ROBO1_MOUSE
ID ROBO1_MOUSE Reviewed; 1612 AA.
AC O89026;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 161.
DE RecName: Full=Roundabout homolog 1;
DE Flags: Precursor;
GN Name=Robo1; Synonyms=Dutt1;
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].
RC TISSUE=Brain;
RA Wu M.C., Lowe N., Fordham R., Rabbitts P.;
RT "The mouse homologue of human DUTT1/H-robo1 gene: protein sequence and
RT chromosomal location.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP POSSIBLE FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11734623; DOI=10.1073/pnas.251407098;
RA Xian J., Clark K.J., Fordham R., Pannell R., Rabbitts T.H., Rabbitts P.H.;
RT "Inadequate lung development and bronchial hyperplasia in mice with a
RT targeted deletion in the Dutt1/Robo1 gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:15062-15066(2001).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15091338; DOI=10.1016/s0896-6273(04)00179-5;
RA Long H., Sabatier C., Ma L., Plump A., Yuan W., Ornitz D.M., Tamada A.,
RA Murakami F., Goodman C.S., Tessier-Lavigne M.;
RT "Conserved roles for slit and robo proteins in midline commissural axon
RT guidance.";
RL Neuron 42:213-223(2004).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=9608531; DOI=10.1006/mcne.1998.0672;
RA Sundaresan V., Roberts I., Bateman A., Bankier A., Sheppard M., Hobbs C.,
RA Xiong J., Minna J., Latif F., Lerman M., Rabbitts P.;
RT "The DUTT1 gene, a novel NCAM family member is expressed in developing
RT murine neural tissues and has an unusually broad pattern of expression.";
RL Mol. Cell. Neurosci. 11:29-35(1998).
RN [5]
RP INTERACTION WITH SLIT1.
RX PubMed=10433822; DOI=10.1006/dbio.1999.9371;
RA Yuan W., Zhou L., Chen J.H., Wu J.Y., Rao Y., Ornitz D.M.;
RT "The mouse SLIT family: secreted ligands for ROBO expressed in patterns
RT that suggest a role in morphogenesis and axon guidance.";
RL Dev. Biol. 212:290-306(1999).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12123796; DOI=10.1016/s0014-5793(02)02904-6;
RA Clark K., Hammond E., Rabbitts P.;
RT "Temporal and spatial expression of two isoforms of the Dutt1/Robo1 gene in
RT mouse development.";
RL FEBS Lett. 523:12-16(2002).
RN [7]
RP UBIQUITINATION, AND INTERACTION WITH USP33.
RX PubMed=19684588; DOI=10.1038/nn.2382;
RA Yuasa-Kawada J., Kinoshita-Kawada M., Wu G., Rao Y., Wu J.Y.;
RT "Midline crossing and Slit responsiveness of commissural axons require
RT USP33.";
RL Nat. Neurosci. 12:1087-1089(2009).
RN [8]
RP INTERACTION WITH USP33.
RX PubMed=19706539; DOI=10.1073/pnas.0801262106;
RA Yuasa-Kawada J., Kinoshita-Kawada M., Rao Y., Wu J.Y.;
RT "Deubiquitinating enzyme USP33/VDU1 is required for Slit signaling in
RT inhibiting breast cancer cell migration.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14530-14535(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
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).
RN [10]
RP INTERACTION WITH FLRT3, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=24560577; DOI=10.1016/j.cub.2014.01.042;
RA Leyva-Diaz E., del Toro D., Menal M.J., Cambray S., Susin R.,
RA Tessier-Lavigne M., Klein R., Egea J., Lopez-Bendito G.;
RT "FLRT3 is a Robo1-interacting protein that determines Netrin-1 attraction
RT in developing axons.";
RL Curr. Biol. 24:494-508(2014).
CC -!- FUNCTION: Receptor for SLIT1 and SLIT2 that mediates cellular responses
CC to molecular guidance cues in cellular migration, including axonal
CC navigation at the ventral midline of the neural tube and projection of
CC axons to different regions during neuronal development
CC (PubMed:10433822, PubMed:24560577). Interaction with the intracellular
CC domain of FLRT3 mediates axon attraction towards cells expressing NTN1
CC (PubMed:24560577). In axon growth cones, the silencing of the
CC attractive effect of NTN1 by SLIT2 may require the formation of a
CC ROBO1-DCC complex (By similarity). Plays a role in the regulation of
CC cell migration via its interaction with MYO9B; inhibits MYO9B-mediated
CC stimulation of RHOA GTPase activity, and thereby leads to increased
CC levels of active, GTP-bound RHOA (By similarity). May be required for
CC lung development (PubMed:11734623). {ECO:0000250|UniProtKB:Q9Y6N7,
CC ECO:0000269|PubMed:10433822, ECO:0000269|PubMed:11734623,
CC ECO:0000269|PubMed:15091338, ECO:0000269|PubMed:24560577}.
CC -!- SUBUNIT: Homodimer. Dimerization is mediated by the extracellular
CC domain and is independent of SLIT liganding (By similarity). Interacts
CC with SLIT1 (PubMed:10433822) Interacts with SLIT2 (By similarity).
