NFASC_RAT
ID NFASC_RAT Reviewed; 1240 AA.
AC P97685; P97684; Q91Z60;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Neurofascin;
DE Flags: Precursor;
GN Name=Nfasc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=Wistar;
RA Tait S., Collinson J.M., Brophy P.J.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-1240 (ISOFORMS 1; 2 AND 3), AND SUBUNIT.
RC TISSUE=Brain;
RX PubMed=8947556; DOI=10.1083/jcb.135.5.1355;
RA Davis J.Q., Lambert S., Bennett V.;
RT "Molecular composition of the node of Ranvier: identification of ankyrin-
RT binding cell adhesion molecules neurofascin (mucin+/third FNIII domain-)
RT and NrCAM at nodal axon segments.";
RL J. Cell Biol. 135:1355-1367(1996).
RN [3]
RP FUNCTION OF ISOFORMS 2/3.
RX PubMed=9562181;
RX DOI=10.1002/(sici)1098-1136(199805)23:1<11::aid-glia2>3.0.co;2-7;
RA Collinson J.M., Marshall D., Gillespie C.S., Brophy P.J.;
RT "Transient expression of neurofascin by oligodendrocytes at the onset of
RT myelinogenesis: implications for mechanisms of axon-glial interaction.";
RL Glia 23:11-23(1998).
RN [4]
RP FUNCTION OF ISOFORMS 1 AND 2/3, INDIRECT ASSOCIATION WITH CNTNAP1,
RP PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX PubMed=10931875; DOI=10.1083/jcb.150.3.657;
RA Tait S., Gunn-Moore F., Collinson J.M., Huang J., Lubetzki C., Pedraza L.,
RA Sherman D.L., Colman D.R., Brophy P.J.;
RT "An oligodendrocyte cell adhesion molecule at the site of assembly of the
RT paranodal axo-glial junction.";
RL J. Cell Biol. 150:657-666(2000).
RN [5]
RP INTERACTION WITH SCN1B AND SCN3B.
RX PubMed=11470829; DOI=10.1083/jcb.200102086;
RA Ratcliffe C.F., Westenbroek R.E., Curtis R., Catterall W.A.;
RT "Sodium channel beta1 and beta3 subunits associate with neurofascin through
RT their extracellular immunoglobulin-like domain.";
RL J. Cell Biol. 154:427-434(2001).
RN [6]
RP FUNCTION, AND INTERACTION WITH GLDN.
RX PubMed=16039564; DOI=10.1016/j.neuron.2005.06.026;
RA Eshed Y., Feinberg K., Poliak S., Sabanay H., Sarig-Nadir O., Spiegel I.,
RA Bermingham J.R. Jr., Peles E.;
RT "Gliomedin mediates Schwann cell-axon interaction and the molecular
RT assembly of the nodes of Ranvier.";
RL Neuron 47:215-229(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1174; SER-1187 AND SER-1190,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-752 AND ASN-1015, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: Cell adhesion, ankyrin-binding protein which may be involved
CC in neurite extension, axonal guidance, synaptogenesis, myelination and
CC neuron-glial cell interactions. Isoform 2/isoform 3 may be responsible
CC for mediating and signaling axon-glial interaction during the early
CC stages of myelination. {ECO:0000269|PubMed:10931875,
CC ECO:0000269|PubMed:16039564, ECO:0000269|PubMed:9562181}.
CC -!- SUBUNIT: Horseshoe-shaped homodimer (By similarity). Probable
CC constituent of a NFASC/NRCAM/ankyrin G complex. Associates with the
CC sodium channel beta-1 (SCN1B) and beta-3 (SCN3B) subunits. Associates
CC to subunit beta-1 in developing axons as early as postanatal day 5,
CC during the period that nodes of Ranvier are forming. Isoform 2/isoform
CC 3 is likely to interact with axonal proteins in close association with
CC CNTNAP1. Interacts with GLDN/gliomedin. Interacts with MYOC (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Note=Isoform 1 colocalizes with ankyrin G at the nodes of
CC Ranvier. Isoform 2/ isoform 3 is a glial component of the paranodal
CC axo-glial junction.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=NF186, 186 kDa isoform;
CC IsoId=P97685-1; Sequence=Displayed;
CC Name=2; Synonyms=NF155, 155 kDa isoform;
CC IsoId=P97685-2; Sequence=VSP_050416, VSP_050417, VSP_050418,
CC VSP_050419;
CC Name=3; Synonyms=NF155, 155 kDa isoform;
CC IsoId=P97685-3; Sequence=VSP_050416, VSP_050417, VSP_008941,
CC VSP_050418, VSP_050419;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed at Nodes of Ranvier while
CC isoform 2/isoform 3 is expressed in unmyelinated axons.
