ID   SEM5A_HUMAN             Reviewed;        1074 AA.
AC   Q13591; D3DTC6; O60408; Q1RLL9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 3.
DT   24-JAN-2024, entry version 207.
DE   RecName: Full=Semaphorin-5A;
DE   AltName: Full=Semaphorin-F;
DE            Short=Sema F;
DE   Flags: Precursor;
GN   Name=SEMA5A; Synonyms=SEMAF;
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=9464278; DOI=10.1006/bbrc.1997.8027;
RA   Simmons A.D., Puschel A.W., McPherson J.D., Overhauser J., Lovett M.;
RT   "Molecular cloning and mapping of human semaphorin F from the Cri-du-chat
RT   candidate interval.";
RL   Biochem. Biophys. Res. Commun. 242:685-691(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   FUNCTION, AND INTERACTION WITH PLXNB3.
RX   PubMed=15218527; DOI=10.1038/sj.embor.7400189;
RA   Artigiani S., Conrotto P., Fazzari P., Gilestro G.F., Barberis D.,
RA   Giordano S., Comoglio P.M., Tamagnone L.;
RT   "Plexin-B3 is a functional receptor for semaphorin 5A.";
RL   EMBO Rep. 5:710-714(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=20696765; DOI=10.1074/jbc.m110.120451;
RA   Li X., Lee A.Y.;
RT   "Semaphorin 5A and plexin-B3 inhibit human glioma cell motility through
RT   RhoGDIalpha-mediated inactivation of Rac1 GTPase.";
RL   J. Biol. Chem. 285:32436-32445(2010).
RN   [7]
RP   FUNCTION.
RX   PubMed=19850054; DOI=10.1016/j.mvr.2009.10.005;
RA   Sadanandam A., Rosenbaugh E.G., Singh S., Varney M., Singh R.K.;
RT   "Semaphorin 5A promotes angiogenesis by increasing endothelial cell
RT   proliferation, migration, and decreasing apoptosis.";
RL   Microvasc. Res. 79:1-9(2010).
RN   [8]
RP   FUNCTION.
RX   PubMed=21706053; DOI=10.1038/onc.2011.256;
RA   Li X., Law J.W., Lee A.Y.;
RT   "Semaphorin 5A and plexin-B3 regulate human glioma cell motility and
RT   morphology through Rac1 and the actin cytoskeleton.";
RL   Oncogene 31:595-610(2012).
RN   [9]
RP   VARIANT 196-ARG--TYR-1074 DEL.
RX   PubMed=26637798; DOI=10.1016/j.neuron.2015.11.009;
RA   D'Gama A.M., Pochareddy S., Li M., Jamuar S.S., Reiff R.E., Lam A.T.,
RA   Sestan N., Walsh C.A.;
RT   "Targeted DNA Sequencing from Autism Spectrum Disorder Brains Implicates
RT   Multiple Genetic Mechanisms.";
RL   Neuron 88:910-917(2015).
CC   -!- FUNCTION: Bifunctional axonal guidance cue regulated by sulfated
CC       proteoglycans; attractive effects result from interactions with heparan
CC       sulfate proteoglycans (HSPGs), while the inhibitory effects depend on
CC       interactions with chondroitin sulfate proteoglycans (CSPGs) (By
CC       similarity). Ligand for receptor PLXNB3. In glioma cells, SEMA5A
CC       stimulation of PLXNB3 results in the disassembly of F-actin stress
CC       fibers, disruption of focal adhesions and cellular collapse as well as
CC       inhibition of cell migration and invasion through ARHGDIA-mediated
CC       inactivation of RAC1. May promote angiogenesis by increasing
CC       endothelial cell proliferation and migration and inhibiting apoptosis.
CC       {ECO:0000250, ECO:0000269|PubMed:15218527, ECO:0000269|PubMed:19850054,
CC       ECO:0000269|PubMed:20696765, ECO:0000269|PubMed:21706053}.
CC   -!- SUBUNIT: Binds PLXNB3.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR   EMBL; U52840; AAC09473.1; -; mRNA.
