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 27-MAR-2024, entry version 174. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-21442; -. DR SMR; O60486; -. DR BioGRID; 115456; 12. DR CORUM; O60486; -. DR IntAct; O60486; 4. DR MINT; O60486; -. DR STRING; 9606.ENSP00000258526; -. DR GlyConnect; 725; 8 N-Linked glycans (5 sites). DR GlyCosmos; O60486; 17 sites, 14 glycans. 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; 9606-ENSP00000258526; -. DR PeptideAtlas; O60486; -. DR ProteomicsDB; 49424; -. DR Pumba; O60486; -. DR Antibodypedia; 30073; 143 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 AGR; HGNC:9106; -. 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; ENSGT01020000230394; -. DR HOGENOM; CLU_004205_0_0_1; -. DR InParanoid; O60486; -. DR OMA; QFDGGSC; -. DR OrthoDB; 1387371at2759; -. 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; 10 hits in 1149 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 196 other cell types or tissues. DR ExpressionAtlas; O60486; baseline and differential. DR GO; GO:0150053; C:cerebellar climbing fiber to Purkinje cell synapse; IEA:Ensembl. 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:1905806; P:regulation of synapse pruning; IEA:Ensembl. DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central. DR CDD; cd00102; IPT; 2. DR CDD; cd12789; RasGAP_plexin_C1; 1. DR CDD; cd11246; Sema_plexin_C1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR046800; Plexin_RBD. 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; PLEXIN; 1. DR PANTHER; PTHR22625:SF4; PLEXIN-C1; 1. DR Pfam; PF08337; Plexin_cytopl; 1. DR Pfam; PF20170; Plexin_RBD; 1. 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; SSF48350; GTPase activation domain, GAP; 1. DR SUPFAM; SSF103575; Plexin repeat; 1. DR SUPFAM; SSF101912; Sema domain; 1. DR PROSITE; PS51004; SEMA; 1. DR Genevisible; O60486; HS. 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 //