PLXA4_MOUSE
ID PLXA4_MOUSE Reviewed; 1893 AA.
AC Q80UG2; E9QN64; Q5DTW8; Q8BKK9;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Plexin-A4;
DE Flags: Precursor;
GN Name=Plxna4; Synonyms=Kiaa1550;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryonic brain;
RX PubMed=12591607; DOI=10.1016/s0925-4773(02)00421-5;
RA Suto F., Murakami Y., Nakamura F., Goshima Y., Fujisawa H.;
RT "Identification and characterization of a novel mouse plexin, plexin-A4.";
RL Mech. Dev. 120:385-396(2003).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1042-1893.
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1695-1893.
RC TISSUE=Fetal 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=18804103; DOI=10.1016/j.ydbio.2008.08.020;
RA Schwarz Q., Waimey K.E., Golding M., Takamatsu H., Kumanogoh A.,
RA Fujisawa H., Cheng H.J., Ruhrberg C.;
RT "Plexin A3 and plexin A4 convey semaphorin signals during facial nerve
RT development.";
RL Dev. Biol. 324:1-9(2008).
RN [7]
RP DISRUPTION PHENOTYPE, INTERACTION WITH NRP1 AND NRP2, AND FUNCTION.
RX PubMed=18262512; DOI=10.1016/j.ydbio.2008.01.002;
RA Waimey K.E., Huang P.H., Chen M., Cheng H.J.;
RT "Plexin-A3 and plexin-A4 restrict the migration of sympathetic neurons but
RT not their neural crest precursors.";
RL Dev. Biol. 315:448-458(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
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. Necessary for signaling by class 3
CC semaphorins and subsequent remodeling of the cytoskeleton. Plays a role
CC in axon guidance in the developing nervous system. Class 3 semaphorins
CC bind to a complex composed of a neuropilin and a plexin. The plexin
CC modulates the affinity of the complex for specific semaphorins, and its
CC cytoplasmic domain is required for the activation of down-stream
CC signaling events in the cytoplasm. {ECO:0000269|PubMed:12591607,
CC ECO:0000269|PubMed:18262512}.
CC -!- SUBUNIT: Interacts with NRP1 and NRP2. {ECO:0000269|PubMed:18262512}.
CC -!- INTERACTION:
CC Q80UG2; O35464: Sema6a; NbExp=3; IntAct=EBI-8057809, EBI-8057848;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the developing nervous system. Widely
CC expressed in both the central and peripheral nervous systems. Expressed
CC in the peripheral ganglia, somatosensory, olfactory, visual, auditory
CC and equilibrium systems. {ECO:0000269|PubMed:12591607}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice exhibit
CC defasciculation of the facial branchiomotor nerve and of the ophthalmic
CC branch of the trigeminus, with variable severity. In mice lacking both
CC Plxna3 and Plxna4, migrating neurons do not show the normal response to
CC Sema3A and Sema3F and do not migrate away from these semaphorins (in
CC vitro). {ECO:0000269|PubMed:18262512, ECO:0000269|PubMed:18804103}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC56599.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB073228; BAC56599.1; ALT_INIT; mRNA.
DR EMBL; AC153629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC158678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK051614; BAC34692.1; -; mRNA.
DR EMBL; AK220402; BAD90257.1; -; mRNA.
DR CCDS; CCDS19985.2; -.
DR RefSeq; NP_786926.2; NM_175750.3.
DR PDB; 5L5K; X-ray; 7.50 A; A=36-1229.
DR PDB; 5L5L; X-ray; 8.00 A; A/B=36-1229.
DR PDB; 5L5M; X-ray; 8.00 A; A=36-1229.
DR PDB; 5L5N; X-ray; 8.50 A; A=36-1229.
DR PDB; 7M0R; EM; 3.70 A; A/B=36-1229.
DR PDBsum; 5L5K; -.
DR PDBsum; 5L5L; -.
DR PDBsum; 5L5M; -.
DR PDBsum; 5L5N; -.
DR PDBsum; 7M0R; -.
DR AlphaFoldDB; Q80UG2; -.
DR SMR; Q80UG2; -.
DR BioGRID; 232552; 7.
DR IntAct; Q80UG2; 4.
DR MINT; Q80UG2; -.
DR STRING; 10090.ENSMUSP00000110748; -.
DR GlyConnect; 2592; 12 N-Linked glycans (5 sites).
