PLXB1_MOUSE
ID PLXB1_MOUSE Reviewed; 2119 AA.
AC Q8CJH3; E9QKS4; Q6ZQC3; Q80ZZ1;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Plexin-B1;
DE Flags: Precursor;
GN Name=Plxnb1; Synonyms=Kiaa0407;
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], TISSUE SPECIFICITY, AND INTERACTION WITH
RP PLXNA1.
RC TISSUE=Brain;
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 [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 913-2119.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1885-2119.
RC TISSUE=Eye;
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 [5]
RP FUNCTION.
RX PubMed=19788569; DOI=10.1111/j.1460-9568.2009.06934.x;
RA Vodrazka P., Korostylev A., Hirschberg A., Swiercz J.M., Worzfeld T.,
RA Deng S., Fazzari P., Tamagnone L., Offermanns S., Kuner R.;
RT "The semaphorin 4D-plexin-B signalling complex regulates dendritic and
RT axonal complexity in developing neurons via diverse pathways.";
RL Eur. J. Neurosci. 30:1193-1208(2009).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-543 AND ASN-1251.
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, 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).
RN [8]
RP FUNCTION.
RX PubMed=23699507; DOI=10.1523/jneurosci.0989-13.2013;
RA Kuzirian M.S., Moore A.R., Staudenmaier E.K., Friedel R.H., Paradis S.;
RT "The class 4 semaphorin Sema4D promotes the rapid assembly of GABAergic
RT synapses in rodent hippocampus.";
RL J. Neurosci. 33:8961-8973(2013).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=29981480; DOI=10.1016/j.mcn.2018.06.008;
RA McDermott J.E., Goldblatt D., Paradis S.;
RT "Class 4 Semaphorins and Plexin-B receptors regulate GABAergic and
RT glutamatergic synapse development in the mammalian hippocampus.";
RL Mol. Cell. Neurosci. 92:50-66(2018).
CC -!- FUNCTION: Receptor for SEMA4D (PubMed:19788569). Plays a role in
CC GABAergic synapse development (PubMed:23699507, PubMed:29981480).
CC Mediates SEMA4A- and SEMA4D-dependent inhibitory synapse development
CC (PubMed:23699507, PubMed:29981480). Plays a role in RHOA activation and
CC subsequent changes of the actin cytoskeleton (By similarity). Plays a
CC role in axon guidance, invasive growth and cell migration (By
CC similarity). {ECO:0000250|UniProtKB:O43157,
CC ECO:0000269|PubMed:19788569, ECO:0000269|PubMed:23699507,
CC ECO:0000269|PubMed:29981480}.
CC -!- SUBUNIT: Monomer, and heterodimer with PLXNB2 after proteolytic
CC processing (By similarity). Binds RAC1 that has been activated by GTP
CC binding (By similarity). Interaction with SEMA4D promotes binding of
CC cytoplasmic ligands (By similarity). Interacts with RRAS, ARHGEF11,
CC ARHGEF12, ERBB2, MET, MST1R, RND1, RHOD, NRP1 and NRP2 (By similarity).
CC Interacts with PLXNA1 (PubMed:12559962). {ECO:0000250|UniProtKB:O43157,
CC ECO:0000269|PubMed:12559962}.
CC -!- INTERACTION:
CC Q8CJH3; Q68FM7: Arhgef11; NbExp=5; IntAct=EBI-2637650, EBI-2365869;
CC Q8CJH3; Q8R4H2: Arhgef12; NbExp=2; IntAct=EBI-2637650, EBI-8046267;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O43157};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in brain, heart, lung, liver, kidney,
CC stomach, testis, uterus and placenta (PubMed:12559962). Expressed in
CC neurons and glia in the developing hippocampus (PubMed:29981480).
CC {ECO:0000269|PubMed:12559962, ECO:0000269|PubMed:29981480}.
CC -!- PTM: Phosphorylated on tyrosine residues by ERBB2 and MET upon SEMA4D
CC binding. {ECO:0000250|UniProtKB:O43157}.
CC -!- PTM: Proteolytic processing favors heterodimerization with PLXNB2 and
CC SEMA4D binding. {ECO:0000250|UniProtKB:O43157}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
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DR EMBL; AB072381; BAC22660.1; -; mRNA.
DR EMBL; AC140383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC174646; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK129133; BAC97943.1; -; mRNA.
DR EMBL; BC043322; AAH43322.1; -; mRNA.
DR CCDS; CCDS23546.1; -.
DR RefSeq; NP_766363.2; NM_172775.2.
DR RefSeq; XP_006512138.1; XM_006512075.3.
DR RefSeq; XP_006512139.1; XM_006512076.3.
DR RefSeq; XP_006512140.1; XM_006512077.3.
DR RefSeq; XP_006512141.1; XM_006512078.2.
