FAS2_DROME
ID FAS2_DROME Reviewed; 873 AA.
AC P34082; P34083; Q6IDE4; Q8IRS5; Q9W4M6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Fasciclin-2;
DE AltName: Full=Fasciclin II;
DE Short=FAS II;
DE Flags: Precursor;
GN Name=Fas2; ORFNames=CG3665;
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] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S;
RX PubMed=1913818; DOI=10.1016/0092-8674(91)90571-f;
RA Grenningloh G., Rehm E.J., Goodman C.S.;
RT "Genetic analysis of growth cone guidance in Drosophila: fasciclin II
RT functions as a neuronal recognition molecule.";
RL Cell 67:45-57(1991).
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, AND ALTERNATIVE SPLICING.
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;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 22-873.
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-330 AND ASN-576, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827; THR-841 AND SER-845, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Neuronal recognition molecule for the MP1 axon pathway,
CC pathway recognition for axons during the development of nerve
CC fascicles. {ECO:0000269|PubMed:1913818}.
CC -!- INTERACTION:
CC P34082; P14599: Appl; NbExp=3; IntAct=EBI-868243, EBI-74135;
CC P34082; Q59E14: CT35363; NbExp=2; IntAct=EBI-868243, EBI-6897236;
CC P34082; Q9VR25: fipi; NbExp=2; IntAct=EBI-868243, EBI-6897191;
CC P34082; Q9GQQ6: X11L; NbExp=2; IntAct=EBI-868243, EBI-2027617;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000305|PubMed:1913818}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000269|PubMed:1913818}; Lipid-anchor, GPI-anchor
CC {ECO:0000305|PubMed:1913818}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1; Synonyms=A, Membrane-linked;
CC IsoId=P34082-1; Sequence=Displayed;
CC Name=2; Synonyms=C, Phosphatidylinositol-linked;
CC IsoId=P34082-2; Sequence=VSP_002508, VSP_002509;
CC Name=3; Synonyms=B;
CC IsoId=P34082-3; Sequence=VSP_002506, VSP_002507;
CC -!- TISSUE SPECIFICITY: In embryos, both isoforms are initially expressed
CC on the surface of the axons in the MP1 pathway and later on several
CC other longitudinal axon fascicles. {ECO:0000269|PubMed:1913818}.
CC -!- MISCELLANEOUS: [Isoform 2]: GPI-anchored form. {ECO:0000305}.
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DR EMBL; M77165; AAA28527.1; -; mRNA.
DR EMBL; M77166; AAA28528.1; -; mRNA.
DR EMBL; AL033125; CAA21825.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF45925.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09118.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09119.1; -; Genomic_DNA.
DR EMBL; BT014661; AAT27285.1; -; mRNA.
DR EMBL; AL033125; CAA21826.1; -; Genomic_DNA.
DR PIR; A41054; A41054.
DR PIR; B41054; B41054.
DR RefSeq; NP_525066.1; NM_080327.3. [P34082-1]
DR RefSeq; NP_726911.1; NM_167004.2. [P34082-3]
DR RefSeq; NP_726912.1; NM_167005.2. [P34082-2]
DR AlphaFoldDB; P34082; -.
DR SMR; P34082; -.
DR BioGRID; 57881; 294.
DR IntAct; P34082; 669.
DR STRING; 7227.FBpp0070633; -.
DR GlyGen; P34082; 6 sites.
DR iPTMnet; P34082; -.
DR PaxDb; P34082; -.
DR DNASU; 31364; -.
DR EnsemblMetazoa; FBtr0070665; FBpp0070633; FBgn0000635. [P34082-1]
DR EnsemblMetazoa; FBtr0070666; FBpp0070634; FBgn0000635. [P34082-3]
DR EnsemblMetazoa; FBtr0070667; FBpp0070635; FBgn0000635. [P34082-2]
DR GeneID; 31364; -.
DR KEGG; dme:Dmel_CG3665; -.
DR CTD; 31364; -.
DR FlyBase; FBgn0000635; Fas2.
DR VEuPathDB; VectorBase:FBgn0000635; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000173388; -.
DR InParanoid; P34082; -.
DR OMA; NCNAAQY; -.
DR PhylomeDB; P34082; -.
DR SignaLink; P34082; -.
DR BioGRID-ORCS; 31364; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Fas2; fly.
DR GenomeRNAi; 31364; -.
DR PRO; PR:P34082; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000635; Expressed in eye disc (Drosophila) and 28 other tissues.
DR ExpressionAtlas; P34082; baseline and differential.
DR Genevisible; P34082; DM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0042995; C:cell projection; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0030426; C:growth cone; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031256; C:leading edge membrane; IDA:FlyBase.
DR GO; GO:0097482; C:muscle cell postsynaptic specialization; IDA:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0043005; C:neuron projection; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:FlyBase.
DR GO; GO:0048786; C:presynaptic active zone; IDA:FlyBase.
DR GO; GO:0042734; C:presynaptic membrane; IMP:FlyBase.
DR GO; GO:0036062; C:presynaptic periactive zone; IDA:FlyBase.
DR GO; GO:0061174; C:type I terminal bouton; IDA:BHF-UCL.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007413; P:axonal fasciculation; TAS:FlyBase.