CC {ECO:0000269|PubMed:10931875}.
CC -!- DEVELOPMENTAL STAGE: Strongly but transiently up-regulated in
CC oligodendrocytes at the onset of myelinogenesis. Once these last have
CC engaged their target exons, expression declines precipitously.
CC -!- DOMAIN: Homophilic adhesion is primarily mediated by the interaction of
CC the second Ig-like domains. {ECO:0000250}.
CC -!- PTM: Isoform 2/isoform 3 is phosphorylated at P12. Dephosphorylation is
CC required for ankyrin binding. {ECO:0000269|PubMed:10931875}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000305}.
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DR EMBL; AY061639; AAL27854.1; -; mRNA.
DR EMBL; U81035; AAB47753.1; -; mRNA.
DR EMBL; U81036; AAB47754.1; -; mRNA.
DR RefSeq; NP_001153785.1; NM_001160313.1. [P97685-2]
DR RefSeq; NP_001153786.1; NM_001160314.1. [P97685-1]
DR RefSeq; NP_446361.1; NM_053909.2. [P97685-3]
DR AlphaFoldDB; P97685; -.
DR SMR; P97685; -.
DR BioGRID; 250572; 6.
DR IntAct; P97685; 1.
DR MINT; P97685; -.
DR STRING; 10116.ENSRNOP00000057594; -.
DR GlyGen; P97685; 12 sites.
DR iPTMnet; P97685; -.
DR PhosphoSitePlus; P97685; -.
DR SwissPalm; P97685; -.
DR jPOST; P97685; -.
DR PaxDb; P97685; -.
DR PRIDE; P97685; -.
DR ABCD; P97685; 1 sequenced antibody.
DR GeneID; 116690; -.
DR KEGG; rno:116690; -.
DR UCSC; RGD:620911; rat. [P97685-1]
DR CTD; 23114; -.
DR RGD; 620911; Nfasc.
DR VEuPathDB; HostDB:ENSRNOG00000030515; -.
DR eggNOG; KOG3513; Eukaryota.
DR InParanoid; P97685; -.
DR OrthoDB; 434404at2759; -.
DR PhylomeDB; P97685; -.
DR TreeFam; TF351098; -.
DR Reactome; R-RNO-447043; Neurofascin interactions.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P97685; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000030515; Expressed in cerebellum and 10 other tissues.
DR ExpressionAtlas; P97685; baseline and differential.
DR Genevisible; P97685; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0043194; C:axon initial segment; IDA:BHF-UCL.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0033268; C:node of Ranvier; IDA:BHF-UCL.
DR GO; GO:0033010; C:paranodal junction; ISO:RGD.
DR GO; GO:0033270; C:paranode region of axon; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0097454; C:Schwann cell microvillus; IDA:RGD.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0045162; P:clustering of voltage-gated sodium channels; ISO:RGD.
DR GO; GO:0042552; P:myelination; IEP:BHF-UCL.
DR GO; GO:0030913; P:paranodal junction assembly; ISO:RGD.
DR GO; GO:0007422; P:peripheral nervous system development; IEP:BHF-UCL.
DR GO; GO:0071205; P:protein localization to juxtaparanode region of axon; ISO:RGD.
DR GO; GO:0002175; P:protein localization to paranode region of axon; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:BHF-UCL.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
DR GO; GO:0019226; P:transmission of nerve impulse; ISO:RGD.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR026966; Neurofascin/L1/NrCAM_C.
DR InterPro; IPR026965; NFASC.
DR PANTHER; PTHR10075; PTHR10075; 2.
