FLRT1_MOUSE
ID FLRT1_MOUSE Reviewed; 646 AA.
AC Q6RKD8; Q14DT7; Q6RKD9;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Leucine-rich repeat transmembrane protein FLRT1;
DE AltName: Full=Fibronectin leucine rich transmembrane protein 1 {ECO:0000312|EMBL:AAR92201.1};
DE Flags: Precursor;
GN Name=Flrt1 {ECO:0000312|MGI:MGI:3026647};
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] {ECO:0000312|EMBL:AAR92201.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH FGFR1, SUBCELLULAR
RP LOCATION, GLYCOSYLATION, DEVELOPMENTAL STAGE, AND INDUCTION BY FGF2.
RC STRAIN=C57BL/6 X DBA/2J {ECO:0000312|EMBL:AAR92201.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAR92201.1};
RX PubMed=16872596; DOI=10.1016/j.ydbio.2006.04.004;
RA Haines B.P., Wheldon L.M., Summerbell D., Heath J.K., Rigby P.W.J.;
RT "Regulated expression of FLRT genes implies a functional role in the
RT regulation of FGF signalling during mouse development.";
RL Dev. Biol. 297:14-25(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 DEVELOPMENTAL STAGE.
RX PubMed=18448090; DOI=10.1016/j.ydbio.2008.03.021;
RA Maretto S., Mueller P.S., Aricescu A.R., Cho K.W., Bikoff E.K.,
RA Robertson E.J.;
RT "Ventral closure, headfold fusion and definitive endoderm migration defects
RT in mouse embryos lacking the fibronectin leucine-rich transmembrane protein
RT FLRT3.";
RL Dev. Biol. 318:184-193(2008).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-572; TYR-605 AND
RP TYR-643, AND MUTAGENESIS OF TYR-572; TYR-605 AND TYR-643.
RX PubMed=20421966; DOI=10.1371/journal.pone.0010264;
RA Wheldon L.M., Haines B.P., Rajappa R., Mason I., Rigby P.W., Heath J.K.;
RT "Critical role of FLRT1 phosphorylation in the interdependent regulation of
RT FLRT1 function and FGF receptor signalling.";
RL PLoS ONE 5:E10264-E10264(2010).
RN [8]
RP SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RX PubMed=21673655; DOI=10.1038/emboj.2011.189;
RA Yamagishi S., Hampel F., Hata K., Del Toro D., Schwark M., Kvachnina E.,
RA Bastmeyer M., Yamashita T., Tarabykin V., Klein R., Egea J.;
RT "FLRT2 and FLRT3 act as repulsive guidance cues for Unc5-positive
RT neurons.";
RL EMBO J. 30:2920-2933(2011).
RN [9]
RP FUNCTION, INTERACTION WITH ADGRL1 AND ADGRL3, AND SUBCELLULAR LOCATION.
RX PubMed=22405201; DOI=10.1016/j.neuron.2012.01.018;
RA O'Sullivan M.L., de Wit J., Savas J.N., Comoletti D., Otto-Hitt S.,
RA Yates J.R. III, Ghosh A.;
RT "FLRT proteins are endogenous latrophilin ligands and regulate excitatory
RT synapse development.";
RL Neuron 73:903-910(2012).
CC -!- FUNCTION: Plays a role in fibroblast growth factor-mediated signaling
CC cascades that lead to the activation of MAP kinases (PubMed:16872596,
CC PubMed:20421966). Promotes neurite outgrowth via FGFR1-mediated
CC activation of downstream MAP kinases. Promotes an increase both in
CC neurite number and in neurite length (PubMed:20421966). May play a role
CC in cell-cell adhesion and cell guidance via its interaction with
CC ADGRL1/LPHN1 and ADGRL3 (PubMed:22405201).
CC {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966,
CC ECO:0000305|PubMed:22405201}.
