PLXC1_HUMAN
ID PLXC1_HUMAN Reviewed; 1568 AA.
AC O60486; Q59H25;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Plexin-C1;
DE AltName: Full=Virus-encoded semaphorin protein receptor;
DE AltName: CD_antigen=CD232;
DE Flags: Precursor;
GN Name=PLXNC1; Synonyms=VESPR;
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], IDENTIFICATION BY MASS SPECTROMETRY,
RP GLYCOSYLATION, INTERACTION WITH VACCINIA VIRUS PROTEIN A39R AND HERPESVIRUS
RP SEMA, AND TISSUE SPECIFICITY.
RC TISSUE=Foreskin;
RX PubMed=9586637; DOI=10.1016/s1074-7613(00)80552-x;
RA Comeau M.R., Johnson R., DuBose R.F., Petersen M., Gearing P.,
RA VandenBos T., Park L., Farrah T., Buller R.M., Cohen J.I., Strockbine L.D.,
RA Rauch C., Spriggs M.K.;
RT "A poxvirus-encoded semaphorin induces cytokine production from monocytes
RT and binds to a novel cellular semaphorin receptor, VESPR.";
RL Immunity 8:473-482(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 358-1568.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1198-1305.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the ubiquitin like domain of PLXNC1.";
RL Submitted (DEC-2009) to the PDB data bank.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 35-507 IN COMPLEXES WITH SEMA7A
RP AND SMALLPOX VIRUS A39R, FUNCTION, SUBUNIT, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-86; ASN-141; ASN-149; ASN-241; ASN-252; ASN-386 AND
RP ASN-407.
RX PubMed=20727575; DOI=10.1016/j.cell.2010.07.040;
RA Liu H., Juo Z.S., Shim A.H., Focia P.J., Chen X., Garcia K.C., He X.;
RT "Structural basis of semaphorin-plexin recognition and viral mimicry from
RT Sema7A and A39R complexes with PlexinC1.";
RL Cell 142:749-761(2010).
CC -!- FUNCTION: Receptor for SEMA7A, for smallpox semaphorin A39R, vaccinia
CC virus semaphorin A39R and for herpesvirus Sema protein. Binding of
CC semaphorins triggers cellular responses leading to the rearrangement of
CC the cytoskeleton and to secretion of IL6 and IL8 (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:20727575}.
CC -!- SUBUNIT: Monomer. Homodimer. Interacts with SEMA7A.
CC {ECO:0000269|PubMed:20727575, ECO:0000269|PubMed:9586637}.
CC -!- INTERACTION:
CC O60486; O75326: SEMA7A; NbExp=4; IntAct=EBI-2927384, EBI-1753538;
CC O60486; Q8JL80: EVM139; Xeno; NbExp=3; IntAct=EBI-2927384, EBI-2927425;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, lung, spleen and
CC placenta. {ECO:0000269|PubMed:9586637}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20727575,
CC ECO:0000269|PubMed:9586637}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
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DR EMBL; AF030339; AAC18823.1; -; mRNA.
DR EMBL; AB208934; BAD92171.1; -; mRNA.
DR CCDS; CCDS9049.1; -.
DR PIR; T09074; T09074.
DR RefSeq; NP_005752.1; NM_005761.2.
DR PDB; 3KUZ; X-ray; 2.30 A; A/B=1198-1305.
DR PDB; 3NVN; X-ray; 2.26 A; B=35-507.
DR PDB; 3NVQ; X-ray; 2.40 A; B/F=35-507.
DR PDB; 6VXK; EM; 3.10 A; B/D=35-1568.
DR PDBsum; 3KUZ; -.
DR PDBsum; 3NVN; -.
DR PDBsum; 3NVQ; -.
DR PDBsum; 6VXK; -.
DR AlphaFoldDB; O60486; -.
DR SMR; O60486; -.
DR BioGRID; 115456; 12.
DR CORUM; O60486; -.
DR IntAct; O60486; 3.
DR MINT; O60486; -.
DR STRING; 9606.ENSP00000258526; -.
DR GlyConnect; 725; 8 N-Linked glycans (5 sites).
DR GlyGen; O60486; 21 sites, 14 N-linked glycans (5 sites).
DR iPTMnet; O60486; -.
DR PhosphoSitePlus; O60486; -.
DR BioMuta; PLXNC1; -.
DR EPD; O60486; -.
DR jPOST; O60486; -.
DR MassIVE; O60486; -.
DR MaxQB; O60486; -.
DR PaxDb; O60486; -.
DR PeptideAtlas; O60486; -.
DR PRIDE; O60486; -.
DR ProteomicsDB; 49424; -.