DR RefSeq; XP_006512142.1; XM_006512079.3.
DR RefSeq; XP_006512143.1; XM_006512080.2.
DR AlphaFoldDB; Q8CJH3; -.
DR SMR; Q8CJH3; -.
DR BioGRID; 231692; 6.
DR CORUM; Q8CJH3; -.
DR IntAct; Q8CJH3; 3.
DR MINT; Q8CJH3; -.
DR STRING; 10090.ENSMUSP00000071966; -.
DR GlyConnect; 2593; 18 N-Linked glycans (4 sites).
DR GlyGen; Q8CJH3; 7 sites, 18 N-linked glycans (4 sites).
DR iPTMnet; Q8CJH3; -.
DR PhosphoSitePlus; Q8CJH3; -.
DR MaxQB; Q8CJH3; -.
DR PaxDb; Q8CJH3; -.
DR PRIDE; Q8CJH3; -.
DR ProteomicsDB; 289941; -.
DR Antibodypedia; 49406; 286 antibodies from 31 providers.
DR DNASU; 235611; -.
DR Ensembl; ENSMUST00000072093; ENSMUSP00000071966; ENSMUSG00000053646.
DR GeneID; 235611; -.
DR KEGG; mmu:235611; -.
DR UCSC; uc009rrz.2; mouse.
DR CTD; 5364; -.
DR MGI; MGI:2154238; Plxnb1.
DR VEuPathDB; HostDB:ENSMUSG00000053646; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01020000230394; -.
DR HOGENOM; CLU_001436_1_1_1; -.
DR InParanoid; Q8CJH3; -.
DR OMA; DAFPCGS; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; Q8CJH3; -.
DR TreeFam; TF312962; -.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-416550; Sema4D mediated inhibition of cell attachment and migration.
DR Reactome; R-MMU-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR BioGRID-ORCS; 235611; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Plxnb1; mouse.
DR PRO; PR:Q8CJH3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8CJH3; protein.
DR Bgee; ENSMUSG00000053646; Expressed in floor plate of midbrain and 240 other tissues.
DR ExpressionAtlas; Q8CJH3; baseline and differential.
DR Genevisible; Q8CJH3; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0002116; C:semaphorin receptor complex; ISS:UniProtKB.
DR GO; GO:0032794; F:GTPase activating protein binding; IPI:BHF-UCL.
DR GO; GO:0017154; F:semaphorin receptor activity; IMP:UniProtKB.
DR GO; GO:1904862; P:inhibitory synapse assembly; IMP:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; IMP:BHF-UCL.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
DR GO; GO:0043931; P:ossification involved in bone maturation; IMP:BHF-UCL.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IGI:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IMP:UniProtKB.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central.
DR GO; GO:1900220; P:semaphorin-plexin signaling pathway involved in bone trabecula morphogenesis; IMP:BHF-UCL.
DR Gene3D; 1.10.506.10; -; 2.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 3.
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; 1.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF01833; TIG; 3.
DR Pfam; PF18020; TIG_2; 1.
DR Pfam; PF17960; TIG_plexin; 1.
DR SMART; SM00429; IPT; 3.
DR SMART; SM00423; PSI; 3.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF81296; SSF81296; 3.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Disulfide bond; Glycoprotein; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..2119
FT /note="Plexin-B1"
FT /id="PRO_0000024672"
FT TOPO_DOM 20..1474
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1475..1495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1496..2119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..479
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 1068..1158
FT /note="IPT/TIG 1"
FT DOMAIN 1160..1247
FT /note="IPT/TIG 2"
FT DOMAIN 1250..1359
FT /note="IPT/TIG 3"
FT REGION 683..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1867..1892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1492..1523
FT /evidence="ECO:0000255"
FT COMPBIAS 685..701