DR   EMBL; AC004615; AAC14668.1; -; Genomic_DNA.
DR   EMBL; AC022446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC027336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC091906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471102; EAX08078.1; -; Genomic_DNA.
DR   EMBL; CH471102; EAX08079.1; -; Genomic_DNA.
DR   EMBL; BC115696; AAI15697.1; -; mRNA.
DR   CCDS; CCDS3875.1; -.
DR   PIR; JC5928; JC5928.
DR   RefSeq; NP_003957.2; NM_003966.2.
DR   RefSeq; XP_006714569.1; XM_006714506.2.
DR   RefSeq; XP_006714570.1; XM_006714507.3.
DR   RefSeq; XP_011512457.1; XM_011514155.2.
DR   RefSeq; XP_011512458.1; XM_011514156.1.
DR   RefSeq; XP_011512459.1; XM_011514157.1.
DR   RefSeq; XP_011512460.1; XM_011514158.1.
DR   AlphaFoldDB; Q13591; -.
DR   SMR; Q13591; -.
DR   IntAct; Q13591; 2.
DR   STRING; 9606.ENSP00000371936; -.
DR   GlyCosmos; Q13591; 11 sites, No reported glycans.
DR   GlyGen; Q13591; 11 sites.
DR   iPTMnet; Q13591; -.
DR   PhosphoSitePlus; Q13591; -.
DR   SwissPalm; Q13591; -.
DR   BioMuta; SEMA5A; -.
DR   DMDM; 109939725; -.
DR   jPOST; Q13591; -.
DR   MassIVE; Q13591; -.
DR   PaxDb; 9606-ENSP00000371936; -.
DR   PeptideAtlas; Q13591; -.
DR   ProteomicsDB; 59586; -.
DR   Antibodypedia; 960; 326 antibodies from 29 providers.
DR   DNASU; 9037; -.
DR   Ensembl; ENST00000382496.10; ENSP00000371936.5; ENSG00000112902.12.
DR   Ensembl; ENST00000652226.1; ENSP00000499013.1; ENSG00000112902.12.
DR   GeneID; 9037; -.
DR   KEGG; hsa:9037; -.
DR   MANE-Select; ENST00000382496.10; ENSP00000371936.5; NM_003966.3; NP_003957.2.
DR   AGR; HGNC:10736; -.
DR   CTD; 9037; -.
DR   DisGeNET; 9037; -.
DR   GeneCards; SEMA5A; -.
DR   HGNC; HGNC:10736; SEMA5A.
DR   HPA; ENSG00000112902; Low tissue specificity.
DR   MalaCards; SEMA5A; -.
DR   MIM; 609297; gene.
DR   neXtProt; NX_Q13591; -.
DR   OpenTargets; ENSG00000112902; -.
DR   Orphanet; 281; Monosomy 5p.
DR   PharmGKB; PA35658; -.
DR   VEuPathDB; HostDB:ENSG00000112902; -.
DR   eggNOG; KOG3611; Eukaryota.
DR   GeneTree; ENSGT00940000158036; -.
DR   HOGENOM; CLU_005410_1_0_1; -.
DR   InParanoid; Q13591; -.
DR   OMA; VEIANCS; -.
DR   OrthoDB; 5399685at2759; -.
DR   PhylomeDB; Q13591; -.
DR   TreeFam; TF329951; -.
DR   PathwayCommons; Q13591; -.
DR   Reactome; R-HSA-416700; Other semaphorin interactions.
DR   Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR   Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR   SignaLink; Q13591; -.
DR   SIGNOR; Q13591; -.
DR   BioGRID-ORCS; 9037; 10 hits in 1140 CRISPR screens.
DR   ChiTaRS; SEMA5A; human.
DR   GeneWiki; SEMA5A; -.
DR   GenomeRNAi; 9037; -.
DR   Pharos; Q13591; Tbio.
DR   PRO; PR:Q13591; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q13591; Protein.
DR   Bgee; ENSG00000112902; Expressed in metanephric glomerulus and 189 other cell types or tissues.