CC -!- SUBUNIT: Interacts with FGFR1 (PubMed:16872596). Interacts (via
CC extracellular domain) with ADGRL1/LPHN1 and ADGRL3 (via olfactomedin-
CC like domain) (PubMed:22405201). {ECO:0000269|PubMed:16872596,
CC ECO:0000269|PubMed:22405201}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16872596,
CC ECO:0000269|PubMed:20421966, ECO:0000269|PubMed:22405201}; Single-pass
CC membrane protein {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:16872596, ECO:0000305|PubMed:20421966}. Cytoplasmic
CC vesicle membrane {ECO:0000269|PubMed:16872596,
CC ECO:0000269|PubMed:20421966}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:20421966}. Cell
CC junction, focal adhesion {ECO:0000269|PubMed:16872596}. Secreted
CC {ECO:0000269|PubMed:21673655}. Cell projection, neuron projection
CC {ECO:0000269|PubMed:20421966}. Cell junction
CC {ECO:0000269|PubMed:20421966}. Note=In addition to its location at the
CC cell membrane, colocalizes with FGFR1 in punctate perinuclear
CC cytoplasmic vesicles (PubMed:16872596, PubMed:20421966). Detected along
CC neurites and at contacts between neurite termini and other cells
CC (PubMed:20421966). Proteolytic cleavage gives rise to a shedded
CC ectodomain (PubMed:21673655). {ECO:0000269|PubMed:16872596,
CC ECO:0000269|PubMed:20421966, ECO:0000269|PubMed:21673655}.
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level).
CC {ECO:0000269|PubMed:21673655}.
CC -!- DEVELOPMENTAL STAGE: Detected at comparable levels in embryonic brain
CC and in brain from ten day old animals (at protein level)
CC (PubMed:16872596). Detected in neuroectoderm at 7.5 dpc. Detected in
CC midbrain between 8.5 and 9 dpc (PubMed:18448090). Detected at 9.5 dpc
CC in embryonic midbrain adjacent to the boundary between midbrain and
CC forebrain (PubMed:16872596). At 10.5 dpc, expression is also detected
CC in the eye, throughout the brain, the dorsal root ganglia and
CC trigeminal ganglia, and in cells adjacent to the urogenital ridge in
CC the torso (PubMed:16872596, PubMed:18448090). At 11 dpc, expression in
CC midbrain is tightly restricted to the boundary between midbrain and
CC hindbrain (PubMed:16872596). {ECO:0000269|PubMed:16872596}.
CC -!- INDUCTION: Up-regulated by FGF2. {ECO:0000269|PubMed:16872596}.
CC -!- PTM: Phosphorylated in response to FGFR1 signaling, but is not a direct
CC substrate of FGFR1 or SRC. A mutant where the Tyr phosphorylation sites
CC have been replaced by Phe displays constitutive FGFR1-dependent
CC activation of downstream MAP kinases. {ECO:0000269|PubMed:20421966}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16872596,
CC ECO:0000269|PubMed:21673655}.
CC -!- PTM: Proteolytic cleavage in the juxtamembrane region gives rise to a
CC soluble ectodomain. {ECO:0000269|PubMed:21673655}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH70403.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI11880.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI12384.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI38215.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAR92201.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE20477.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EDL33290.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY495667; AAR92200.1; -; mRNA.
DR EMBL; AY495668; AAR92201.1; ALT_INIT; mRNA.
DR EMBL; AK031503; BAE20477.1; ALT_INIT; mRNA.
DR EMBL; AC109619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466612; EDL33290.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC070403; AAH70403.1; ALT_INIT; mRNA.
DR EMBL; BC111879; AAI11880.1; ALT_INIT; mRNA.
DR EMBL; BC112383; AAI12384.1; ALT_INIT; mRNA.
DR EMBL; BC138214; AAI38215.1; ALT_INIT; mRNA.
DR RefSeq; NP_958813.1; NM_201411.2.
DR RefSeq; XP_006527232.1; XM_006527169.2.
DR RefSeq; XP_006527233.1; XM_006527170.3.
DR RefSeq; XP_006527234.1; XM_006527171.3.
DR AlphaFoldDB; Q6RKD8; -.
DR SMR; Q6RKD8; -.
DR STRING; 10090.ENSMUSP00000109010; -.
DR GlyConnect; 2475; 1 N-Linked glycan (1 site).
DR GlyGen; Q6RKD8; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q6RKD8; -.
DR PhosphoSitePlus; Q6RKD8; -.
DR PaxDb; Q6RKD8; -.
DR PRIDE; Q6RKD8; -.
DR ProteomicsDB; 273002; -.
DR DNASU; 396184; -.
DR GeneID; 396184; -.
DR KEGG; mmu:396184; -.
DR UCSC; uc008gkh.3; mouse.
DR CTD; 23769; -.
