FT HELIX 24..34 FT /evidence="ECO:0007829|PDB:1W3W" FT STRAND 35..38 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 41..48 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 53..67 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 71..78 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 81..91 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 96..107 FT /evidence="ECO:0007829|PDB:1W3W" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 113..122 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 125..139 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 143..150 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 153..163 FT /evidence="ECO:0007829|PDB:1W3W" FT STRAND 167..170 FT /evidence="ECO:0007829|PDB:1W45" FT HELIX 176..191 FT /evidence="ECO:0007829|PDB:1W3W" FT STRAND 193..195 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 198..207 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 210..224 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 228..235 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 238..252 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 254..266 FT /evidence="ECO:0007829|PDB:1W3W" FT STRAND 267..270 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 273..283 FT /evidence="ECO:0007829|PDB:1W3W" FT TURN 284..286 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 288..299 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 303..310 FT /evidence="ECO:0007829|PDB:1W3W" FT HELIX 313..323 FT /evidence="ECO:0007829|PDB:1W3W" SQ SEQUENCE 327 AA; 36881 MW; 5DBBDBB6E723C298 CRC64; MAWWKSWIEQ EGVTVKSSSH FNPDPDAETL YKAMKGIGTN EQAIIDVLTK RSNTQRQQIA KSFKAQFGKD LTETLKSELS GKFERLIVAL MYPPYRYEAK ELHDAMKGLG TKEGVIIEIL ASRTKNQLRE IMKAYEEDYG SSLEEDIQAD TSGYLERILV CLLQGSRDDV SSFVDPGLAL QDAQDLYAAG EKIRGTDEMK FITILCTRSA THLLRVFEEY EKIANKSIED SIKSETHGSL EEAMLTVVKC TQNLHSYFAE RLYYAMKGAG TRDGTLIRNI VSRSEIDLNL IKCHFKKMYG KTLSSMIMED TSGDYKNALL SLVGSDP //