PLXB_DROME
ID PLXB_DROME Reviewed; 2051 AA.
AC Q9V4A7; O96682;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Plexin-B;
DE Flags: Precursor;
GN Name=PlexB {ECO:0000312|FlyBase:FBgn0025740};
GN ORFNames=CG17245 {ECO:0000312|FlyBase:FBgn0025740};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=9875845; DOI=10.1016/s0092-8674(00)81715-8;
RA Winberg M.L., Noordermeer J.N., Tamagnone L., Comoglio P.M., Spriggs M.K.,
RA Tessier-Lavigne M., Goodman C.S.;
RT "Plexin A is a neuronal semaphorin receptor that controls axon guidance.";
RL Cell 95:903-916(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND INTERACTION WITH RHO1; RAC1 AND RAC2.
RX PubMed=11604137; DOI=10.1016/s0896-6273(01)00453-6;
RA Hu H., Marton T.F., Goodman C.S.;
RT "Plexin B mediates axon guidance in Drosophila by simultaneously inhibiting
RT active Rac and enhancing RhoA signaling.";
RL Neuron 32:39-51(2001).
RN [6]
RP FUNCTION, INTERACTION WITH PLEXA AND SEMA-2A, AND DEVELOPMENTAL STAGE.
RX PubMed=16672342; DOI=10.1242/dev.02380;
RA Ayoob J.C., Terman J.R., Kolodkin A.L.;
RT "Drosophila Plexin B is a Sema-2a receptor required for axon guidance.";
RL Development 133:2125-2135(2006).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=29520219; DOI=10.3389/fnmol.2018.00055;
RA Grice S.J., Sleigh J.N., Zameel Cader M.;
RT "Plexin-Semaphorin Signaling Modifies Neuromuscular Defects in a Drosophila
RT Model of Peripheral Neuropathy.";
RL Front. Mol. Neurosci. 11:55-55(2018).
CC -!- FUNCTION: Involved in peripheral and central nervous system axon
CC guidance. Acts as a receptor for Sema-2a and seems to transduce signal
CC by suppressing Rac activity and enhancing Rho activity.
CC {ECO:0000269|PubMed:11604137, ECO:0000269|PubMed:16672342}.
CC -!- SUBUNIT: Interacts with PlexA. Interacts with Rho1 and with the active
CC forms of Rac1 and Rac2. Interacts with Sema-2a.
CC {ECO:0000269|PubMed:11604137, ECO:0000269|PubMed:16672342}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the embryonic and larval
CC nervous system. {ECO:0000269|PubMed:16672342,
CC ECO:0000269|PubMed:29520219, ECO:0000269|PubMed:9875845}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
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DR EMBL; AF106933; AAD09426.1; -; mRNA.
DR EMBL; AE014135; AAF59374.2; -; Genomic_DNA.
DR EMBL; BT010009; AAQ22478.1; -; mRNA.
DR PIR; T13164; T13164.
DR RefSeq; NP_001245400.1; NM_001258471.2.
DR RefSeq; NP_524616.2; NM_079877.4.
DR AlphaFoldDB; Q9V4A7; -.
DR SMR; Q9V4A7; -.
DR BioGRID; 68604; 12.
DR IntAct; Q9V4A7; 2.
DR STRING; 7227.FBpp0300616; -.
DR GlyGen; Q9V4A7; 13 sites.
DR PaxDb; Q9V4A7; -.
DR PRIDE; Q9V4A7; -.
DR EnsemblMetazoa; FBtr0089179; FBpp0088246; FBgn0025740.
DR EnsemblMetazoa; FBtr0308297; FBpp0300616; FBgn0025740.
DR GeneID; 43766; -.
DR KEGG; dme:Dmel_CG17245; -.
DR CTD; 43766; -.
DR FlyBase; FBgn0025740; PlexB.
DR VEuPathDB; VectorBase:FBgn0025740; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01020000230394; -.
DR HOGENOM; CLU_001436_2_0_1; -.
