PLXA3_HUMAN
ID PLXA3_HUMAN Reviewed; 1871 AA.
AC P51805; Q5HY36;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Plexin-A3;
DE AltName: Full=Plexin-4;
DE AltName: Full=Semaphorin receptor SEX;
DE Flags: Precursor;
GN Name=PLXNA3; Synonyms=PLXN4, SEX;
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].
RC TISSUE=Embryo, Fetal brain, and Skeletal muscle;
RX PubMed=8570614; DOI=10.1073/pnas.93.2.674;
RA Maestrini E., Tamagnone L., Longati P., Cremona O., Gulisano M., Bione S.,
RA Tamanini F., Neel B.G., Toniolo D., Comoglio P.M.;
RT "A family of transmembrane proteins with homology to the MET-hepatocyte
RT growth factor receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:674-678(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP INTERACTION WITH CBFA2T3/MTG16.
RX PubMed=20138877; DOI=10.1016/j.febslet.2010.02.007;
RA Fiedler S.E., Schillace R.V., Daniels C.J., Andrews S.F., Carr D.W.;
RT "Myeloid translocation gene 16b is a dual A-kinase anchoring protein that
RT interacts selectively with plexins in a phospho-regulated manner.";
RL FEBS Lett. 584:873-877(2010).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1596, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [5]
RP VARIANT MET-1238.
RX PubMed=28585349; DOI=10.1002/humu.23270;
RA Poirier K., Hubert L., Viot G., Rio M., Billuart P., Besmond C.,
RA Bienvenu T.;
RT "CSNK2B splice site mutations in patients cause intellectual disability
RT with or without myoclonic epilepsy.";
RL Hum. Mutat. 38:932-941(2017).
CC -!- FUNCTION: Coreceptor for SEMA3A and SEMA3F. Necessary for signaling by
CC class 3 semaphorins and subsequent remodeling of the cytoskeleton.
CC Plays a role in axon guidance in the developing nervous system.
CC Regulates the migration of sympathetic neurons, but not of neural crest
CC precursors. Required for normal dendrite spine morphology in pyramidal
CC neurons. May play a role in regulating semaphorin-mediated programmed
CC cell death in the developing nervous system. Class 3 semaphorins bind
CC 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.
CC -!- SUBUNIT: Interacts with CBFA2T3/MTG16. {ECO:0000269|PubMed:20138877}.
CC -!- INTERACTION:
CC P51805; O75081: CBFA2T3; NbExp=2; IntAct=EBI-7135904, EBI-1190217;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
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DR EMBL; X87852; CAA61132.1; -; mRNA.
DR EMBL; BX936365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS14752.1; -.
DR RefSeq; NP_059984.3; NM_017514.4.
DR AlphaFoldDB; P51805; -.
DR BioGRID; 120717; 158.
DR CORUM; P51805; -.
DR DIP; DIP-57386N; -.
DR IntAct; P51805; 48.
DR MINT; P51805; -.
DR STRING; 9606.ENSP00000358696; -.
DR GlyGen; P51805; 10 sites.
DR iPTMnet; P51805; -.
DR PhosphoSitePlus; P51805; -.
DR BioMuta; PLXNA3; -.
DR DMDM; 118572690; -.
DR EPD; P51805; -.
DR jPOST; P51805; -.
DR MassIVE; P51805; -.
DR MaxQB; P51805; -.
DR PaxDb; P51805; -.
DR PeptideAtlas; P51805; -.
DR PRIDE; P51805; -.
DR ProteomicsDB; 56401; -.
DR Antibodypedia; 31267; 61 antibodies from 18 providers.
DR DNASU; 55558; -.
DR Ensembl; ENST00000369682.4; ENSP00000358696.3; ENSG00000130827.6.
DR GeneID; 55558; -.
DR KEGG; hsa:55558; -.
DR MANE-Select; ENST00000369682.4; ENSP00000358696.3; NM_017514.5; NP_059984.3.
DR UCSC; uc004flm.5; human.
DR CTD; 55558; -.
DR DisGeNET; 55558; -.