DR MGI; MGI:3026647; Flrt1.
DR eggNOG; ENOG502QWDS; Eukaryota.
DR HOGENOM; CLU_027624_0_0_1; -.
DR InParanoid; Q6RKD8; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q6RKD8; -.
DR TreeFam; TF331598; -.
DR Reactome; R-MMU-5654687; Downstream signaling of activated FGFR1.
DR BioGRID-ORCS; 396184; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Flrt1; mouse.
DR PRO; PR:Q6RKD8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6RKD8; protein.
DR Genevisible; Q6RKD8; MM.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0044306; C:neuron projection terminus; IDA:UniProtKB.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005104; F:fibroblast growth factor receptor binding; IPI:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016358; P:dendrite development; IMP:UniProtKB.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:1990138; P:neuron projection extension; IMP:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS51450; LRR; 8.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cell membrane; Cell projection; Cytoplasm;
KW Cytoplasmic vesicle; Developmental protein; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Leucine-rich repeat; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..646
FT /note="Leucine-rich repeat transmembrane protein FLRT1"
FT /id="PRO_0000434522"
FT TOPO_DOM 24..524
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 546..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 26..52
FT /note="LRRNT"
FT /evidence="ECO:0000255"
FT REPEAT 53..77
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 78..98
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 99..121
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 123..147
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 148..169
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 170..192
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 194..218
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 219..241
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 242..264
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 265..288
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT DOMAIN 300..351
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT DOMAIN 409..504
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT MOD_RES 572
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:20421966"
FT MOD_RES 605
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:20421966"
FT MOD_RES 643
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:20421966"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..32
FT /evidence="ECO:0000250|UniProtKB:Q8BGT1"
FT DISULFID 30..39
FT /evidence="ECO:0000250|UniProtKB:Q8BGT1"
FT DISULFID 304..329
FT /evidence="ECO:0000250|UniProtKB:Q8BGT1"
FT MUTAGEN 572
FT /note="Y->F: Decreases phosphorylation. Nearly abolishes
FT phosphorylation; when associated with F-605 and F-643."
FT /evidence="ECO:0000269|PubMed:20421966"
FT MUTAGEN 605
FT /note="Y->F: Decreases phosphorylation. Nearly abolishes
FT phosphorylation; when associated with F-572 and F-643."
FT /evidence="ECO:0000269|PubMed:20421966"
FT MUTAGEN 643
FT /note="Y->F: Decreases phosphorylation. Nearly abolishes
FT phosphorylation; when associated with F-572 and F-605."
FT /evidence="ECO:0000269|PubMed:20421966"
FT CONFLICT 453
FT /note="T -> I (in Ref. 5; AAI11880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 646 AA; 71492 MW; 628B5CAEF3D88E5E CRC64;
MDLRDWLFLC YGLIAFLTEV IDSTTCPSVC RCDNGFIYCN DRGLTSIPSD IPDDATTLYL
QNNQINNAGI PQDLKTKVKV QVIYLYENDL DEFPINLPRS LRELHLQDNN VRTIARDSLA
RIPLLEKLHL DDNSVSTVSI EEDAFADSKQ LKLLFLSRNH LSSIPSGLPH TLEELRLDDN
RISTIPLHAF KGLNSLRRLV LDGNLLANQR IADDTFSRLQ NLTELSLVRN SLAAPPLNLP
SAHLQKLYLQ DNAISHIPYN TLAKMRELER LDLSNNNLTT LPRGLFDDLG NLAQLLLRNN
PWFCGCNLMW LRDWVRARAA VVNVRGLMCQ GPEKVRGMAI KDITSEMDEC FEAGSQGGAA
NAAAKTTVSN HASATTPQGS LFTLKAKRPG LRLPDSNIDY PMATGDGAKT LVIQVKPLTA
DSIRITWKAM LPASSFRLSW LRLGHSPAVG SITETLVQGD KTEYLLTALE PKSTYIICMV
TMETGNTYVA DETPVCAKAE TADSYGPTTT LNQEQNAGPM AGLPLAGIIG GAVALVFLFL
VLGAICWYVH RAGELLTRER VYNRGSRRKD DYMESGTKKD NSILEIRGPG LQMLPINPYR
SKEEYVVHTI FPSNGSSLCK GAHTIGYGTT RGYREAGIPD VDYSYT
