LRFN1_MOUSE
ID LRFN1_MOUSE Reviewed; 766 AA.
AC Q2WF71; Q460M4; Q8C1V9; Q99KT6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Leucine-rich repeat and fibronectin type III domain-containing protein 1;
DE AltName: Full=Synaptic adhesion-like molecule 2;
DE AltName: Full=Synaptic differentiation-enhancing molecule 1;
DE Flags: Precursor;
GN Name=Lrfn1; Synonyms=Salm2, Semo1;
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] (ISOFORM 1), FUNCTION, INTERACTION WITH DLG4,
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, GLYCOSYLATION, SUBCELLULAR
RP LOCATION, AND TOPOLOGY.
RC STRAIN=Swiss Webster;
RX PubMed=16828986; DOI=10.1016/j.gene.2006.05.014;
RA Morimura N., Inoue T., Katayama K., Aruga J.;
RT "Comparative analysis of structure, expression and PSD95-binding capacity
RT of Lrfn, a novel family of neuronal transmembrane proteins.";
RL Gene 380:72-83(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=16495444; DOI=10.1523/jneurosci.3799-05.2006;
RA Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K., Wenthold R.J.;
RT "A novel family of adhesion-like molecules that interacts with the NMDA
RT receptor.";
RL J. Neurosci. 26:2174-2183(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
RA Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K.,
RA Kim E.;
RT "SALM synaptic cell adhesion-like molecules regulate the differentiation of
RT excitatory synapses.";
RL Neuron 50:233-245(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [6]
RP INTERACTION WITH LRFN1; LRFN2; LRFN3; LRFN4 AND LRFN5, AND MUTAGENESIS OF
RP 760-GLU--VAL-766.
RX PubMed=18227064; DOI=10.1074/jbc.m709456200;
RA Seabold G.K., Wang P.Y., Chang K., Wang C.Y., Wang Y.X., Petralia R.S.,
RA Wenthold R.J.;
RT "The SALM family of adhesion-like molecules forms heteromeric and homomeric
RT complexes.";
RL J. Biol. Chem. 283:8395-8405(2008).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF 760-GLU--VAL-766.
RX PubMed=18585462; DOI=10.1016/j.mcn.2008.05.019;
RA Wang P.Y., Seabold G.K., Wenthold R.J.;
RT "Synaptic adhesion-like molecules (SALMs) promote neurite outgrowth.";
RL Mol. Cell. Neurosci. 39:83-94(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Promotes neurite outgrowth in hippocampal neurons. Involved
CC in the regulation and maintenance of excitatory synapses. Induces the
CC clustering of excitatory postsynaptic proteins, including DLG4, DLGAP1,
CC GRIA1 and GRIN1. {ECO:0000269|PubMed:16828986,
CC ECO:0000269|PubMed:18585462}.
CC -!- SUBUNIT: Can form heteromeric complexes with LRFN2, LRFN3, LRFN4 and
CC LRFN5. Forms homomeric complexes, but not across cell junctions.
CC Interacts with DLG4. Interacts also with DLG1, DLG2, and DLG3 (By
CC similarity). Interacts with 2 AMPA receptor subunits GRIA1 and GRIA2
CC and NMDA receptor subunit GRIN1. {ECO:0000250,
CC ECO:0000269|PubMed:16828986, ECO:0000269|PubMed:18227064}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Synapse {ECO:0000250}. Postsynaptic
CC density membrane {ECO:0000250}. Note=Detected in excitatory, but not
CC inhibitory, synaptic plasma membrane. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q2WF71-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2WF71-2; Sequence=VSP_033618, VSP_033619;
CC Name=3;
CC IsoId=Q2WF71-3; Sequence=VSP_033617;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the brain, with a weak,
CC but broad expression in the cerebral cortex and diencephalic nuclei.
CC Also detected in other parts of the central nervous system, including
CC the olfactory bulb, pons, cerebellum, and medulla oblongata, as well as
CC in the peripheral nervous system, such as the ganglia of cranial nerves
CC and the dorsal root ganglion during gestation.
CC {ECO:0000269|PubMed:16828986}.