DR PANTHER; PTHR10075:SF35; PTHR10075:SF35; 2.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1240
FT /note="Neurofascin"
FT /id="PRO_0000015051"
FT TOPO_DOM 25..1110
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1111..1131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1132..1240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..137
FT /note="Ig-like C2-type 1"
FT DOMAIN 143..230
FT /note="Ig-like C2-type 2"
FT DOMAIN 244..332
FT /note="Ig-like C2-type 3"
FT DOMAIN 337..424
FT /note="Ig-like C2-type 4"
FT DOMAIN 429..517
FT /note="Ig-like C2-type 5"
FT DOMAIN 521..603
FT /note="Ig-like C2-type 6"
FT DOMAIN 630..725
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 727..823
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 827..922
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1007..1099
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 710..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 481
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O94856"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94856"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810U3"
FT MOD_RES 1174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810U3"
FT MOD_RES 1227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810U3"
FT MOD_RES 1231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810U3"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 778
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 866
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 881
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1015
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 1026
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1047
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 162..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 268..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 358..408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 452..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 543..592
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 31..36
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:8947556, ECO:0000303|Ref.1"
FT /id="VSP_050416"
FT VAR_SEQ 236
FT /note="T -> NNPYNDSSLRNHPDIYSA (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:8947556, ECO:0000303|Ref.1"
FT /id="VSP_050417"
FT VAR_SEQ 611..625
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8947556, ECO:0000303|Ref.1"
FT /id="VSP_008941"
FT VAR_SEQ 824
FT /note="L -> YPRAAPTEVKIRVLNSTAISLQWNRVYPDTVQGQLREYRAYYWRESS
FT LLKNLWVSQKRQQASFPGDRPRGVVGRLFPYSNYKLEMVVVNGRGDGPRSETKEFTTPE
FT GV (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:8947556, ECO:0000303|Ref.1"
FT /id="VSP_050418"
FT VAR_SEQ 928..1096
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:8947556, ECO:0000303|Ref.1"
FT /id="VSP_050419"
FT CONFLICT 482
FT /note="E -> Q (in Ref. 2; AAB47753/AAB47754)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="W -> L (in Ref. 2; AAB47753/AAB47754)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="Q -> D (in Ref. 2; AAB47753/AAB47754)"
FT /evidence="ECO:0000305"
FT CONFLICT 763
FT /note="Y -> YY (in Ref. 2; AAB47753/AAB47754)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1240 AA; 138004 MW; 636A187BC3772513 CRC64;
MARQQAPPWV HVALILFLLS LGGAIEIPMD PSIQNELTQP PTITKQSVKD HIVDPRDNIL
IECEAKGNPA PSFHWTRNSR FFNIAKDPRV SMRRRSGTLV IDFRSGGRPE EYEGEYQCFA
RNKFGTALSN RIRLQVSKSP LWPKENLDPV VVQEGAPLTL QCNPPPGLPS PVIFWMSSSM
EPITQDKRVS QGHNGDLYFS NVMLQDMQTD YSCNARFHFT HTIQQKNPFT LKVLTTRGVA
ERTPSFMYPQ GTSSSQMVLR GMDLLLECIA SGVPTPDIAW YKKGGDLPSD KAKFENFNKA
LRITNVSEED SGEYFCLASN KMGSIRHTIS VRVKAAPYWL DEPKNLILAP GEDGRLVCRA
NGNPKPTVQW LVNGDPLQSA PPNPNREVAG DTIIFRDTQI SSRAVYQCNT SNEHGYLLAN
AFVSVLDVPP RMLSPRNQLI RVILYNRTRL DCPFFGSPIP TLRWFKNGQG SNLDGGNYHV
YENGSLEIKM IRKEDQGIYT CVATNILGKA ENQVRLEVKD PTRIYRMPED QVAKRGTTVQ
LECRVKHDPS LKLTVSWLKD DEPLYIGNRM KKEDDSLTIF GVAERDQGSY TCMASTELDQ
DLAKAYLTVL ADQATPTNRL AALPKGRPDR PRDLELTDLA ERSVRLTWIP GDDNNSPITD
YVVQFEEDQF QPGVWHDHSK FPGSVNSAVL HLSPYVNYQF RVIAVNEVGS SHPSLPSERY
RTSGAPPESN PSDVKGEGTR KNNMEITWTP MNATSAFGPN LRYIVKWRRR ETRETWNNVT
VWGSRYVVGQ TPVYVPYEIR VQAENDFGKG PEPETVIGYS GEDLPSAPRR FRVRQPNLET
INLEWDHPEH PNGILIGYTL RYVPFNGTKL GKQMVENFSP NQTKFSVQRA DPVSRYRFSL
SARTQVGSGE AATEESPTPP NEATPTAAPP TLPPTTVGTT GLVSSTDATA LAATSEATTV
PIIPTVVPTT VATTIATTTT TTAAATTTTT TESPPTTTTG TKIHETAPDE QSIWNVTVLP
NSKWANITWK HNFRPGTDFV VEYIDSNHTK KTVPVKAQAQ PIQLTDLFPG MTYTLRVYSR
DNEGISSTVI TFMTSTAYTN NQTDIATQGW FIGLMCAIAL LVLILLIVCF IKRSRGGKYP
VREKKDVPLG PEDPKEEDGS FDYSDEDNKP LQGSQTSLDG TIKQQESDDS LVDYGEGGEG
QFNEDGSFIG QYTVRKDKEE TEGNESSEAT SPVNAIYSLA
