ID   S10AD_HUMAN             Reviewed;          98 AA.
AC   Q99584; Q52PI9; Q6FGF8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   24-JAN-2024, entry version 195.
DE   RecName: Full=Protein S100-A13;
DE   AltName: Full=S100 calcium-binding protein A13;
GN   Name=S100A13;
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].
RX   PubMed=8878558; DOI=10.1006/bbrc.1996.1551;
RA   Wicki R., Schaefer B.W., Erne P., Heizmann C.W.;
RT   "Characterization of the human and mouse cDNAs coding for S100A13, a new
RT   member of the S100 protein family.";
RL   Biochem. Biophys. Res. Commun. 227:594-599(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Skin;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 2-98.
RC   TISSUE=Thyroid;
RA   Wen G.B., Yang J., Cao R.X., Liu J.H., Peng Z.L.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION.
RX   PubMed=12746488; DOI=10.1242/jcs.00471;
RA   Mandinova A., Soldi R., Graziani I., Bagala C., Bellum S., Landriscina M.,
RA   Tarantini F., Prudovsky I., Maciag T.;
RT   "S100A13 mediates the copper-dependent stress-induced release of IL-1alpha
RT   from both human U937 and murine NIH 3T3 cells.";
RL   J. Cell Sci. 116:2687-2696(2003).
RN   [8]
RP   FUNCTION.
RX   PubMed=20863990; DOI=10.1016/s0929-6646(10)60103-9;
RA   Cao R., Yan B., Yang H., Zu X., Wen G., Zhong J.;
RT   "Effect of human S100A13 gene silencing on FGF-1 transportation in human
RT   endothelial cells.";
RL   J. Formos. Med. Assoc. 109:632-640(2010).
RN   [9]
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   [10]
RP   STRUCTURE BY NMR IN COMPLEX WITH CALCIUM IONS, COPPER-BINDING, AND SUBUNIT.
RX   PubMed=16145699; DOI=10.1002/anie.200500540;
RA   Arnesano F., Banci L., Bertini I., Fantoni A., Tenori L., Viezzoli M.S.;
RT   "Structural interplay between calcium(II) and copper(II) binding to S100A13
RT   protein.";
RL   Angew. Chem. Int. Ed. 44:6341-6344(2005).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, AND
RP   SUBUNIT.
RX   PubMed=17374362; DOI=10.1016/j.bbrc.2007.03.014;
RA   Li M., Zhang P.F., Pan X.W., Chang W.R.;
RT   "Crystal structure study on human S100A13 at 2.0 A resolution.";
RL   Biochem. Biophys. Res. Commun. 356:616-621(2007).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, AND
RP   SUBUNIT.
RX   PubMed=18259052; DOI=10.1107/s1744309107068236;
RA   Imai F.L., Nagata K., Yonezawa N., Nakano M., Tanokura M.;
RT   "Structure of calcium-bound human S100A13 at pH 7.5 at 1.8 A resolution.";
RL   Acta Crystallogr. F 64:70-76(2008).
RN   [13]
RP   STRUCTURE BY NMR IN COMPLEX WITH SYT1, AND SUBUNIT.
RX   PubMed=19284995; DOI=10.1016/j.bbrc.2009.01.143;
RA   Mohan S.K., Rani S.G., Kumar S.M., Yu C.;
RT   "S100A13-C2A binary complex structure-a key component in the acidic
RT   fibroblast growth factor for the non-classical pathway.";
RL   Biochem. Biophys. Res. Commun. 380:514-519(2009).
RN   [14] {ECO:0007744|PDB:2L5X}
RP   STRUCTURE BY NMR, AND INTERACTION WITH IL1A.
RX   PubMed=21270123; DOI=10.1074/jbc.m110.201954;
RA   Mohan S.K., Yu C.;
RT   "The IL1alpha-S100A13 heterotetrameric complex structure: a component in
RT   the non-classical pathway for interleukin 1alpha secretion.";
RL   J. Biol. Chem. 286:14608-14617(2011).
CC   -!- FUNCTION: Plays a role in the export of proteins that lack a signal
CC       peptide and are secreted by an alternative pathway. Binds two calcium
CC       ions per subunit. Binds one copper ion. Binding of one copper ion does
CC       not interfere with calcium binding. Required for the copper-dependent
CC       stress-induced export of IL1A and FGF1. The calcium-free protein binds
CC       to lipid vesicles containing phosphatidylserine, but not to vesicles
CC       containing phosphatidylcholine (By similarity).
CC       {ECO:0000250|UniProtKB:P97352, ECO:0000269|PubMed:12746488,
CC       ECO:0000269|PubMed:20863990}.
CC   -!- SUBUNIT: Homodimer. Part of a copper-dependent multiprotein complex
CC       containing S100A13, FGF1 and SYT1. Interacts with FGF1 and SYT1 (By
CC       similarity). Interacts with IL1A (PubMed:21270123).
