PLXA1_MOUSE
ID PLXA1_MOUSE Reviewed; 1894 AA.
AC P70206; B2RQP7; Q5DTR0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Plexin-A1;
DE Short=Plex 1;
DE Short=Plexin-1;
DE Flags: Precursor;
GN Name=Plxna1; Synonyms=Kiaa4053;
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], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ, and ICR; TISSUE=Brain;
RX PubMed=8806667; DOI=10.1006/bbrc.1996.1388;
RA Kameyama T., Murakami Y., Suto F., Kawakami A., Takagi S., Hirata T.,
RA Fujisawa H.;
RT "Identification of a neuronal cell surface molecule, plexin, in mice.";
RL Biochem. Biophys. Res. Commun. 226:524-529(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 495-1894.
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND INTERACTION WITH NRP1; NRP2; SEMA3A AND SEMA3F.
RX PubMed=10520994; DOI=10.1016/s0092-8674(00)80062-8;
RA Takahashi T., Fournier A., Nakamura F., Wang L.-H., Murakami Y., Kalb R.G.,
RA Fujisawa H., Strittmatter S.M.;
RT "Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors.";
RL Cell 99:59-69(1999).
RN [5]
RP FUNCTION, AND INTERACTION WITH NRP1; NRP2; SEMA3A AND SEMA3C.
RX PubMed=10781943; DOI=10.1016/s0925-4773(00)00269-0;
RA Rohm B., Ottemeyer A., Lohrum M., Pueschel A.W.;
RT "Plexin/neuropilin complexes mediate repulsion by the axonal guidance
RT signal semaphorin 3A.";
RL Mech. Dev. 93:95-104(2000).
RN [6]
RP INTERACTION WITH PLXNB1, AND TISSUE SPECIFICITY.
RX PubMed=12559962; DOI=10.1016/s0006-291x(02)02966-2;
RA Usui H., Taniguchi M., Yokomizo T., Shimizu T.;
RT "Plexin-A1 and plexin-B1 specifically interact at their cytoplasmic
RT domains.";
RL Biochem. Biophys. Res. Commun. 300:927-931(2003).
RN [7]
RP INTERACTION WITH CRMP1; DPYSL2/CRMP2; DPYSL3/CRMP3 AND DPYSL4/CRMP4.
RX PubMed=14685275; DOI=10.1038/sj.emboj.7600021;
RA Deo R.C., Schmidt E.F., Elhabazi A., Togashi H., Burley S.K.,
RA Strittmatter S.M.;
RT "Structural bases for CRMP function in plexin-dependent semaphorin3A
RT signaling.";
RL EMBO J. 23:9-22(2004).
RN [8]
RP INTERACTION WITH SEMA6D AND KDR.
RX PubMed=14977921; DOI=10.1101/gad.1167304;
RA Toyofuku T., Zhang H., Kumanogoh A., Takegahara N., Suto F., Kamei J.,
RA Aoki K., Yabuki M., Hori M., Fujisawa H., Kikutani H.;
RT "Dual roles of Sema6D in cardiac morphogenesis through region-specific
RT association of its receptor, Plexin-A1, with off-track and vascular
RT endothelial growth factor receptor type 2.";
RL Genes Dev. 18:435-447(2004).
RN [9]
RP INTERACTION WITH FARP2 AND RND1, AND MUTAGENESIS OF 1266-LYS--LYS-1268.
RX PubMed=16286926; DOI=10.1038/nn1596;
RA Toyofuku T., Yoshida J., Sugimoto T., Zhang H., Kumanogoh A., Hori M.,
RA Kikutani H.;
RT "FARP2 triggers signals for Sema3A-mediated axonal repulsion.";
RL Nat. Neurosci. 8:1712-1719(2005).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1041.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Coreceptor for SEMA3A, SEMA3C, SEMA3F and SEMA6D. Necessary
CC for signaling by class 3 semaphorins and subsequent remodeling of the
CC cytoskeleton. Plays a role in axon guidance, invasive growth and cell
CC migration. Class 3 semaphorins bind to a complex composed of a
CC neuropilin and a plexin. The plexin modulates the affinity of the
CC complex for specific semaphorins, and its cytoplasmic domain is
CC required for the activation of down-stream signaling events in the
CC cytoplasm. {ECO:0000269|PubMed:10520994, ECO:0000269|PubMed:10781943}.