DR InParanoid; Q9V4A7; -.
DR OMA; IMQIKPL; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; Q9V4A7; -.
DR Reactome; R-DME-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-DME-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-DME-399956; CRMPs in Sema3A signaling.
DR Reactome; R-DME-416482; G alpha (12/13) signalling events.
DR Reactome; R-DME-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-DME-416700; Other semaphorin interactions.
DR Reactome; R-DME-9013405; RHOD GTPase cycle.
DR SignaLink; Q9V4A7; -.
DR BioGRID-ORCS; 43766; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43766; -.
DR PRO; PR:Q9V4A7; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0025740; Expressed in brain and 18 other tissues.
DR ExpressionAtlas; Q9V4A7; baseline and differential.
DR Genevisible; Q9V4A7; DM.
DR GO; GO:0030425; C:dendrite; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
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:0007411; P:axon guidance; IDA:UniProtKB.
DR GO; GO:0070593; P:dendrite self-avoidance; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:0071678; P:olfactory bulb axon guidance; IMP:FlyBase.
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 GO; GO:0097374; P:sensory neuron axon guidance; IMP:FlyBase.
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; 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; 3.
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; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Membrane; Neurogenesis; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..2051
FT /note="Plexin-B"
FT /id="PRO_0000248554"
FT TOPO_DOM 34..1380
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1381..1401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1402..2051
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 61..533
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 535..587
FT /note="PSI 1"
FT DOMAIN 683..730
FT /note="PSI 2"
FT DOMAIN 834..880
FT /note="PSI 3"
FT DOMAIN 888..975
FT /note="IPT/TIG 1"
FT DOMAIN 977..1064
FT /note="IPT/TIG 2"
FT DOMAIN 1097..1193
FT /note="IPT/TIG 3"
FT REGION 1402..1784
FT /note="Interaction with PlexA"
FT REGION 1722..1728
FT /note="Interaction with activated Rac1 and Rac2"
FT REGION 1788..1827
FT /note="Interaction with Rho1"
FT COILED 1402..1451
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 863
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1053
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1092
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 131..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 165..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 322..380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 536..553
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 542..586
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 545..562
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 556..568