DR GO; GO:0048149; P:behavioral response to ethanol; TAS:FlyBase.
DR GO; GO:0001746; P:Bolwig's organ morphogenesis; IMP:FlyBase.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:FlyBase.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:FlyBase.
DR GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IMP:FlyBase.
DR GO; GO:0007611; P:learning or memory; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IGI:FlyBase.
DR GO; GO:1904800; P:negative regulation of neuron remodeling; IMP:FlyBase.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase.
DR GO; GO:0008038; P:neuron recognition; IDA:FlyBase.
DR GO; GO:0008355; P:olfactory learning; TAS:FlyBase.
DR GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
DR GO; GO:1904059; P:regulation of locomotor rhythm; IDA:FlyBase.
DR GO; GO:0050803; P:regulation of synapse structure or activity; TAS:FlyBase.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IGI:FlyBase.
DR GO; GO:0035158; P:regulation of tube diameter, open tracheal system; IMP:FlyBase.
DR GO; GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
DR GO; GO:0007614; P:short-term memory; TAS:FlyBase.
DR GO; GO:0050808; P:synapse organization; IMP:FlyBase.
DR GO; GO:0072553; P:terminal button organization; IMP:FlyBase.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 7.
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; IPR009138; Neural_cell_adh.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 3.
DR PRINTS; PR01838; NCAMFAMILY.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Neurogenesis; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..873
FT /note="Fasciclin-2"
FT /id="PRO_0000014758"
FT TOPO_DOM 29..751
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 752..769
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 770..873
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..131
FT /note="Ig-like C2-type 1"
FT DOMAIN 138..223
FT /note="Ig-like C2-type 2"
FT DOMAIN 230..318
FT /note="Ig-like C2-type 3"
FT DOMAIN 323..423
FT /note="Ig-like C2-type 4"
FT DOMAIN 428..520
FT /note="Ig-like C2-type 5"
FT DOMAIN 524..622
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 638..738
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 611..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..826
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 841
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT DISULFID 54..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 159..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 251..302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 343..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 451..504
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 737..773
FT /note="GIDVIQVAERQVFSSAAIVGIAIGGVLLLLFVVDLLC -> DNPHPSTSGAA
FT PLAQLLVIFTALPTMLLILPPTTHTA (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_002506"
FT VAR_SEQ 738..811
FT /note="IDVIQVAERQVFSSAAIVGIAIGGVLLLLFVVDLLCCITVHMGVMATMCRKA
FT KRSPSEIDDEAKLGSGQLVKEP -> ESDSANNNLGTLLYSAGFNSGVGALHKRLFTTT
FT TTTTATSTTTITSITTATTTIITLATTISITLLSVLASMLA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1913818"
FT /id="VSP_002508"
FT VAR_SEQ 774..873
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_002507"
FT VAR_SEQ 812..873
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1913818"
FT /id="VSP_002509"
FT CONFLICT 804
FT /note="S -> R (in Ref. 5; CAA21826)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 873 AA; 96926 MW; E48F0484CCE62AC9 CRC64;
MGELPPNSVG VFLALLLCSC SLIELTRAQS PILEIYPKQE VQRKPVGKPL ILTCRPTVPE
PSLVADLQWK DNRNNTILPK PNGRNQPPMY TETLPGESLA LMITSLSVEM GGKYYCTASY
ANTEILEKGV TIKTYVAITW TNAPENQYPT LGQDYVVMCE VKADPNPTID WLRNGDPIRT
TNDKYVVQTN GLLIRNVQES DEGIYTCRAA VIETGELLER TIRVEVFIQP EIISLPTNLE
AVEGKPFAAN CTARGKPVPE ISWIRDATQL NVATADRFQV NPQTGLVTIS SVSQDDYGTY
TCLAKNRAGV VDQKTKLNVL VRPQIYELYN VTGARTKEIA ITCRAKGRPA PAITFRRWGT
QEEYTNGQQD DDPRIILEPN FDEERGESTG TLRISNAERS DDGLYQCIAR NKGADAYKTG
HITVEFAPDF SHMKELPPVF SWEQRKANLS CLAMGIPNAT IEWHWNGRKI KDLYDTNLKI
VGTGPRSDLI VHPVTRQYYS GYKCIATNIH GTAEHDMQLK EARVPDFVSE AKPSQLTATT
MTFDIRGPST ELGLPILAYS VQYKEALNPD WSTAYNRSWS PDSPYIVEGL RPQTEYSFRF
AARNQVGLGN WGVNQQQSTP RRSAPEEPKP LHNPVQHDKE EPVVVSPYSD HFELRWGVPA
DNGEPIDRYQ IKYCPGVKIS GTWTELENSC NTVEVMETTS FEMTQLVGNT YYRIELKAHN
AIGYSSPASI IMKTTRGIDV IQVAERQVFS SAAIVGIAIG GVLLLLFVVD LLCCITVHMG
VMATMCRKAK RSPSEIDDEA KLGSGQLVKE PPPSPLPLPP PVKLGGSPMS TPLDEKEPLR
TPTGSIKQNS TIEFDGRFVH SRSGEIIGKN SAV