DR   ExpressionAtlas; Q13591; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR   GO; GO:0035373; F:chondroitin sulfate proteoglycan binding; ISS:UniProtKB.
DR   GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISS:UniProtKB.
DR   GO; GO:0030215; F:semaphorin receptor binding; ISS:UniProtKB.
DR   GO; GO:0045545; F:syndecan binding; ISS:UniProtKB.
DR   GO; GO:0048675; P:axon extension; IBA:GO_Central.
DR   GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR   GO; GO:0007413; P:axonal fasciculation; ISS:UniProtKB.
DR   GO; GO:0002043; P:blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR   GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   GO; GO:0021536; P:diencephalon development; ISS:UniProtKB.
DR   GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; ISS:UniProtKB.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB.
DR   GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR   GO; GO:0050918; P:positive chemotaxis; ISS:UniProtKB.
DR   GO; GO:0030836; P:positive regulation of actin filament depolymerization; ISS:UniProtKB.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR   GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; ISS:UniProtKB.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR   GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; ISS:UniProtKB.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB.
DR   GO; GO:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
DR   GO; GO:1990256; P:signal clustering; ISS:UniProtKB.
DR   CDD; cd11263; Sema_5A; 1.
DR   Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 6.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR042821; Sema5A_sema.
DR   InterPro; IPR001627; Semap_dom.
DR   InterPro; IPR036352; Semap_dom_sf.
DR   InterPro; IPR027231; Semaphorin.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR11036; SEMAPHORIN; 1.
DR   PANTHER; PTHR11036:SF78; SEMAPHORIN-5A; 1.
DR   Pfam; PF01437; PSI; 1.
DR   Pfam; PF01403; Sema; 1.
DR   Pfam; PF00090; TSP_1; 5.
DR   PRINTS; PR01705; TSP1REPEAT.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00630; Sema; 1.
DR   SMART; SM00209; TSP1; 6.
DR   SUPFAM; SSF103575; Plexin repeat; 1.
DR   SUPFAM; SSF101912; Sema domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 6.
DR   PROSITE; PS51004; SEMA; 1.
DR   PROSITE; PS50092; TSP1; 6.
DR   Genevisible; Q13591; HS.
PE   1: Evidence at protein level;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Membrane; Neurogenesis; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..1074
FT                   /note="Semaphorin-5A"
FT                   /id="PRO_0000032335"
FT   TOPO_DOM        23..968
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        969..989
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        990..1074
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          35..484
FT                   /note="Sema"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DOMAIN          540..593
FT                   /note="TSP type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          595..651
FT                   /note="TSP type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          653..702
FT                   /note="TSP type-1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          707..765
FT                   /note="TSP type-1 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          784..839
FT                   /note="TSP type-1 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          841..896
FT                   /note="TSP type-1 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          897..944
FT                   /note="TSP type-1 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        367
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        437
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        536
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        591
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        717
