SEM3A_MOUSE
ID SEM3A_MOUSE Reviewed; 772 AA.
AC O08665; E9QK85; Q5BL08; Q62180; Q62215;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Semaphorin-3A;
DE AltName: Full=Semaphorin III;
DE Short=Sema III;
DE AltName: Full=Semaphorin-D;
DE Short=Sema D;
DE Flags: Precursor;
GN Name=Sema3a; Synonyms=Semad, SemD;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NMRI; TISSUE=Embryo;
RX PubMed=7748561; DOI=10.1016/0896-6273(95)90332-1;
RA Pueschel A.W., Adams R.H., Betz H.;
RT "Murine semaphorin D/collapsin is a member of a diverse gene family and
RT creates domains inhibitory for axonal extension.";
RL Neuron 14:941-948(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9331345; DOI=10.1016/s0896-6273(00)80368-2;
RA Taniguchi M., Yuasa S., Fujisawa H., Naruse I., Saga S., Mishina M.,
RA Yagi T.;
RT "Disruption of semaphorin III/D gene causes severe abnormality in
RT peripheral nerve projection.";
RL Neuron 19:519-530(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kimura T., Fishman M.C.;
RT "cDNA sequence of mouse collapsin/semaphorin III.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 107-772.
RC TISSUE=Fetal brain;
RX PubMed=7748562; DOI=10.1016/0896-6273(95)90333-x;
RA Messersmith E.K., Leonardo E.D., Shatz C.J., Tessier-Lavigne M.,
RA Goodman C.S., Kolodkin A.L.;
RT "Semaphorin III can function as a selective chemorepellent to pattern
RT sensory projections in the spinal cord.";
RL Neuron 14:949-959(1995).
RN [7]
RP INTERACTION WITH PLXND1.
RX PubMed=15239958; DOI=10.1016/j.devcel.2004.06.002;
RA Gitler A.D., Lu M.M., Epstein J.A.;
RT "PlexinD1 and semaphorin signaling are required in endothelial cells for
RT cardiovascular development.";
RL Dev. Cell 7:107-116(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 26-520, GLYCOSYLATION AT ASN-53
RP AND ASN-125, AND DISULFIDE BONDS.
RX PubMed=12925274; DOI=10.1016/s0896-6273(03)00502-6;
RA Antipenko A., Himanen J.P., van Leyen K., Nardi-Dei V., Lesniak J.,
RA Barton W.A., Rajashankar K.R., Lu M., Hoemme C., Puschel A.W.,
RA Nikolov D.B.;
RT "Structure of the semaphorin-3A receptor binding module.";
RL Neuron 39:589-598(2003).
CC -!- FUNCTION: Plays a role in growth cones guidance. May function to
CC pattern sensory projections by selectively repelling axons that
CC normally terminate dorsally. Involved in the development of the
CC olfactory system and in neuronal control of puberty (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PXND1. {ECO:0000269|PubMed:15239958}.
CC -!- INTERACTION:
CC O08665; P97333: Nrp1; NbExp=3; IntAct=EBI-8586029, EBI-1555129;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DEVELOPMENTAL STAGE: Expressed early in embryonic development (11 dpc)
CC in distinct regions of the neuroectoderm and mesoderm. Expression
CC became more extensive at later stages.
CC -!- DOMAIN: Strong binding to neuropilin is mediated by the carboxy third
CC of the protein.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; X85993; CAA59985.1; -; mRNA.
DR EMBL; D85028; BAA19773.1; -; mRNA.
DR EMBL; L41541; AAL77611.1; -; mRNA.
DR EMBL; AC022368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057588; AAH57588.1; -; mRNA.
DR EMBL; BC090844; AAH90844.1; -; mRNA.
DR EMBL; L40484; AAA73934.1; -; mRNA.
DR CCDS; CCDS19092.1; -.
DR PIR; I48747; I48747.
DR PIR; I58169; I58169.
DR RefSeq; NP_001230001.1; NM_001243072.1.
DR RefSeq; NP_001230002.1; NM_001243073.1.
DR RefSeq; NP_033178.2; NM_009152.4.
DR RefSeq; XP_006503620.1; XM_006503557.3.
DR RefSeq; XP_006503621.1; XM_006503558.3.
DR RefSeq; XP_006503622.1; XM_006503559.1.
DR RefSeq; XP_011238967.1; XM_011240665.2.
DR PDB; 1Q47; X-ray; 2.80 A; A/B=26-520.
DR PDB; 4GZ8; X-ray; 3.30 A; A/B=21-569.
DR PDB; 4GZA; X-ray; 7.00 A; G=21-555.
DR PDB; 7M0R; EM; 3.70 A; C/D=21-569.
DR PDBsum; 1Q47; -.
DR PDBsum; 4GZ8; -.