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 622..641
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT CONFLICT 1082
FT /note="S -> A (in Ref. 1; AAD09426)"
FT /evidence="ECO:0000305"
FT CONFLICT 1289
FT /note="S -> T (in Ref. 1; AAD09426)"
FT /evidence="ECO:0000305"
FT CONFLICT 1526
FT /note="R -> Q (in Ref. 1; AAD09426)"
FT /evidence="ECO:0000305"
FT CONFLICT 1685
FT /note="R -> K (in Ref. 1; AAD09426)"
FT /evidence="ECO:0000305"
FT CONFLICT 1691
FT /note="V -> L (in Ref. 1; AAD09426)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2051 AA; 231680 MW; B65A57D7A255B44D CRC64;
MLRKELYCAN IIHVLHVLCI IIILGSQHYC VNCIEELPAQ ALSPLNDIVA QFNLPSIPVQ
STASSYGNRS IGNNIESVRD SQSKNYFTHM SFDFMHNVLF AGATNKILKL NENLRVLAEA
VTGPLHDSPQ CHAGGCPEDI ETSLVNNFNK ILVVSYAHDG ILIACGSIRQ GACEIYSLPR
FPATPQFFAV PLAANDENAS TYAFVGPARY AWKEEDILYV GTTFTNVGDY RHDVPAISSR
RLDDLNYAEF SIQQSIINID VKYRDHFLVD YIYGFNSSEY AYFIIVQKKS HLADEAGYVT
RLARICITDP NYDSYTEITV QCTATENNVD YNIVRDAKVT PASHKLAQKM GIKKDDHVLV
TVFSPSREIS NQPESKSAMC IYSIKDIEDM FIENIHLCFN GTTKDRNLGY ISGTINDGRC
PIVGSLGNIY NFCSVGLKIS GVSPITAHAL FHFDNVSVTS VTATSTTDQQ HSLAFLGTNM
GVIKKVLLSG QSPGEYEEIV VDAGNRILPN TMMSPKKDFL YVLSQRKITK LRIEHCSVYT
NCSACLESRD PFCGWCSLEK RCTVRSTCQR DTSASRWLSL GSGQQCIEFE SIIPEKIPIS
ELSHLHLIIR TLPEPFNAKY RCVFGNSTPI DAEILENGLG CATPPLDERP LIPTNTDHIL
VPLSVRSSET NKDFVSRNFA FFDCSHHGNC QECLQSSWGC NWCIFDNKCV HKSLQCRNIE
NAVSTVGHCP HLKKNRPEIL LPVRVPIEIR LEIENLPKPK SAHAGFLCTI HIEAAQMLLP
AHVESNKIVV CEKTPYFYEI NTHEYQAKVV VTWNFQHYVD TAIVTLYKCD VLGSHREHPD
CSLCVTRDPK YKCAWCSNSC VYNETCIADK NSISSGSKSA IENECPLPRI DIIKPLSGPV
EGGTLITIEG SNLGIREEDV RGKIFIGSVP CELENYQISV KIECRTGASL YEMSAPIKVA
NDAGFTESSV QFHFKNVLLT GLYPTIGPRS GGTQLSLIGK FLNIGSTMRA FLDEYECHID
VTQASSSQVS CTTSEATQPE PIRSLHLVID GANRTLECQI STPSITNTNP TRSNFGSYQL
RSLPRQPCSI FNYTQDPRIM QIKPLRSFKS GGRVLTVHGI YLNSIQKPEL EVFYDNERVN
KTSCVVINSN QMECPSPPVN YKFETFKKTN RKMDTELHLQ NSSFQTETRY KNEYDRKKRR
ADFGDTFRLY TNAGSSANYF VNNNMDVTTF VKVHETQLNL QLSFVMDNVQ LVRNLNKYFH
DIRSTIVYLA DPKYLPFPND GVKLYKGDSL VIEGELLNLA ADEYDVNVTI GTSQCNITSL
ALNQLLCIPP EQQPLPTDEN GVDQSTDLPL VVVKVGRNLR FVIGYLKYDL NKPYVFSHAL
LVGILTVALL VVVFVIVLII FRRKSTQAER EYKRIQIQMI TLESNVRSEC KQAFAELQTD
MTDLTADLES TGIPTLDHVN YIMKVFFPGV SDHPILNSPK FREGSPQTNY DAAMVQFEQL
IGNKYFLLMF IETLEAQRSS FSIRDRVNVA SLIMVVLMNK MEYATEILKS LLLRLIDKSL
ASKHPQLMLR RTESVVEKML TNYLAICMYD YLKEYAGSNL FLLFKAIKHQ IEKGLVDAIT
NDARYSLSEE RLLHEQVTHS VVILHILQDD LDEKVQCRVN DWDTISQVKL KILDAIFKNT
PFSMRPSVNE VDLEWRHGRG GHLTLQDEDL TTKTVNGWKR LNTLAHYGVK ESAVMSLIAR
QNDNYHIPYS KNQNSAPYHN FYFINNSQSH IIINNDIESG LQQPRVYHLV KPNIPDHYMN
IKNSVLSGGS PAFQSHVVNN CNDRVNKTIP EVYLTRLLAT KGTIQKFVDD FFSIILTVNE
ELPPAVKWLF DLLDEAARRH DIADTDIVHA WKSNCLPLRF WVNFIKNPDF IFDVNKTYSV
DSCLSVIAQT FMDACSTSEH RLGKDSPSNK LLFAKDIPNY RIMVKEFYRD VSRLPQISDQ
EMSTAMQQLS VRQNEEFDTI SALKELYIYI TKYKDQIMES LETDINCRKM HLSRKLGNVA
ATLDGDCTSN C