CC -!- SUBUNIT: Interacts directly with NRP1 and NRP2. Interacts with FARP2,
CC RND1 and KDR/VEGFR2. Binding of SEMA3A leads to dissociation of FARP2.
CC Interacts with CRMP1, DPYSL2/CRMP2, DPYSL3/CRMP3 and DPYSL4/CRMP4.
CC {ECO:0000269|PubMed:10520994, ECO:0000269|PubMed:10781943,
CC ECO:0000269|PubMed:12559962, ECO:0000269|PubMed:14685275,
CC ECO:0000269|PubMed:14977921, ECO:0000269|PubMed:16286926}.
CC -!- INTERACTION:
CC P70206; Q8BNV8: A530064D06Rik; NbExp=3; IntAct=EBI-771260, EBI-15687021;
CC P70206; P97333: Nrp1; NbExp=4; IntAct=EBI-771260, EBI-1555129;
CC P70206; Q99NH8: Trem2; NbExp=4; IntAct=EBI-771260, EBI-15982016;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12559962,
CC ECO:0000269|PubMed:8806667}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
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DR EMBL; D86948; BAA13188.1; -; mRNA.
DR EMBL; BC138023; AAI38024.1; -; mRNA.
DR EMBL; AK220460; BAD90489.1; -; mRNA.
DR CCDS; CCDS20344.1; -.
DR PIR; JC4980; JC4980.
DR RefSeq; NP_032907.1; NM_008881.2.
DR PDB; 3RYT; X-ray; 3.58 A; A/B=1269-1894.
DR PDB; 5L56; X-ray; 4.00 A; A=37-1236.
DR PDB; 5L59; X-ray; 6.00 A; A/B=37-1236.
DR PDB; 5L5C; X-ray; 6.00 A; A=37-1236.
DR PDB; 5L7N; X-ray; 2.20 A; A=861-1241.
DR PDBsum; 3RYT; -.
DR PDBsum; 5L56; -.
DR PDBsum; 5L59; -.
DR PDBsum; 5L5C; -.
DR PDBsum; 5L7N; -.
DR AlphaFoldDB; P70206; -.
DR SMR; P70206; -.
DR BioGRID; 202261; 12.
DR CORUM; P70206; -.
DR DIP; DIP-29745N; -.
DR IntAct; P70206; 6.
DR MINT; P70206; -.
DR STRING; 10090.ENSMUSP00000131840; -.
DR GlyConnect; 2589; 4 N-Linked glycans (4 sites).
DR GlyGen; P70206; 8 sites, 4 N-linked glycans (4 sites).
DR iPTMnet; P70206; -.
DR PhosphoSitePlus; P70206; -.
DR SwissPalm; P70206; -.
DR EPD; P70206; -.
DR MaxQB; P70206; -.
DR PaxDb; P70206; -.
DR PeptideAtlas; P70206; -.
DR PRIDE; P70206; -.
DR ProteomicsDB; 289628; -.
DR ABCD; P70206; 5 sequenced antibodies.
DR Antibodypedia; 2368; 185 antibodies from 27 providers.
DR DNASU; 18844; -.
DR Ensembl; ENSMUST00000049845; ENSMUSP00000063066; ENSMUSG00000030084.
DR Ensembl; ENSMUST00000163139; ENSMUSP00000131840; ENSMUSG00000030084.
DR GeneID; 18844; -.
DR KEGG; mmu:18844; -.
DR UCSC; uc009cwg.2; mouse.
DR CTD; 5361; -.
DR MGI; MGI:107685; Plxna1.
DR VEuPathDB; HostDB:ENSMUSG00000030084; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01050000244850; -.
DR HOGENOM; CLU_001436_2_0_1; -.
DR InParanoid; P70206; -.
DR OMA; WCVSERR; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; P70206; -.
DR TreeFam; TF312962; -.
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 Reactome; R-MMU-416700; Other semaphorin interactions.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 18844; 3 hits in 75 CRISPR screens.