CC -!- DEVELOPMENTAL STAGE: Expression starts around 10.5 dpc. At 11.5 dpc,
CC broadly expressed in the telencephalic and diencephalic vesicles. This
CC pattern of expression continues until 17.5 dpc.
CC {ECO:0000269|PubMed:16828986}.
CC -!- DOMAIN: The PDZ-binding motif is required for neurite outgrowth
CC promotion. This motif is also involved in DLG1-, DLG3- and DLG4-binding
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:16828986}.
CC -!- SIMILARITY: Belongs to the LRFN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41123.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB243740; BAE53711.1; -; mRNA.
DR EMBL; DQ070870; AAZ20639.1; -; mRNA.
DR EMBL; DQ314497; ABC40967.1; -; mRNA.
DR EMBL; AK090175; BAC41123.1; ALT_FRAME; mRNA.
DR EMBL; BC004018; AAH04018.1; -; mRNA.
DR CCDS; CCDS21045.1; -. [Q2WF71-2]
DR CCDS; CCDS52163.1; -. [Q2WF71-1]
DR RefSeq; NP_001135393.1; NM_001141921.1. [Q2WF71-1]
DR RefSeq; NP_085039.2; NM_030562.2. [Q2WF71-2]
DR RefSeq; XP_006540501.1; XM_006540438.1. [Q2WF71-1]
DR PDB; 5XWU; X-ray; 3.16 A; B/D=32-390.
DR PDBsum; 5XWU; -.
DR AlphaFoldDB; Q2WF71; -.
DR SMR; Q2WF71; -.
DR BioGRID; 219807; 1.
DR IntAct; Q2WF71; 2.
DR STRING; 10090.ENSMUSP00000103923; -.
DR GlyGen; Q2WF71; 3 sites.
DR iPTMnet; Q2WF71; -.
DR PhosphoSitePlus; Q2WF71; -.
DR MaxQB; Q2WF71; -.
DR PaxDb; Q2WF71; -.
DR PeptideAtlas; Q2WF71; -.
DR PRIDE; Q2WF71; -.
DR ProteomicsDB; 252519; -. [Q2WF71-1]
DR ProteomicsDB; 252520; -. [Q2WF71-2]
DR ProteomicsDB; 252521; -. [Q2WF71-3]
DR Antibodypedia; 30291; 74 antibodies from 24 providers.
DR Ensembl; ENSMUST00000055110; ENSMUSP00000057645; ENSMUSG00000030600. [Q2WF71-2]
DR Ensembl; ENSMUST00000108288; ENSMUSP00000103923; ENSMUSG00000030600. [Q2WF71-1]
DR Ensembl; ENSMUST00000189877; ENSMUSP00000139609; ENSMUSG00000030600. [Q2WF71-2]
DR GeneID; 80749; -.
DR KEGG; mmu:80749; -.
DR UCSC; uc009fza.1; mouse. [Q2WF71-1]
DR UCSC; uc009fzb.2; mouse. [Q2WF71-2]
DR CTD; 57622; -.
DR MGI; MGI:2136810; Lrfn1.
DR VEuPathDB; HostDB:ENSMUSG00000030600; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160922; -.
DR HOGENOM; CLU_016998_1_0_1; -.
DR InParanoid; Q2WF71; -.
DR OMA; TRVRWDG; -.
DR OrthoDB; 151757at2759; -.
DR PhylomeDB; Q2WF71; -.
DR TreeFam; TF350185; -.
DR Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
DR BioGRID-ORCS; 80749; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Lrfn1; mouse.
DR PRO; PR:Q2WF71; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q2WF71; protein.
DR Bgee; ENSMUSG00000030600; Expressed in embryonic brain and 121 other tissues.
DR ExpressionAtlas; Q2WF71; baseline and differential.