DR PDBsum; 4GZA; -.
DR PDBsum; 7M0R; -.
DR AlphaFoldDB; O08665; -.
DR SMR; O08665; -.
DR BioGRID; 203161; 7.
DR DIP; DIP-59997N; -.
DR IntAct; O08665; 2.
DR MINT; O08665; -.
DR STRING; 10090.ENSMUSP00000030714; -.
DR GlyGen; O08665; 3 sites.
DR iPTMnet; O08665; -.
DR PhosphoSitePlus; O08665; -.
DR MaxQB; O08665; -.
DR PaxDb; O08665; -.
DR PeptideAtlas; O08665; -.
DR PRIDE; O08665; -.
DR ProteomicsDB; 256770; -.
DR Antibodypedia; 29608; 325 antibodies from 32 providers.
DR DNASU; 20346; -.
DR GeneID; 20346; -.
DR KEGG; mmu:20346; -.
DR UCSC; uc008wmb.3; mouse.
DR CTD; 10371; -.
DR MGI; MGI:107558; Sema3a.
DR VEuPathDB; HostDB:ENSMUSG00000028883; -.
DR eggNOG; KOG3611; Eukaryota.
DR InParanoid; O08665; -.
DR OrthoDB; 297290at2759; -.
DR PhylomeDB; O08665; -.
DR TreeFam; TF316102; -.
DR Reactome; R-MMU-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-MMU-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-MMU-399956; CRMPs in Sema3A signaling.
DR BioGRID-ORCS; 20346; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Sema3a; mouse.
DR EvolutionaryTrace; O08665; -.
DR PRO; PR:O08665; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O08665; protein.
DR ExpressionAtlas; O08665; baseline and differential.
DR Genevisible; O08665; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045499; F:chemorepellent activity; IDA:MGI.
DR GO; GO:0038191; F:neuropilin binding; IPI:BHF-UCL.
DR GO; GO:0030215; F:semaphorin receptor binding; IPI:MGI.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0048675; P:axon extension; IDA:MGI.
DR GO; GO:0048846; P:axon extension involved in axon guidance; IDA:MGI.
DR GO; GO:0007411; P:axon guidance; IDA:MGI.
DR GO; GO:0007413; P:axonal fasciculation; IMP:MGI.
DR GO; GO:0060385; P:axonogenesis involved in innervation; IMP:BHF-UCL.
DR GO; GO:0150020; P:basal dendrite arborization; IGI:ARUK-UCL.
DR GO; GO:0021785; P:branchiomotor neuron axon guidance; IMP:ParkinsonsUK-UCL.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR GO; GO:0060666; P:dichotomous subdivision of terminal units involved in salivary gland branching; IDA:MGI.
DR GO; GO:0010631; P:epithelial cell migration; IDA:MGI.
DR GO; GO:0021612; P:facial nerve structural organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903375; P:facioacoustic ganglion development; IMP:ParkinsonsUK-UCL.
DR GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; IMP:BHF-UCL.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:ParkinsonsUK-UCL.
DR GO; GO:0050919; P:negative chemotaxis; IGI:MGI.
DR GO; GO:0030517; P:negative regulation of axon extension; IDA:MGI.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IDA:MGI.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IDA:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR GO; GO:0021675; P:nerve development; IMP:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; IGI:MGI.
DR GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903045; P:neural crest cell migration involved in sympathetic nervous system development; IMP:BHF-UCL.
DR GO; GO:0001764; P:neuron migration; IMP:BHF-UCL.
DR GO; GO:0021772; P:olfactory bulb development; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:2000020; P:positive regulation of male gonad development; IMP:BHF-UCL.
DR GO; GO:2001224; P:positive regulation of neuron migration; IGI:BHF-UCL.
DR GO; GO:0048841; P:regulation of axon extension involved in axon guidance; IDA:UniProtKB.
DR GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IGI:MGI.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IMP:ParkinsonsUK-UCL.
DR GO; GO:1902285; P:semaphorin-plexin signaling pathway involved in neuron projection guidance; IMP:BHF-UCL.
DR GO; GO:0061549; P:sympathetic ganglion development; IMP:BHF-UCL.
DR GO; GO:0097490; P:sympathetic neuron projection extension; IMP:BHF-UCL.
DR GO; GO:0097491; P:sympathetic neuron projection guidance; IMP:BHF-UCL.
DR GO; GO:0061551; P:trigeminal ganglion development; IMP:ParkinsonsUK-UCL.
DR GO; GO:0021637; P:trigeminal nerve structural organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0036486; P:ventral trunk neural crest cell migration; IMP:ParkinsonsUK-UCL.
DR CDD; cd11249; Sema_3A; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR041416; IL-1RAcP-like_ig.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR042820; Sema3A_sema.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR027231; Semaphorin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR11036; PTHR11036; 1.