DR PRO; PR:P70206; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P70206; protein.
DR Bgee; ENSMUSG00000030084; Expressed in undifferentiated genital tubercle and 257 other tissues.
DR ExpressionAtlas; P70206; baseline and differential.
DR Genevisible; P70206; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; IPI:MGI.
DR GO; GO:0060666; P:dichotomous subdivision of terminal units involved in salivary gland branching; IDA:MGI.
DR GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; IGI:ARUK-UCL.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:1990138; P:neuron projection extension; IGI:MGI.
DR GO; GO:0097485; P:neuron projection guidance; IMP:MGI.
DR GO; GO:0021628; P:olfactory nerve formation; IGI:ARUK-UCL.
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:0014910; P:regulation of smooth muscle cell migration; IMP:MGI.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central.
DR CDD; cd11271; Sema_plexin_A1; 1.
DR Gene3D; 1.10.506.10; -; 2.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR031148; Plexin.
DR InterPro; IPR042744; Plexin-A1_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; IPR041019; TIG1_plexin.
DR InterPro; IPR041362; TIG2_plexin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR22625; PTHR22625; 1.
DR Pfam; PF08337; Plexin_cytopl; 1.
DR Pfam; PF01437; PSI; 2.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF01833; TIG; 4.
DR Pfam; PF18020; TIG_2; 1.
DR Pfam; PF17960; TIG_plexin; 1.
DR SMART; SM00429; IPT; 4.
DR SMART; SM00423; PSI; 3.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF81296; SSF81296; 4.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Coiled coil; Disulfide bond; Glycoprotein;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1894
FT /note="Plexin-A1"
FT /id="PRO_0000232746"
FT TOPO_DOM 28..1242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1243..1263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1264..1894
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..510
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 862..957
FT /note="IPT/TIG 1"
FT DOMAIN 959..1043
FT /note="IPT/TIG 2"
FT DOMAIN 1046..1145
FT /note="IPT/TIG 3"
FT DOMAIN 1148..1234
FT /note="IPT/TIG 4"
FT COILED 1262..1315
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 699
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1041
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 1185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 93..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 128..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 284..405
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 300..356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 374..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 513..530
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 519..561
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 522..539
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 533..545
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 596..615
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT MUTAGEN 1266..1268
FT /note="KRK->AAA: Loss of interaction with FARP2."
FT /evidence="ECO:0000269|PubMed:16286926"
FT STRAND 863..868
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 870..873
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 879..887
FT /evidence="ECO:0007829|PDB:5L7N"
FT HELIX 891..893
FT /evidence="ECO:0007829|PDB:5L7N"
FT TURN 894..896
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 898..900
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 903..907
FT /evidence="ECO:0007829|PDB:5L7N"
FT HELIX 909..911
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 915..922
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 931..933