CC       {ECO:0000250|UniProtKB:P97352, ECO:0000269|PubMed:21270123}.
CC   -!- INTERACTION:
CC       Q99584; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-721909, EBI-742388;
CC       Q99584; Q9HCY8: S100A14; NbExp=5; IntAct=EBI-721909, EBI-751842;
CC       Q99584; P01375: TNF; NbExp=2; IntAct=EBI-721909, EBI-359977;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted. Note=Secretion is mediated
CC       by exposure to stress and requires copper ions.
CC   -!- TISSUE SPECIFICITY: Expressed in heart and skeletal muscle.
CC   -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/44197/S100A13";
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DR   EMBL; X99920; CAA68188.1; -; mRNA.
DR   EMBL; CR542149; CAG46946.1; -; mRNA.
DR   EMBL; BT006724; AAP35370.1; -; mRNA.
DR   EMBL; BX470102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC000632; AAH00632.1; -; mRNA.
DR   EMBL; BC068064; AAH68064.1; -; mRNA.
DR   EMBL; BC070291; AAH70291.1; -; mRNA.
DR   EMBL; AY987392; AAX89402.1; -; mRNA.
DR   CCDS; CCDS30874.1; -.
DR   PIR; JC5064; JC5064.
DR   RefSeq; NP_001019381.1; NM_001024210.1.
DR   RefSeq; NP_001019382.1; NM_001024211.1.
DR   RefSeq; NP_001019383.1; NM_001024212.1.
DR   RefSeq; NP_001019384.1; NM_001024213.1.
DR   RefSeq; NP_005970.1; NM_005979.2.
DR   RefSeq; XP_005245491.1; XM_005245434.3.
DR   RefSeq; XP_011508164.1; XM_011509862.2.
DR   RefSeq; XP_011508165.1; XM_011509863.2.
DR   RefSeq; XP_011508166.1; XM_011509864.1.
DR   RefSeq; XP_016857523.1; XM_017002034.1.
DR   RefSeq; XP_016857524.1; XM_017002035.1.
DR   RefSeq; XP_016857525.1; XM_017002036.1.
DR   PDB; 1YUR; NMR; -; A/B=1-98.
DR   PDB; 1YUS; NMR; -; A/B=1-98.
DR   PDB; 1YUT; NMR; -; A/B=1-98.
DR   PDB; 1YUU; NMR; -; A/B=1-98.
DR   PDB; 2EGD; X-ray; 1.80 A; A/B=1-98.
DR   PDB; 2H2K; X-ray; 2.00 A; A/B=1-98.
DR   PDB; 2K8M; NMR; -; B/C=1-98.
DR   PDB; 2KI4; NMR; -; B/C=1-98.
DR   PDB; 2KI6; NMR; -; C/D=1-98.
DR   PDB; 2KOT; NMR; -; A/B=1-98.
DR   PDB; 2L5X; NMR; -; B/C=1-98.
DR   PDB; 2LE9; NMR; -; B/C=2-98.
DR   PDBsum; 1YUR; -.
DR   PDBsum; 1YUS; -.
DR   PDBsum; 1YUT; -.
DR   PDBsum; 1YUU; -.
DR   PDBsum; 2EGD; -.
DR   PDBsum; 2H2K; -.
DR   PDBsum; 2K8M; -.
DR   PDBsum; 2KI4; -.
DR   PDBsum; 2KI6; -.
DR   PDBsum; 2KOT; -.
DR   PDBsum; 2L5X; -.
DR   PDBsum; 2LE9; -.
DR   AlphaFoldDB; Q99584; -.
DR   BMRB; Q99584; -.
DR   SMR; Q99584; -.
DR   BioGRID; 112192; 39.
DR   IntAct; Q99584; 23.
DR   MINT; Q99584; -.
DR   STRING; 9606.ENSP00000392767; -.
DR   DrugBank; DB01025; Amlexanox.
DR   DrugBank; DB01373; Calcium.
DR   DrugBank; DB01164; Calcium chloride.
DR   DrugBank; DB11093; Calcium citrate.
DR   DrugBank; DB11348; Calcium Phosphate.
DR   DrugBank; DB14481; Calcium phosphate dihydrate.
DR   DrugBank; DB00768; Olopatadine.
DR   GlyGen; Q99584; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q99584; -.
DR   PhosphoSitePlus; Q99584; -.
DR   BioMuta; S100A13; -.
DR   DMDM; 2493416; -.
DR   EPD; Q99584; -.
DR   jPOST; Q99584; -.
DR   MassIVE; Q99584; -.
DR   MaxQB; Q99584; -.
DR   PaxDb; 9606-ENSP00000357688; -.
DR   PeptideAtlas; Q99584; -.
DR   ProteomicsDB; 78342; -.
DR   Pumba; Q99584; -.
DR   TopDownProteomics; Q99584; -.