DR Genevisible; Q2WF71; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; ISO:MGI.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
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; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Leucine-rich repeat; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat;
KW Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..766
FT /note="Leucine-rich repeat and fibronectin type III domain-
FT containing protein 1"
FT /id="PRO_0000334146"
FT TOPO_DOM 32..536
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..766
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..65
FT /note="LRRNT"
FT REPEAT 66..87
FT /note="LRR 1"
FT REPEAT 90..111
FT /note="LRR 2"
FT REPEAT 114..135
FT /note="LRR 3"
FT REPEAT 138..159
FT /note="LRR 4"
FT REPEAT 163..184
FT /note="LRR 5"
FT REPEAT 187..208
FT /note="LRR 6"
FT REPEAT 211..232
FT /note="LRR 7"
FT DOMAIN 252..298
FT /note="LRRCT"
FT DOMAIN 299..386
FT /note="Ig-like"
FT DOMAIN 424..520
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 397..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 763..766
FT /note="PDZ-binding"
FT COMPBIAS 578..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P244"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 321..370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 469..492
FT /note="RMIPSTSQTFLVNDLAAGRAYDLC -> SSSCPGTHYVDQDGLEIRVPLASA
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033618"
FT VAR_SEQ 470..766
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033617"
FT VAR_SEQ 493..766
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033619"
FT MUTAGEN 760..766
FT /note="Missing: Decreased promotion of neurite outgrowth.
FT No effect on homomeric interactions."
FT /evidence="ECO:0000269|PubMed:18227064,
FT ECO:0000269|PubMed:18585462"
FT CONFLICT 9
FT /note="G -> R (in Ref. 5; AAH04018)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="G -> S (in Ref. 5; AAH04018)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="N -> D (in Ref. 2; AAZ20639)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="S -> F (in Ref. 4; BAC41123)"
FT /evidence="ECO:0000305"
FT CONFLICT 423..424
FT /note="TS -> AT (in Ref. 5; AAH04018)"
FT /evidence="ECO:0000305"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:5XWU"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:5XWU"
FT TURN 106..111
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:5XWU"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:5XWU"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:5XWU"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:5XWU"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:5XWU"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:5XWU"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:5XWU"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:5XWU"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:5XWU"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 367..374
FT /evidence="ECO:0007829|PDB:5XWU"
FT STRAND 377..384
FT /evidence="ECO:0007829|PDB:5XWU"
SQ SEQUENCE 766 AA; 81945 MW; 316FE5D5BE48D3CE CRC64;
MAPGPFSSGL FSPPPAALPF LLLLWAGASR GQPCPGRCIC QNVAPTLTML CAKTGLLFVP
PAIDRRVVEL RLTDNFIAAV RRRDFANMTS LVHLTLSRNT IGQVAAGAFA DLRALRALHL
DSNRLAEVRG DQLRGLGNLR HLILGNNQIR KVESAAFDAF LSTVEDLDLS YNNLEALPWE
AVGQMVNLNT LTLDHNLIDH IAEGTFVQLH KLVRLDMTSN RLHKLPPDGL FLRSQGGGPK
PPTPLTVSFG GNPLHCNCEL LWLRRLTRED DLETCATPEH LTDRYFWSIP EEEFLCEPPL
ITRQAGGRAL VVEGQAVSLR CRAVGDPEPV VHWVAPDGRL LGNSSRTRVR GDGTLDVTIT
TLRDSGTFTC IASNAAGEAT APVEVCVVPL PLMAPPPAAP PPLTEPGSSD IATPGRPGAN
DSTSERRLVA AELTSSSVLI RWPAQRPVPG IRMYQVQYNS SADDSLVYRM IPSTSQTFLV
NDLAAGRAYD LCVLAVYDDG ATALPATRVV GCVQFTTAGD PAPCRPLRAH FLGGTMIIAI
GGVIVASVLV FIVLLMIRYK VYGDGDSRRI KGTSRTPPRV SHVCSQTNGA GAQQASAPPA
PDRYEALREV AVPAAIEAKA MEAEATSTEL EVVLGRSLGG SATSLCLLPS EETSGEESRA
MTGPRRSRSG ALGPPTSAPP TLALVPGGAP ARPRPQQRYS FDGDYGALFQ SHSYPRRARR
TKRHRSTPHL DGAGGGAAGE DGDLGLGSAR ARLAFTSTEW MLESTV