DR Pfam; PF18452; Ig_6; 1.
DR Pfam; PF01403; Sema; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Neurogenesis; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..772
FT /note="Semaphorin-3A"
FT /id="PRO_0000032304"
FT DOMAIN 31..514
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 579..665
FT /note="Ig-like C2-type"
FT REGION 729..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12925274"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12925274"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..114
FT /evidence="ECO:0000269|PubMed:12925274"
FT DISULFID 132..141
FT /evidence="ECO:0000269|PubMed:12925274"
FT DISULFID 269..381
FT /evidence="ECO:0000269|PubMed:12925274"
FT DISULFID 293..341
FT /evidence="ECO:0000269|PubMed:12925274"
FT DISULFID 517..535
FT /evidence="ECO:0000250"
FT DISULFID 650..723
FT /evidence="ECO:0000250"
FT CONFLICT 193
FT /note="D -> N (in Ref. 6; AAA73934)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="H -> D (in Ref. 1; CAA59985)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="D -> G (in Ref. 1; CAA59985)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="F -> L (in Ref. 6; AAA73934)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="A -> G (in Ref. 1; CAA59985)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="I -> V (in Ref. 1; CAA59985, 2; BAA19773, 3;
FT AAL77611, 5; AAH57588/AAH90844 and 6; AAA73934)"
FT /evidence="ECO:0000305"
FT CONFLICT 571..572
FT /note="QH -> ED (in Ref. 1; CAA59985)"
FT /evidence="ECO:0000305"
FT CONFLICT 616..620
FT /note="EDRKE -> RRSKR (in Ref. 1; CAA59985)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="R -> K (in Ref. 6; AAA73934)"
FT /evidence="ECO:0000305"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:4GZ8"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:1Q47"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1Q47"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:1Q47"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:1Q47"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:4GZ8"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:1Q47"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:4GZ8"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 199..208
FT /evidence="ECO:0007829|PDB:1Q47"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1Q47"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 242..250
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 261..269
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 307..314
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:1Q47"
FT HELIX 345..352
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:4GZ8"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:1Q47"
FT HELIX 397..404
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:1Q47"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 421..429
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 431..440
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 445..453
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 458..462
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 491..495
FT /evidence="ECO:0007829|PDB:1Q47"
FT TURN 496..499
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 500..507
FT /evidence="ECO:0007829|PDB:1Q47"
FT STRAND 509..514
FT /evidence="ECO:0007829|PDB:1Q47"
FT HELIX 517..519
FT /evidence="ECO:0007829|PDB:4GZ8"
FT HELIX 524..529
FT /evidence="ECO:0007829|PDB:4GZ8"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:4GZ8"
FT TURN 564..566
FT /evidence="ECO:0007829|PDB:4GZ8"
SQ SEQUENCE 772 AA; 88813 MW; C6533FF007018D0C CRC64;
MGWFTGIACL FWGVLLTARA NYANGKNNVP RLKLSYKEML ESNNVITFNG LANSSSYHTF
LLDEERSRLY VGAKDHIFSF NLVNIKDFQK IVWPVSYTRR DECKWAGKDI LKECANFIKV
LEAYNQTHLY ACGTGAFHPI CTYIEVGHHP EDNIFKLQDS HFENGRGKSP YDPKLLTASL
LIDGELYSGT AADFMGRDFA IFRTLGHHHP IRTEQHDSRW LNDPRFISAH LIPESDNPED
DKVYFFFREN AIDGEHSGKA THARIGQICK NDFGGHRSLV NKWTTFLKAR LICSVPGPNG
IDTHFDELQD VFLMNSKDPK NPIVYGVFTT SSNIFKGSAV CMYSMSDVRR VFLGPYAHRD
GPNYQWVPYQ GRVPYPRPGT CPSKTFGGFD STKDLPDDVI TFARSHPAMY NPVFPINNRP
IMIKTDVNYQ FTQIVVDRVD AEDGQYDVMF IGTDVGTVLK VVSVPKETWH DLEEILLEEM
TVFREPTTIS AMELSTKQQQ LYIGSTAGVA QLPLHRCDIY GKACAECCLA RDPYCAWDGS
SCSRYFPTAK RRTRRQDIRN GDPLTHCSDL QHHDNHHGPS LEERIIYGVE NSSTFLECSP
KSQRALVYWQ FQRRNEDRKE EIRMGDHIIR TEQGLLLRSL QKKDSGNYLC HAVEHGFMQT
LLKVTLEVID TEHLEELLHK DDDGDGSKIK EMSSSMTPSQ KVWYRDFMQL INHPNLNTMD
EFCEQVWKRD RKQRRQRPGH SQGSSNKWKH MQESKKGRNR RTHEFERAPR SV