DR GeneCards; PLXNA3; -.
DR HGNC; HGNC:9101; PLXNA3.
DR HPA; ENSG00000130827; Low tissue specificity.
DR MIM; 300022; gene.
DR neXtProt; NX_P51805; -.
DR OpenTargets; ENSG00000130827; -.
DR PharmGKB; PA33427; -.
DR VEuPathDB; HostDB:ENSG00000130827; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01050000244850; -.
DR HOGENOM; CLU_001436_2_0_1; -.
DR InParanoid; P51805; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; P51805; -.
DR TreeFam; TF312962; -.
DR PathwayCommons; P51805; -.
DR Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-HSA-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-HSA-399956; CRMPs in Sema3A signaling.
DR SignaLink; P51805; -.
DR BioGRID-ORCS; 55558; 9 hits in 703 CRISPR screens.
DR ChiTaRS; PLXNA3; human.
DR GeneWiki; PLXNA3; -.
DR GenomeRNAi; 55558; -.
DR Pharos; P51805; Tbio.
DR PRO; PR:P51805; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P51805; protein.
DR Bgee; ENSG00000130827; Expressed in adenohypophysis and 130 other tissues.
DR Genevisible; P51805; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0048846; P:axon extension involved in axon guidance; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0021785; P:branchiomotor neuron axon guidance; ISS:UniProtKB.
DR GO; GO:0021612; P:facial nerve structural organization; ISS:UniProtKB.
DR GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; ISS:UniProtKB.
DR GO; GO:0050919; P:negative chemotaxis; IEA:Ensembl.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IEA:Ensembl.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:0097485; P:neuron projection guidance; ISS:UniProtKB.
DR GO; GO:0021628; P:olfactory nerve formation; IEA:Ensembl.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0021860; P:pyramidal neuron development; ISS:UniProtKB.
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:0071526; P:semaphorin-plexin signaling pathway; NAS:BHF-UCL.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; ISS:UniProtKB.
DR GO; GO:0021637; P:trigeminal nerve structural organization; ISS:UniProtKB.
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; 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 Cell membrane; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1871
FT /note="Plexin-A3"
FT /id="PRO_0000024670"
FT TOPO_DOM 20..1220
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1221..1241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1242..1871
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..488
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 840..933
FT /note="IPT/TIG 1"
FT DOMAIN 935..1020
FT /note="IPT/TIG 2"
FT DOMAIN 1023..1122
FT /note="IPT/TIG 3"
FT DOMAIN 1125..1211
FT /note="IPT/TIG 4"
FT MOD_RES 1596
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 637
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 738
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1009
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1036
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1073
