SYT5_HUMAN
ID SYT5_HUMAN Reviewed; 386 AA.
AC O00445; B3KWJ8; B7Z300; Q86X72;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Synaptotagmin-5;
DE AltName: Full=Synaptotagmin V;
DE Short=SytV;
GN Name=SYT5;
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 [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=9177789; DOI=10.1006/geno.1997.4722;
RA Craxton M.A., Olsen A., Goedert M.;
RT "Human synaptotagmin V (SYT5): sequence, genomic structure, and chromosomal
RT location.";
RL Genomics 42:165-169(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Caudate nucleus;
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=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-111.
RC TISSUE=Brain;
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] {ECO:0007744|PDB:5H4Y, ECO:0007744|PDB:5H4Z}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 107-233 IN COMPLEX WITH CALCIUM,
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 105-233 OF MUTANT GLY-202 IN
RP COMPLEX WITH CALCIUM, AND MUTAGENESIS OF SER-202.
RX PubMed=27793683; DOI=10.1016/j.ijbiomac.2016.10.083;
RA Qiu X., Ge J., Gao Y., Teng M., Niu L.;
RT "Structural analysis of Ca2+-binding pocket of synaptotagmin 5 C2A
RT domain.";
RL Int. J. Biol. Macromol. 95:946-953(2017).
CC -!- FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory
CC vesicles through Ca(2+) and phospholipid binding to the C2 domain or
CC may serve as Ca(2+) sensors in the process of vesicular trafficking and
CC exocytosis. Regulates the Ca(2+)-dependent secretion of norepinephrine
CC in PC12 cells. Required for export from the endocytic recycling
CC compartment to the cell surface (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041,
CC ECO:0000269|PubMed:27793683};
CC Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
CC domains. {ECO:0000269|PubMed:15057824};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with both alpha- and
CC beta-tubulin (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P47861}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250}; Single-pass membrane protein
CC {ECO:0000250}. Recycling endosome membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}. Note=In mast cells, localizes to the
CC endocytic recycling compartment. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00445-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00445-2; Sequence=VSP_057177, VSP_057178;
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; X96783; CAA65579.1; -; Genomic_DNA.
DR EMBL; AK125182; BAG54160.1; -; mRNA.
DR EMBL; AK295337; BAH12036.1; -; mRNA.
DR EMBL; AC010327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046157; AAH46157.1; -; mRNA.
DR CCDS; CCDS12919.1; -. [O00445-1]
DR CCDS; CCDS74455.1; -. [O00445-2]
DR RefSeq; NP_001284703.1; NM_001297774.1. [O00445-2]
DR RefSeq; NP_003171.2; NM_003180.2. [O00445-1]
DR RefSeq; XP_006723402.1; XM_006723339.3. [O00445-1]
DR RefSeq; XP_016882664.1; XM_017027175.1. [O00445-1]
DR RefSeq; XP_016882665.1; XM_017027176.1.
DR PDB; 5H4Y; X-ray; 1.90 A; A=102-242.
DR PDB; 5H4Z; X-ray; 3.01 A; A/B=102-242.
DR PDBsum; 5H4Y; -.
DR PDBsum; 5H4Z; -.
DR AlphaFoldDB; O00445; -.
DR SMR; O00445; -.
DR BioGRID; 112725; 11.
DR ELM; O00445; -.
DR IntAct; O00445; 8.
DR MINT; O00445; -.
DR STRING; 9606.ENSP00000346265; -.
DR iPTMnet; O00445; -.
DR PhosphoSitePlus; O00445; -.
DR BioMuta; SYT5; -.
DR jPOST; O00445; -.
DR MassIVE; O00445; -.
DR MaxQB; O00445; -.
DR PaxDb; O00445; -.
DR PeptideAtlas; O00445; -.
DR PRIDE; O00445; -.
DR ProteomicsDB; 47896; -. [O00445-1]
DR ProteomicsDB; 6480; -.
DR Antibodypedia; 2420; 216 antibodies from 33 providers.
DR DNASU; 6861; -.
DR Ensembl; ENST00000354308.8; ENSP00000346265.2; ENSG00000129990.15. [O00445-1]
DR Ensembl; ENST00000537500.5; ENSP00000442896.1; ENSG00000129990.15. [O00445-1]
DR Ensembl; ENST00000590851.5; ENSP00000465576.1; ENSG00000129990.15. [O00445-2]
DR GeneID; 6861; -.
DR KEGG; hsa:6861; -.
DR MANE-Select; ENST00000354308.8; ENSP00000346265.2; NM_003180.3; NP_003171.2.
DR UCSC; uc002qjm.2; human. [O00445-1]
DR CTD; 6861; -.