DR GlyGen; Q80UG2; 6 sites, 12 N-linked glycans (5 sites).
DR iPTMnet; Q80UG2; -.
DR PhosphoSitePlus; Q80UG2; -.
DR SwissPalm; Q80UG2; -.
DR MaxQB; Q80UG2; -.
DR PaxDb; Q80UG2; -.
DR PRIDE; Q80UG2; -.
DR ProteomicsDB; 289632; -.
DR Antibodypedia; 32143; 207 antibodies from 26 providers.
DR DNASU; 243743; -.
DR Ensembl; ENSMUST00000115096; ENSMUSP00000110748; ENSMUSG00000029765.
DR GeneID; 243743; -.
DR KEGG; mmu:243743; -.
DR UCSC; uc009bgm.3; mouse.
DR CTD; 91584; -.
DR MGI; MGI:2179061; Plxna4.
DR VEuPathDB; HostDB:ENSMUSG00000029765; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01050000244850; -.
DR HOGENOM; CLU_001436_2_0_1; -.
DR InParanoid; Q80UG2; -.
DR OMA; KVYLYKC; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; Q80UG2; -.
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 BioGRID-ORCS; 243743; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Plxna4; mouse.
DR PRO; PR:Q80UG2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q80UG2; protein.
DR Bgee; ENSMUSG00000029765; Expressed in superior cervical ganglion and 211 other tissues.
DR Genevisible; Q80UG2; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:MGI.
DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR GO; GO:0017154; F:semaphorin receptor activity; IGI:MGI.
DR GO; GO:0021960; P:anterior commissure morphogenesis; IMP:MGI.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0021785; P:branchiomotor neuron axon guidance; IMP:ParkinsonsUK-UCL.
DR GO; GO:0021793; P:chemorepulsion of branchiomotor axon; IMP:MGI.
DR GO; GO:0021602; P:cranial nerve morphogenesis; IMP:MGI.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
DR GO; GO:0021610; P:facial nerve morphogenesis; IMP:MGI.
DR GO; GO:0021612; P:facial nerve structural organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0021615; P:glossopharyngeal nerve morphogenesis; IMP:MGI.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:ParkinsonsUK-UCL.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IGI:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:MGI.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0021784; P:postganglionic parasympathetic fiber development; IMP:MGI.
DR GO; GO:0048841; P:regulation of axon extension involved in axon guidance; IMP:MGI.
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:0050923; P:regulation of negative chemotaxis; IMP:MGI.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IMP:MGI.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IMP:ParkinsonsUK-UCL.
DR GO; GO:0048485; P:sympathetic nervous system development; IMP:MGI.
DR GO; GO:0097492; P:sympathetic neuron axon guidance; IGI:MGI.
DR GO; GO:0021636; P:trigeminal nerve morphogenesis; IMP:MGI.
DR GO; GO:0021637; P:trigeminal nerve structural organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0021644; P:vagus nerve morphogenesis; IMP:MGI.
DR DisProt; DP02528; -.
DR Gene3D; 1.10.506.10; -; 1.
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; 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; 3.
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; Acetylation; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1893
FT /note="Plexin-A4"
FT /id="PRO_0000240284"
FT TOPO_DOM 24..1236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1237..1257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1258..1893
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..506