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        933
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        104..114
FT                   /evidence="ECO:0000250"
FT   DISULFID        131..140
FT                   /evidence="ECO:0000250"
FT   DISULFID        254..357
FT                   /evidence="ECO:0000250"
FT   DISULFID        278..320
FT                   /evidence="ECO:0000250"
FT   DISULFID        487..504
FT                   /evidence="ECO:0000250"
FT   DISULFID        496..513
FT                   /evidence="ECO:0000250"
FT   DISULFID        607..644
FT                   /evidence="ECO:0000250"
FT   DISULFID        611..650
FT                   /evidence="ECO:0000250"
FT   DISULFID        622..634
FT                   /evidence="ECO:0000250"
FT   DISULFID        665..696
FT                   /evidence="ECO:0000250"
FT   DISULFID        669..701
FT                   /evidence="ECO:0000250"
FT   DISULFID        680..686
FT                   /evidence="ECO:0000250"
FT   DISULFID        796..833
FT                   /evidence="ECO:0000250"
FT   DISULFID        800..838
FT                   /evidence="ECO:0000250"
FT   DISULFID        811..823
FT                   /evidence="ECO:0000250"
FT   DISULFID        853..890
FT                   /evidence="ECO:0000250"
FT   DISULFID        857..895
FT                   /evidence="ECO:0000250"
FT   DISULFID        868..880
FT                   /evidence="ECO:0000250"
FT   VARIANT         196..1074
FT                   /note="Missing (found in a patient with autism spectrum
FT                   disorder; likely pathogenic)"
FT                   /evidence="ECO:0000269|PubMed:26637798"
FT                   /id="VAR_078706"
FT   VARIANT         246
FT                   /note="V -> L (in dbSNP:rs1806079)"
FT                   /id="VAR_030294"
FT   VARIANT         792
FT                   /note="S -> L (in dbSNP:rs2290734)"
FT                   /id="VAR_030295"
FT   CONFLICT        56
FT                   /note="V -> A (in Ref. 1; AAC09473)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149
FT                   /note="T -> A (in Ref. 1; AAC09473)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        382
FT                   /note="M -> V (in Ref. 1; AAC09473)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        494
FT                   /note="S -> R (in Ref. 2; AAC14668)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        723
FT                   /note="G -> D (in Ref. 1; AAC09473)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        835
FT                   /note="I -> T (in Ref. 1; AAC09473)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1074 AA;  120615 MW;  AE073413AC974CCC CRC64;
     MKGTCVIAWL FSSLGLWRLA HPEAQGTTQC QRTEHPVISY KEIGPWLREF RAKNAVDFSQ
     LTFDPGQKEL VVGARNYLFR LQLEDLSLIQ AVEWECDEAT KKACYSKGKS KEECQNYIRV
     LLVGGDRLFT CGTNAFTPVC TNRSLSNLTE IHDQISGMAR CPYSPQHNST ALLTAGGELY
     AATAMDFPGR DPAIYRSLGI LPPLRTAQYN SKWLNEPNFV SSYDIGNFTY FFFRENAVEH
     DCGKTVFSRA ARVCKNDIGG RFLLEDTWTT FMKARLNCSR PGEVPFYYNE LQSTFFLPEL
     DLIYGIFTTN VNSIAASAVC VFNLSAIAQA FSGPFKYQEN SRSAWLPYPN PNPHFQCGTV
     DQGLYVNLTE RNLQDAQKFI LMHEVVQPVT TVPSFMEDNS RFSHVAVDVV QGREALVHII
     YLATDYGTIK KVRVPLNQTS SSCLLEEIEL FPERRREPIR SLQILHSQSV LFVGLREHVV
     KIPLKRCQFY RTRSTCIGAQ DPYCGWDVVM KKCTSLEESL SMTQWEQSIS ACPTRNLTVD
     GHFGVWSPWT PCTHTDGSAV GSCLCRTRSC DSPAPQCGGW QCEGPGMEIA NCSRNGGWTP
     WTSWSPCSTT CGIGFQVRQR SCSNPTPRHG GRVCVGQNRE ERYCNEHLLC PPHMFWTGWG
     PWERCTAQCG GGIQARRRIC ENGPDCAGCN VEYQSCNTNP CPELKKTTPW TPWTPVNISD
     NGGHYEQRFR YTCKARLADP NLLEVGRQRI EMRYCSSDGT SGCSTDGLSG DFLRAGRYSA
     HTVNGAWSAW TSWSQCSRDC SRGIRNRKRV CNNPEPKYGG MPCLGPSLEY QECNILPCPV
     DGVWSCWSPW TKCSATCGGG HYMRTRSCSN PAPAYGGDIC LGLHTEEALC NTQPCPESWS
     EWSDWSECEA SGVQVRARQC ILLFPMGSQC SGNTTESRPC VFDSNFIPEV SVARSSSVEE
     KRCGEFNMFH MIAVGLSSSI LGCLLTLLVY TYCQRYQQQS HDATVIHPVS PAPLNTSITN
     HINKLDKYDS VEAIKAFNKN NLILEERNKY FNPHLTGKTY SNAYFTDLNN YDEY
//