DR DisGeNET; 6861; -.
DR GeneCards; SYT5; -.
DR HGNC; HGNC:11513; SYT5.
DR HPA; ENSG00000129990; Group enriched (brain, pituitary gland).
DR MIM; 600782; gene.
DR neXtProt; NX_O00445; -.
DR OpenTargets; ENSG00000129990; -.
DR PharmGKB; PA36294; -.
DR VEuPathDB; HostDB:ENSG00000129990; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000161816; -.
DR HOGENOM; CLU_023008_0_1_1; -.
DR InParanoid; O00445; -.
DR OMA; CLCRKRC; -.
DR PhylomeDB; O00445; -.
DR TreeFam; TF315600; -.
DR PathwayCommons; O00445; -.
DR Reactome; R-HSA-422356; Regulation of insulin secretion.
DR SignaLink; O00445; -.
DR BioGRID-ORCS; 6861; 29 hits in 1075 CRISPR screens.
DR GeneWiki; SYT5; -.
DR GenomeRNAi; 6861; -.
DR Pharos; O00445; Tbio.
DR PRO; PR:O00445; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O00445; protein.
DR Bgee; ENSG00000129990; Expressed in cortical plate and 137 other tissues.
DR ExpressionAtlas; O00445; baseline and differential.
DR Genevisible; O00445; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0031045; C:dense core granule; IBA:GO_Central.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0099066; C:integral component of neuronal dense core vesicle membrane; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1990769; C:proximal neuron projection; IEA:Ensembl.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IBA:GO_Central.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IBA:GO_Central.
DR GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR GO; GO:0014059; P:regulation of dopamine secretion; IBA:GO_Central.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001565; Synaptotagmin.
DR InterPro; IPR028689; SYT5.
DR PANTHER; PTHR10024:SF282; PTHR10024:SF282; 1.
DR Pfam; PF00168; C2; 2.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00399; SYNAPTOTAGMN.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cytoplasmic vesicle; Endosome;
KW Membrane; Metal-binding; Reference proteome; Repeat; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..386
FT /note="Synaptotagmin-5"
FT /id="PRO_0000183951"
FT TOPO_DOM 1..24
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 108..227
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 239..372
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT VAR_SEQ 1..84
FT /note="MFPEPPTPGPPSPDTPPDSSRISHGPVPPWALATIVLVSGLLIFSCCFCLYR
FT KSCRRRTGKKSQAQAQVHLQEVKGLGQSYIDK -> MTRGGCPVSARLFAQRPHGSWSS
FT LLCVGLKGRLGWEWGTRVLECLCRKDSRTPPPCSRSPQPRGLHRPTRLPTPVASATAQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057177"
FT VAR_SEQ 237
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057178"
FT VARIANT 4
FT /note="E -> D (in dbSNP:rs2301279)"
FT /id="VAR_052240"
FT VARIANT 111
FT /note="R -> Q (in dbSNP:rs11542503)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_034528"
FT MUTAGEN 202
FT /note="S->G: Does not affect Ca(2+) affinity as measured by
FT isothermal titration calorimetry of the mutant protein."
FT /evidence="ECO:0000269|PubMed:27793683"
FT CONFLICT 24
FT /note="H -> R (in Ref. 2; BAG54160)"
FT /evidence="ECO:0000305"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:5H4Y"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:5H4Y"
FT STRAND 124..134
FT /evidence="ECO:0007829|PDB:5H4Y"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:5H4Y"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:5H4Y"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:5H4Y"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:5H4Y"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:5H4Y"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:5H4Y"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:5H4Y"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:5H4Y"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:5H4Y"
SQ SEQUENCE 386 AA; 42900 MW; 96A36792D177FD55 CRC64;
MFPEPPTPGP PSPDTPPDSS RISHGPVPPW ALATIVLVSG LLIFSCCFCL YRKSCRRRTG
KKSQAQAQVH LQEVKGLGQS YIDKVQPEVE ELEPAPSGPG QQVADKHELG RLQYSLDYDF
QSGQLLVGIL QAMGLAALDL GGSSDPYVRV YLLPDKRRRY ETKVHRQTLN PHFGETFAFK
VPYVELGGRV LVMAVYDFDR FSRNDAIGEV RVPMSSVDLG RPVQAWRELQ AAPREEQEKL
GDICFSLRYV PTAGKLTVIV LEAKNLKKMD VGGLSDPYVK VHLLQGGKKV RKKKTTIKKN
TLNPYYNEAF SFEVPCDQVQ KVQVELTVLD YDKLGKNEAI GRVAVGAAAG GAGLRHWADM
LANPRRPIAQ WHSLRPPDRV RLLPAP