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 508..558
FT /note="PSI 1"
FT DOMAIN 654..701
FT /note="PSI 2"
FT DOMAIN 802..855
FT /note="PSI 3"
FT DOMAIN 857..951
FT /note="IPT/TIG 1"
FT DOMAIN 953..1036
FT /note="IPT/TIG 2"
FT DOMAIN 1039..1138
FT /note="IPT/TIG 3"
FT DOMAIN 1141..1229
FT /note="IPT/TIG 4"
FT MOD_RES 1349
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCM2"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1006
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 129..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 283..404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 299..355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 373..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 509..526
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 515..557
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 518..535
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 529..541
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 592..611
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT CONFLICT 683..684
FT /note="DP -> GR (in Ref. 1; BAC56599)"
FT /evidence="ECO:0000305"
FT CONFLICT 1607
FT /note="V -> E (in Ref. 3; BAC34692)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1893 AA; 212560 MW; C785B0D895AD8DB7 CRC64;
MKAMPWNWTC LLSHLLVVGM GSSTLLPRQP PQLSQKPSFV TFRGEPAEGF NHLVVDERTG
HIYLGAVNRI YKLSSDLKVL VTHQTGPDED NPKCYPPRIV QTCNEPLAST NNVNKMLLID
YKENRLIACG SLYQGICKLL RLEDLFKLGE PFHKKEHYLS GVNESGSVFG VIVSYSNFDD
KLFIATAVDG KPEYFPTISS RKLTKNSEAD GMFAYVFHDE FVASMIKIPS DTFTVIPDFD
IYYVYGFSSG NFVYFLTLQP EMVSPPGSTT KEQVYTSKLV RLCKEDTAFN SYVEVPIGCE
RNGVEYRLLQ AAYLSKAGAV LGRTLGVRPD DDLLFTVFSK GQKRKMKSLD ESALCIFILK
QINDRIKDRL QSCYRGEGTL DLAWLKVKDI PCSSALLTID DNFCGLDMNA PLGVSEMVRG
IPVFTEDRDR MTSVIAYVYK NHSLAFVGTK SGKLKKIRVD GPKGNALQYE TVQVVDSGPV
LRDMAFSKDH EQLYIMSERQ LTRVPVESCG QYRSCGECLG SGDPHCGWCV LHNTCTRKER
CERSREPRRF ASEMKQCVRL TVHPNNISVS QYNVLLVLET YNVPELSAGV NCTFEDLSEM
DGLVIGNQIQ CYSPAAKEVP RIITENGDHH VVQLQLKSKE TGMTFASTSF VFYNCSVHNS
CLSCVESPYR CHWCKYRHVC THDPNTCSFQ EGRVKLPEDC PQLLRVDKIL VPVEVIKPIT
LKAKNLPQPQ SGQRGYECIL NIQGIEQRVP ALRFNSSSVQ CQNTSYSYEG MEINNLPVEL
TVVWNGHFNI DNPAQNKVYL YKCGAMRESC GLCLKADPDF ECGWCQSPGQ CTLRQHCPAH
ESRWLELSGA NSKCTNPRIT EIIPVTGPRE GGTKVTIRGE NLGLEFRDIA SHVKVAGVEC
SPLVDGYIPA EQIVCEMGEA KPSQHAGFVE ICVAVCRPEF MARSSQLYYF MTLTLADLKP
NRGPMSGGTQ VTITGTNLNA GSNVVVMFGS QPCLFHRRSP SYIICNTTSS EEVLDMKVTV
QVDRARIRQD LVFQYVEDPT IVRIEPEWSI VSGNTPIAVW GTHLDLIQNP QIRAKHGGKE
HINICEVLNA TEMTCQAPAL ALGPDHQSDL TERPEEFGFI LDNVQSLLIL NKTNFTYYPN
PVFEAFSPSG ILELKPGTPI ILKGKNLIPP VAGGNVKLNY TVLVGEKPCT VTVSDVQLLC
ESPNLIGRHK VMARVGGMEY SPGMVYIAPD SPLSLPAIVS IAVAGGLLII FIVAVLIAYK
RKSRESDLTL KRLQMQMDNL ESRVALECKE AFAELQTDIH ELTSDLDGAG IPFLDYRTYT
MRVLFPGIED HPVLRDLEVP GYRQERVEKG LKLFAQLINN KVFLLSFIRT LESQRSFSMR
DRGNVASLIM TVLQSKLEYA TDVLKQLLAD LIDKNLESKN HPKLLLRRTE SVAEKMLTNW
FTFLLYKFLK ECAGEPLFSL FCAIKQQMEK GPIDAITGEA RYSLSEDKLI RQQIEYKTLV
LSCVSPDNVN SPEVPVKILN CDTITQVKEK ILDAIFKNVP CSHRPKAADM DLEWRQGSGA
RMILQDEDIT TKIENDWKRL NTVAHYQVPD GSVVALVSKQ VTAYNAVNNS TVSRTSASKY
ENMIRYTGSP DSLRSRTPMI TPDLESGVKL WHLVKNHEHG DQKEGDRGSK MVSEIYLTRL
LATKGTLQKF VDDLFETIFS TAHRGSALPL AIKYMFDFLD EQADKHGIHD PHVRHTWKSN
CLPLRFWVNM IKNPQFVFDI HKNSITDACL SVVAQTFMDS CSTSEHRLGK DSPSNKLLYA
KDIPSYKNWV ERYYSDIGKM PAISDQDMNA YLAEQSRMHM NEFNTMSALS EIFSYVGKYS
EEILGPLDHD DQCGKQKLAY KLEQVITLMS LDS