DR   Antibodypedia; 34130; 208 antibodies from 29 providers.
DR   DNASU; 6284; -.
DR   Ensembl; ENST00000339556.8; ENSP00000344822.3; ENSG00000189171.15.
DR   Ensembl; ENST00000392622.3; ENSP00000376398.1; ENSG00000189171.15.
DR   Ensembl; ENST00000392623.5; ENSP00000376399.1; ENSG00000189171.15.
DR   Ensembl; ENST00000440685.7; ENSP00000392767.2; ENSG00000189171.15.
DR   Ensembl; ENST00000476133.6; ENSP00000507299.1; ENSG00000189171.15.
DR   GeneID; 6284; -.
DR   KEGG; hsa:6284; -.
DR   MANE-Select; ENST00000476133.6; ENSP00000507299.1; NM_001024211.2; NP_001019382.1.
DR   UCSC; uc001fcf.5; human.
DR   AGR; HGNC:10490; -.
DR   CTD; 6284; -.
DR   DisGeNET; 6284; -.
DR   GeneCards; S100A13; -.
DR   HGNC; HGNC:10490; S100A13.
DR   HPA; ENSG00000189171; Low tissue specificity.
DR   MIM; 601989; gene.
DR   neXtProt; NX_Q99584; -.
DR   OpenTargets; ENSG00000189171; -.
DR   PharmGKB; PA34902; -.
DR   VEuPathDB; HostDB:ENSG00000189171; -.
DR   eggNOG; ENOG502S3RT; Eukaryota.
DR   GeneTree; ENSGT00940000161854; -.
DR   HOGENOM; CLU_138624_3_0_1; -.
DR   InParanoid; Q99584; -.
DR   OMA; TFFTFAK; -.
DR   OrthoDB; 3954907at2759; -.
DR   PhylomeDB; Q99584; -.
DR   TreeFam; TF332727; -.
DR   PathwayCommons; Q99584; -.
DR   SignaLink; Q99584; -.
DR   SIGNOR; Q99584; -.
DR   BioGRID-ORCS; 6284; 11 hits in 1161 CRISPR screens.
DR   ChiTaRS; S100A13; human.
DR   EvolutionaryTrace; Q99584; -.
DR   GeneWiki; S100A13; -.
DR   GenomeRNAi; 6284; -.
DR   Pharos; Q99584; Tbio.
DR   PRO; PR:Q99584; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q99584; Protein.
DR   Bgee; ENSG00000189171; Expressed in right lobe of thyroid gland and 110 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR   GO; GO:0017134; F:fibroblast growth factor binding; IPI:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0050786; F:RAGE receptor binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0043303; P:mast cell degranulation; NAS:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IDA:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IMP:UniProtKB.
DR   GO; GO:0032730; P:positive regulation of interleukin-1 alpha production; IDA:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd05022; S-100A13; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR013787; S100_Ca-bd_sub.
DR   PANTHER; PTHR11639:SF57; PROTEIN S100-A13; 1.
DR   PANTHER; PTHR11639; S100 CALCIUM-BINDING PROTEIN; 1.
DR   Pfam; PF01023; S_100; 1.
DR   SMART; SM01394; S_100; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   Genevisible; Q99584; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Copper; Cytoplasm; Lipid-binding; Metal-binding;
KW   Phosphoprotein; Protein transport; Reference proteome; Repeat; Secreted;
KW   Transport.
FT   CHAIN           1..98
FT                   /note="Protein S100-A13"
FT                   /id="PRO_0000144019"
FT   DOMAIN          18..53
FT                   /note="EF-hand"
FT   BINDING         32
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         37
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         64
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         66
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         68
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         70
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         75
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97352"
FT   HELIX           1..3
FT                   /evidence="ECO:0007829|PDB:2H2K"
FT   HELIX           8..24
FT                   /evidence="ECO:0007829|PDB:2EGD"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:2EGD"
FT   STRAND          32..34
FT                   /evidence="ECO:0007829|PDB:2K8M"
FT   HELIX           35..45
FT                   /evidence="ECO:0007829|PDB:2EGD"
FT   TURN            47..52
FT                   /evidence="ECO:0007829|PDB:2EGD"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:2KI4"
FT   HELIX           56..63
FT                   /evidence="ECO:0007829|PDB:2EGD"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:2EGD"
FT   HELIX           73..88
FT                   /evidence="ECO:0007829|PDB:2EGD"
FT   HELIX           93..95
FT                   /evidence="ECO:0007829|PDB:1YUR"
SQ   SEQUENCE   98 AA;  11471 MW;  1D1BE57F3CD49E81 CRC64;
     MAAEPLTELE ESIETVVTTF FTFARQEGRK DSLSVNEFKE LVTQQLPHLL KDVGSLDEKM
     KSLDVNQDSE LKFNEYWRLI GELAKEIRKK KDLKIRKK
//