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 77..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 112..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 266..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 282..338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 356..375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 491..508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 497..539
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 500..517
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 511..523
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 574..594
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT VARIANT 384
FT /note="G -> S (in dbSNP:rs34585333)"
FT /id="VAR_050595"
FT VARIANT 413
FT /note="G -> S (in dbSNP:rs36115591)"
FT /id="VAR_050596"
FT VARIANT 863
FT /note="E -> D (in dbSNP:rs5945430)"
FT /id="VAR_050597"
FT VARIANT 1238
FT /note="V -> M (in dbSNP:rs200880623)"
FT /evidence="ECO:0000269|PubMed:28585349"
FT /id="VAR_083660"
FT CONFLICT 222
FT /note="F -> L (in Ref. 1; CAA61132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1871 AA; 207717 MW; E0C8C19263D2EE7D CRC64;
MPSVCLLLLL FLAVGGALGN RPFRAFVVTD TTLTHLAVHR VTGEVFVGAV NRVFKLAPNL
TELRAHVTGP VEDNARCYPP PSMRVCAHRL APVDNINKLL LIDYAARRLV ACGSIWQGIC
QFLRLDDLFK LGEPHHRKEH YLSGAQEPDS MAGVIVEQGQ GPSKLFVGTA VDGKSEYFPT
LSSRKLISDE DSADMFSLVY QDEFVSSQIK IPSDTLSLYP AFDIYYIYGF VSASFVYFLT
LQLDTQQTLL DTAGEKFFTS KIVRMCAGDS EFYSYVEFPI GCSWRGVEYR LVQSAHLAKP
GLLLAQALGV PADEDVLFTI FSQGQKNRAS PPRQTILCLF TLSNINAHIR RRIQSCYRGE
GTLALPWLLN KELPCINTPM QINGNFCGLV LNQPLGGLHV IEGLPLLADS TDGMASVAAY
TYRQHSVVFI GTRSGSLKKV RVDGFQDAHL YETVPVVDGS PILRDLLFSP DHRHIYLLSE
KQVSQLPVET CEQYQSCAAC LGSGDPHCGW CVLRHRCCRE GACLGASAPH GFAEELSKCV
QVRVRPNNVS VTSPGVQLTV TLHNVPDLSA GVSCAFEAAA ENEAVLLPSG ELLCPSPSLQ
ELRALTRGHG ATRTVRLQLL SKETGVRFAG ADFVFYNCSV LQSCMSCVGS PYPCHWCKYR
HTCTSRPHEC SFQEGRVHSP EGCPEILPSG DLLIPVGVMQ PLTLRAKNLP QPQSGQKNYE
CVVRVQGRQQ RVPAVRFNSS SVQCQNASYS YEGDEHGDTE LDFSVVWDGD FPIDKPPSFR
ALLYKCWAQR PSCGLCLKAD PRFNCGWCIS EHRCQLRTHC PAPKTNWMHL SQKGTRCSHP
RITQIHPLVG PKEGGTRVTI VGENLGLLSR EVGLRVAGVR CNSIPAEYIS AERIVCEMEE
SLVPSPPPGP VELCVGDCSA DFRTQSEQVY SFVTPTFDQV SPSRGPASGG TRLTISGSSL
DAGSRVTVTV RDSECQFVRR DAKAIVCISP LSTLGPSQAP ITLAIDRANI SSPGLIYTYT
QDPTVTRLEP TWSIINGSTA ITVSGTHLLT VQEPRVRAKY RGIETTNTCQ VINDTAMLCK
APGIFLGRPQ PRAQGEHPDE FGFLLDHVQT ARSLNRSSFT YYPDPSFEPL GPSGVLDVKP
GSHVVLKGKN LIPAAAGSSR LNYTVLIGGQ PCSLTVSDTQ LLCDSPSQTG RQPVMVLVGG
LEFWLGTLHI SAERALTLPA MMGLAAGGGL LLLAITAVLV AYKRKTQDAD RTLKRLQLQM
DNLESRVALE CKEAFAELQT DINELTNHMD EVQIPFLDYR TYAVRVLFPG IEAHPVLKEL
DTPPNVEKAL RLFGQLLHSR AFVLTFIHTL EAQSSFSMRD RGTVASLTMV ALQSRLDYAT
GLLKQLLADL IEKNLESKNH PKLLLRRTES VAEKMLTNWF TFLLHKFLKE CAGEPLFLLY
CAIKQQMEKG PIDAITGEAR YSLSEDKLIR QQIDYKTLTL HCVCPENEGS AQVPVKVLNC
DSITQAKDKL LDTVYKGIPY SQRPKAEDMD LEWRQGRMTR IILQDEDVTT KIECDWKRLN
SLAHYQVTDG SLVALVPKQV SAYNMANSFT FTRSLSRYES LLRTASSPDS LRSRAPMITP
DQETGTKLWH LVKNHDHADH REGDRGSKMV SEIYLTRLLA TKGTLQKFVD DLFETVFSTA
HRGSALPLAI KYMFDFLDEQ ADQRQISDPD VRHTWKSNCL PLRFWVNVIK NPQFVFDIHK
NSITDACLSV VAQTFMDSCS TSEHRLGKDS PSNKLLYAKD IPNYKSWVER YYRDIAKMAS
ISDQDMDAYL VEQSRLHASD FSVLSALNEL YFYVTKYRQE ILTALDRDAS CRKHKLRQKL
EQIISLVSSD S