DR Antibodypedia; 30073; 121 antibodies from 22 providers.
DR DNASU; 10154; -.
DR Ensembl; ENST00000258526.9; ENSP00000258526.4; ENSG00000136040.9.
DR GeneID; 10154; -.
DR KEGG; hsa:10154; -.
DR MANE-Select; ENST00000258526.9; ENSP00000258526.4; NM_005761.3; NP_005752.1.
DR UCSC; uc001tdc.3; human.
DR CTD; 10154; -.
DR DisGeNET; 10154; -.
DR GeneCards; PLXNC1; -.
DR HGNC; HGNC:9106; PLXNC1.
DR HPA; ENSG00000136040; Low tissue specificity.
DR MIM; 604259; gene.
DR neXtProt; NX_O60486; -.
DR OpenTargets; ENSG00000136040; -.
DR PharmGKB; PA33432; -.
DR VEuPathDB; HostDB:ENSG00000136040; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01050000244850; -.
DR HOGENOM; CLU_004205_0_0_1; -.
DR InParanoid; O60486; -.
DR OMA; LFHGENK; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; O60486; -.
DR TreeFam; TF312962; -.
DR PathwayCommons; O60486; -.
DR Reactome; R-HSA-416700; Other semaphorin interactions.
DR SignaLink; O60486; -.
DR SIGNOR; O60486; -.
DR BioGRID-ORCS; 10154; 8 hits in 1065 CRISPR screens.
DR ChiTaRS; PLXNC1; human.
DR EvolutionaryTrace; O60486; -.
DR GenomeRNAi; 10154; -.
DR Pharos; O60486; Tbio.
DR PRO; PR:O60486; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O60486; protein.
DR Bgee; ENSG00000136040; Expressed in buccal mucosa cell and 194 other tissues.
DR ExpressionAtlas; O60486; baseline and differential.
DR Genevisible; O60486; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR GO; GO:0017154; F:semaphorin receptor activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central.
DR CDD; cd11246; Sema_plexin_C1; 1.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR031148; Plexin.
DR InterPro; IPR041853; Plexin-C1_Sema.
DR InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR22625; PTHR22625; 1.
DR Pfam; PF08337; Plexin_cytopl; 2.
DR Pfam; PF01437; PSI; 1.
DR Pfam; PF01833; TIG; 2.
DR SMART; SM00429; IPT; 2.
DR SMART; SM00423; PSI; 2.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..1568
FT /note="Plexin-C1"
FT /id="PRO_0000232749"
FT TOPO_DOM 35..944
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 945..965
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 966..1568
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..452
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZC2"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20727575"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20727575"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20727575"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20727575"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20727575"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20727575"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20727575"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 771
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 796
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 871
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 890
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 64..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:20727575"
FT DISULFID 156..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:20727575"
FT DISULFID 226..354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:20727575"
FT DISULFID 283..329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:20727575"
FT DISULFID 455..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:20727575"
FT DISULFID 461..506
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:20727575"
FT DISULFID 464..481
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:20727575"
FT DISULFID 475..487
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:20727575"
FT VARIANT 1499
FT /note="E -> K (in dbSNP:rs11107500)"
FT /id="VAR_050602"
FT CONFLICT 671
FT /note="K -> R (in Ref. 2; BAD92171)"
FT /evidence="ECO:0000305"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:3NVN"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:3NVN"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:3NVN"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:3NVN"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 203..212
FT /evidence="ECO:0007829|PDB:3NVN"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 241..252
FT /evidence="ECO:0007829|PDB:3NVN"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 263..272
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:3NVN"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 305..311
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 325..332
FT /evidence="ECO:0007829|PDB:3NVN"
FT HELIX 333..339
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:3NVN"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 371..394