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 935..938
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 946..949
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 954..957
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 960..970
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 976..983
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 991..994
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 997..1004
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 1006..1012
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 1017..1028
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 1031..1043
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 1047..1057
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 1063..1070
FT /evidence="ECO:0007829|PDB:5L7N"
FT HELIX 1071..1073
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 1078..1083
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 1086..1096
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 1099..1103
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 1122..1127
FT /evidence="ECO:0007829|PDB:5L7N"
FT HELIX 1132..1134
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 1143..1145
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 1167..1173
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 1187..1189
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 1201..1206
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 1219..1221
FT /evidence="ECO:0007829|PDB:5L7N"
FT STRAND 1224..1226
FT /evidence="ECO:0007829|PDB:5L7N"
SQ SEQUENCE 1894 AA; 211099 MW; A8E6BB29C6824C94 CRC64;
MPLPPLSSRT LLLLLLLLLR GVWIAISSPP AGLGPQPAFR TFVASDWGLT HLVVHEQTGE
VYVGAVNRIY KLSGNLTLLR AHVTGPVEDN EKCYPPPSVQ SCPHGLGSTD NVNKLLLLDY
AANRLLACGS ASQGICQFLR LDDLFKLGEP HHRKEHYLSS VREAGSMAGV LIAGPPGQGQ
AKLFVGTPID GKSEYFPTLS SRRLMANEED ADMFGFVYQD EFVSSQLKIP SDTLSKFPAF
DIYYVYSFRS EQFVYYLTLQ LDTQLTSPDA AGEHFFTSKI VRLCVNDPKF YSYVEFPIGC
EQAGVEYRLV QDAYLSRPGQ ALAKQLGLAE DEEVLFTVFA QGQKNRVKPP KESALCLFTL
RAIKEKIKER IQSCYRGEGK LSLPWLLNKE LGCINSPLQI DDDFCGQDFN QPLGGTVTIE
GTPLFVDKED GLTAVAAYDY QGRTVVFAGT RSGRIRKILV DLANPSGRPA LAYESVVAQE
GNPILRDLVL SPNRQYLYAM TEKQVTQVPV ESCVQYTSCE LCLGSRDPHC GWCVLHSICS
RQDACERAEE PQRFASDLLQ CVQLTVQPRN VSVTMSQVPL VLQAWNVPDL SAGVNCSFED
FTETESILED GRIHCHSPSA REVAPITQGQ GDQRVVKLYL KSKETGKKFA SVDFVFYNCS
VHQSCLACVN GSFPCHWCKY RHVCTNNAAD CAFLEGRVNM SEDCPQILPS THIYVPVGVV
KPITLAARNL PQPQSGQRGY ECLFHIPGSP ARVTALRFNS SSLQCQNSSY SYEGNDVSDL
PVNLSVVWNG NFVIDNPQNI QAHLYKCPAL RQSCGLCLKA DPRFECGWCV AERRCSLRHH
CPADSPASWM HAHHGSSRCT DPKILKLSPE TGPRQGGTRL TITGENLGLR FEDVRLGVHV
GKVLCSPVES EYISAEQIVC EIGDASTLRA HDALVEVCVR DCSLHYRALS PKRFTFVTPT
FYRVSPSRGP LSGGTWIGIE GSHLNAGSDV AVSIGGRPCS FSWRNSREIR CLTPPGHTPG
SAPIVININR AQLSNPEVKY NYTEDPTILR IDPEWSINSG GTLLTVTGTN LATVREPRIR
AKYGGIEREN SCMVYNDTTM VCRAPSIDNP KRSPPELGER PDEIGFIMDN VRTLLVLNSS
SFLYYPDPVL EPLSPTGLLE LKPSSPLILK GRNLLPPAPG NSRLNYTVLI GSTPCILTVS
ETQLLCEAPN LTGQHKVTVR AGGFEFSPGM LQVYSDSLLT LPAIVGIGGG GGLLLLVIVA
VLIAYKRKSR DADRTLKRLQ LQMDNLESRV ALECKEAFAE LQTDIHELTS DLDGAGIPFL
DYRTYAMRVL FPGIEDHPVL KEMEVQANVE KSLTLFGQLL TKKHFLLTFI RTLEAQRSFS
MRDRGNVASL IMTALQGEME YATGVLKQLL SDLIEKNLES KNHPKLLLRR TESVAEKMLT
NWFTFLLYKF LKECAGEPLF MLYCAIKQQM EKGPIDAITG EARYSLSEDK LIRQQIDYKT
LTLNCVNPEH ENAPEVPVKG LNCDTVTQVK EKLLDAVYKG VPYSQRPKAG DMDLEWRQGR
MARIILQDED VTTKIDNDWK RLNTLAHYQV TDGSSVALVP KQTSAYNISN SSTFTKSLSR
YESMLRTASS PDSLRSRTPM ITPDLESGTK LWHLVKNHDH LDQREGDRGS KMVSEIYLTR
LLATKGTLQK FVDDLFETIF STAHRGSALP LAIKYMFDFL DEQADKHQIH DSDVRHTWKS
NCLPLRFWVN VIKNPQFVFD IHKNSITDAC LSVVAQTFMD SCSTSEHKLG KDSPSNKLLY
AKDIPNYKSW VERYYADIAK MPAISDQDMS AYLAEQSRLH LSQFNSMSAL HEIYSYIAKY
KDEILVALEK DEQARRQRLR SKLEQVVDTM ALSS