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..769
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1799
FT /note="Important for interaction with RAC1 and RND1"
FT /evidence="ECO:0000250"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 1251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 1314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 79..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 111..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 252..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 268..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 340..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 482..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 488..533
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 491..508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 502..514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 570..588
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT CONFLICT 36
FT /note="Q -> L (in Ref. 1; BAC22660)"
FT /evidence="ECO:0000305"
FT CONFLICT 1777
FT /note="P -> L (in Ref. 3; BAC97943)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2119 AA; 231376 MW; 08FB5ECD2E6DE342 CRC64;
MSVLGPVLLQ VFWAGCVVTL RSPLPAAFTA NGTHLQHLAR DPTTGTLYVG ATNFLFQLSP
GLQLEAVVST GPVNDSRDCL PPVIPDECPQ AQPTNNPNQL LLVSPEALVV CGSVHQGICE
LRSLGQIRQL LLRPERPGDT QYVAANDPAV STVGLVAQGL VGEPLLFVGR GYTSRGVGGG
IPPITTRALR PPDPQAAFSY EETAKLAVGR LSEYSHHFVS AFVRGASAYF LFLRRDLKAP
SRAFRAYVSR VCLQDQHYYS YVELPLACQG GRYGLIQAAA VATSKEVARG DVLFAAFSSV
APPTVDWPLS ASTGASGTSV LCAFPLDEVD QLANYTRDAC YTREGRAENG TKVADIAYDV
LSDCAQLPVD TPDAFPCGSD HTPSPMVSCV PLEATPILEL PGVQLTAVAV TMEDGHTIAF
LGDSQGQLHR VYLGPGRSAA PYSKQSIQPG SPVNRDLTFD GTFEHLYVAT QTTLVKVPVA
PCAQHLDCDS CLAHRDPYCG WCVLLGRCSR RSECSRDQGP EQWLWSFQPE LGCLRVVAVS
PANISREERR EVFLSVPGLP SLWPGESYFC YFGDQQSPAL LTSSGVMCPS PDPSEAPVLQ
RGADHISVNV ELRFGAVVIA STSLSFYDCV AVTASSPSAP CRACVSSRWG CNWCVWQQLC
THKASCDAGP MVASQQSPLL PLIPPARDEL TPFPPTVPQT TVTPTPNSFP IEPRAPSTAS
DVLPGAKPSR LSLWGPWAGP GPILSPTSTE SPLHEKPLPP DPPTIPGTTV PAPTGLGPST
TPEDLLASYP FPSDAAAVSP AEPGPEALPS MVALDQPPGT VPDTTFPGAP GSMKPVLDWL
TKGGGELPEA DEWMGGDTPA FSTSTLLSGD GDSAEHEGPP APLILLSSLD YQYDTPGLWE
LGEVNQRVSS CPCVETVQGS LLIPVHVERE VQLRGRNLWL FQDGPRSSEC VLELGSREVA
VEAQVECAPP PDVWCHIKCQ QHQFSYEALK PELQVGLFLR WAGGLRVDSA DGLHVVLYDC
SVGHGDCSRC QTAMPQYDCV WCEGERPRCV AREACNEAET VATQCPAPLI HSVDPLTGPI
DGGTRVTIRG SNLGQHVQDV LDMVRVAGVP CAVDAGEYDV SSSLVCITGA SGEEVTGTVA
VEVPGRGHGV SEFSFAYQDP KVHSIFPARG PRAGGTRLTL HGSKLLTGRL EDIRVVVGDQ
PCHLLLEQQS EQLHCETGPY PVPAELPVTV LFGATERRLQ HGQFKYTSDP NVTSVGPSKS
FFSGGREIWV RGQDLDVVQR PRIRVTVVPR QHGQGLAQKQ HVVPEKFEEP CLVNSSHLLM
CRTPALPGPP WDSGVQVEFI LDNMVFDFAA LSPTPFSYEA DPTLRSLNPE DPSTPFRHKP
GSVFSVEGEN LDLAMSKEEV VAMIGDGPCV VKTLTRNHLY CEPPVEQPLP HPHALREAPD
ALPEFTVQMG NLRFSLGHVQ YDGESPVAFP VAAQVGLGVG TSLLALGVII IVLIYRRKSK
QALRDYKKVQ IQLENLESSV RDRCKKEFTD LMTEMTDLTS DLLGSGIPFL DYKVYAERVF
FPGYRESPLH RDLGVPDSRR PTVEQGLGQL SNLLNSKLFL TKFIHTLESQ RTFSARDRAY
VASLLTVALH GKLEYFTDIL RTLLSDLVAQ YVAKNPKLML RRTETVVEKL LTNWMSICLY
TFVRDSVGEP LYMLFRGIKH QVDKGPVDSV TGKAKYTLND NRLLREDVEY RPLTLNALLA
VGPGAGEAQC VPVKVLDCDT ISQAKEKMLD QLYKGVPLAQ RPDSCTLDVE WRSGVAGHLI
LSDEDVTSEL QGLWRRLNTL QHYKVPDGAT VALVPCLTKH ILRENQDYVP GERTPMLEDV
DEGGIRPWHL VKPSDEPEPP RPRRGSLRGG ERERAKAIPE IYLTRLLSMK GTLQKFVDDL
FQVILSTSRP VPLAVKYFFD LLDEQAQQHG ISDQDTIHIW KTNSLPLRFW INIIKNPQFV
FDVQTSDNMD AVLLVIAQTF MDACTLADHK LGRDSPINKL LYARDIPRYK QMVERYYADI
RQTVPASDQE MNSVLAELSR NCSADLGARV ALHELYKYIN KYYDQIITAL EEDGTAQKMQ
LGYRLQQIAA AVENKVTDL