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 397..403
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:3NVN"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:3NVQ"
FT HELIX 461..465
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 472..475
FT /evidence="ECO:0007829|PDB:3NVN"
FT TURN 476..479
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 480..483
FT /evidence="ECO:0007829|PDB:3NVN"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:3NVQ"
FT TURN 499..501
FT /evidence="ECO:0007829|PDB:3NVN"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 532..536
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 574..580
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 582..585
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 663..668
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 670..673
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 677..685
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 694..698
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 700..703
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 706..709
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 718..723
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 730..736
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 738..741
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 743..751
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 756..761
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 763..765
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 770..777
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 784..788
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 803..809
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 821..828
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 831..841
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 846..849
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 859..863
FT /evidence="ECO:0007829|PDB:6VXK"
FT HELIX 874..876
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 877..880
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 889..893
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 905..909
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 926..929
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 932..934
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 1198..1205
FT /evidence="ECO:0007829|PDB:3KUZ"
FT STRAND 1219..1225
FT /evidence="ECO:0007829|PDB:3KUZ"
FT HELIX 1230..1245
FT /evidence="ECO:0007829|PDB:3KUZ"
FT HELIX 1253..1255
FT /evidence="ECO:0007829|PDB:3KUZ"
FT STRAND 1256..1262
FT /evidence="ECO:0007829|PDB:3KUZ"
FT STRAND 1265..1269
FT /evidence="ECO:0007829|PDB:3KUZ"
FT HELIX 1290..1292
FT /evidence="ECO:0007829|PDB:3KUZ"
FT STRAND 1299..1304
FT /evidence="ECO:0007829|PDB:3KUZ"
SQ SEQUENCE 1568 AA; 175742 MW; EA0CE5519BEF925D CRC64;
MEVSRRKAPP RPPRPAAPLP LLAYLLALAA PGRGADEPVW RSEQAIGAIA ASQEDGVFVA
SGSCLDQLDY SLEHSLSRLY RDQAGNCTEP VSLAPPARPR PGSSFSKLLL PYREGAAGLG
GLLLTGWTFD RGACEVRPLG NLSRNSLRNG TEVVSCHPQG STAGVVYRAG RNNRWYLAVA
ATYVLPEPET ASRCNPAASD HDTAIALKDT EGRSLATQEL GRLKLCEGAG SLHFVDAFLW
NGSIYFPYYP YNYTSGAATG WPSMARIAQS TEVLFQGQAS LDCGHGHPDG RRLLLSSSLV
EALDVWAGVF SAAAGEGQER RSPTTTALCL FRMSEIQARA KRVSWDFKTA ESHCKEGDQP
ERVQPIASST LIHSDLTSVY GTVVMNRTVL FLGTGDGQLL KVILGENLTS NCPEVIYEIK
EETPVFYKLV PDPVKNIYIY LTAGKEVRRI RVANCNKHKS CSECLTATDP HCGWCHSLQR
CTFQGDCVHS ENLENWLDIS SGAKKCPKIQ IIRSSKEKTT VTMVGSFSPR HSKCMVKNVD
SSRELCQNKS QPNRTCTCSI PTRATYKDVS VVNVMFSFGS WNLSDRFNFT NCSSLKECPA
CVETGCAWCK SARRCIHPFT ACDPSDYERN QEQCPVAVEK TSGGGRPKEN KGNRTNQALQ
VFYIKSIEPQ KVSTLGKSNV IVTGANFTRA SNITMILKGT STCDKDVIQV SHVLNDTHMK
FSLPSSRKEM KDVCIQFDGG NCSSVGSLSY IALPHCSLIF PATTWISGGQ NITMMGRNFD
VIDNLIISHE LKGNINVSEY CVATYCGFLA PSLKSSKVRT NVTVKLRVQD TYLDCGTLQY
REDPRFTGYR VESEVDTELE VKIQKENDNF NISKKDIEIT LFHGENGQLN CSFENITRNQ
DLTTILCKIK GIKTASTIAN SSKKVRVKLG NLELYVEQES VPSTWYFLIV LPVLLVIVIF
AAVGVTRHKS KELSRKQSQQ LELLESELRK EIRDGFAELQ MDKLDVVDSF GTVPFLDYKH
FALRTFFPES GGFTHIFTED MHNRDANDKN ESLTALDALI CNKSFLVTVI HTLEKQKNFS
VKDRCLFASF LTIALQTKLV YLTSILEVLT RDLMEQCSNM QPKLMLRRTE SVVEKLLTNW
MSVCLSGFLR ETVGEPFYLL VTTLNQKINK GPVDVITCKA LYTLNEDWLL WQVPEFSTVA
LNVVFEKIPE NESADVCRNI SVNVLDCDTI GQAKEKIFQA FLSKNGSPYG LQLNEIGLEL
QMGTRQKELL DIDSSSVILE DGITKLNTIG HYEISNGSTI KVFKKIANFT SDVEYSDDHC
HLILPDSEAF QDVQGKRHRG KHKFKVKEMY LTKLLSTKVA IHSVLEKLFR SIWSLPNSRA
PFAIKYFFDF LDAQAENKKI TDPDVVHIWK TNSLPLRFWV NILKNPQFVF DIKKTPHIDG
CLSVIAQAFM DAFSLTEQQL GKEAPTNKLL YAKDIPTYKE EVKSYYKAIR DLPPLSSSEM
EEFLTQESKK HENEFNEEVA LTEIYKYIVK YFDEILNKLE RERGLEEAQK QLLHVKVLFD
EKKKCKWM