CC Interacts with FLRT3 (PubMed:24560577). Interacts with MYO9B (via Rho-
CC GAP domain) (By similarity). {ECO:0000250|UniProtKB:Q9Y6N7,
CC ECO:0000269|PubMed:10433822, ECO:0000269|PubMed:19684588,
CC ECO:0000269|PubMed:19706539, ECO:0000269|PubMed:24560577}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24560577};
CC Single-pass type I membrane protein {ECO:0000305}. Cell projection,
CC axon {ECO:0000269|PubMed:24560577}. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000250|UniProtKB:O55005};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:O55005}.
CC Note=Detected at growth cones in thalamus neurons (PubMed:24560577).
CC PRRG4 prevents cell surface location and both colocalize in the
CC Endoplasmic reticulum/Golgi adjacent to the cell nucleus (By
CC similarity). {ECO:0000250|UniProtKB:O55005,
CC ECO:0000269|PubMed:24560577}.
CC -!- TISSUE SPECIFICITY: Detected in embryonic thalamus neurons (at protein
CC level) (PubMed:24560577). Expressed in embryonal spinal chord.
CC Expressed in embryonal lung, and in adult lung bronchial epithelial
CC cells of large proximal airways. {ECO:0000269|PubMed:12123796,
CC ECO:0000269|PubMed:15091338, ECO:0000269|PubMed:24560577}.
CC -!- DEVELOPMENTAL STAGE: Earliest and highest expression at 11 dpc.
CC Expression is detected in developing somits, brain, neural tube, and
CC pericardiac mesenchyme. By in situ hybridization is detected in
CC marginal zones bordering the mitotically active periventricular region,
CC weakly extending to the ventral aspect impinging on motor neuron
CC columns. Also detected in the ventral third of the developing neural
CC tube, and in spinal cord throughout the full length of the neural tube.
CC Also detected at 17.5 dpc in lung mesenchyme. Expressed at 11.5 dpc in
CC spinal cord, predominantly localized to postcrossing commissural axons.
CC {ECO:0000269|PubMed:12123796, ECO:0000269|PubMed:15091338,
CC ECO:0000269|PubMed:9608531}.
CC -!- PTM: Ubiquitinated. May be deubiquitinated by USP33.
CC {ECO:0000269|PubMed:19684588}.
CC -!- DISRUPTION PHENOTYPE: Mice show defects in commissural axon guidance in
CC spinal cord including midline recrossing and an altered lateral and
CC ventral funiculi projection. The phenotype resembles that of a
CC SLIT1;SLIT2;SLIT3 triple mutant. They also mimick a naturally occurring
CC human homozygous deletion mutant detected in a small lung cancer cell
CC line, frequently die at birth by respiratory failure with accompanying
CC abnormal lung histology. Surviving mice develop bronchial hyperplasia.
CC {ECO:0000269|PubMed:11734623}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ROBO family.
CC {ECO:0000305}.
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DR EMBL; Y17793; CAA76850.1; -; mRNA.
DR CCDS; CCDS37376.1; -.
DR PIR; T30805; T30805.
DR RefSeq; NP_062286.2; NM_019413.2.
DR AlphaFoldDB; O89026; -.
DR SMR; O89026; -.
DR BioGRID; 202949; 7.
DR STRING; 10090.ENSMUSP00000023600; -.
DR GlyConnect; 2687; 1 N-Linked glycan (1 site).
DR GlyGen; O89026; 5 sites, 1 N-linked glycan (1 site).
DR iPTMnet; O89026; -.
DR PhosphoSitePlus; O89026; -.
DR MaxQB; O89026; -.
DR PaxDb; O89026; -.
DR PRIDE; O89026; -.
DR ProteomicsDB; 260915; -.
DR DNASU; 19876; -.
DR GeneID; 19876; -.
DR KEGG; mmu:19876; -.
DR CTD; 6091; -.
DR MGI; MGI:1274781; Robo1.
DR eggNOG; KOG4222; Eukaryota.
DR InParanoid; O89026; -.
DR OrthoDB; 45439at2759; -.
DR PhylomeDB; O89026; -.
DR Reactome; R-MMU-376176; Signaling by ROBO receptors.
DR Reactome; R-MMU-428890; Role of ABL in ROBO-SLIT signaling.
DR Reactome; R-MMU-8985586; SLIT2:ROBO1 increases RHOA activity.
DR Reactome; R-MMU-9010553; Regulation of expression of SLITs and ROBOs.
DR BioGRID-ORCS; 19876; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Robo1; mouse.
DR PRO; PR:O89026; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O89026; protein.
DR GO; GO:0030673; C:axolemma; IDA:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008046; F:axon guidance receptor activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030275; F:LRR domain binding; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0035904; P:aorta development; IGI:BHF-UCL.
DR GO; GO:0003180; P:aortic valve morphogenesis; IGI:BHF-UCL.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0016199; P:axon midline choice point recognition; IGI:UniProtKB.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0021836; P:chemorepulsion involved in postnatal olfactory bulb interneuron migration; ISO:MGI.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR GO; GO:0003272; P:endocardial cushion formation; IGI:BHF-UCL.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0060763; P:mammary duct terminal end bud growth; IMP:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; ISO:MGI.
DR GO; GO:0050925; P:negative regulation of negative chemotaxis; ISO:MGI.
DR GO; GO:0021891; P:olfactory bulb interneuron development; IGI:UniProtKB.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; IGI:BHF-UCL.
DR GO; GO:0050772; P:positive regulation of axonogenesis; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0035481; P:positive regulation of Notch signaling pathway involved in heart induction; IDA:BHF-UCL.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; ISO:MGI.
DR GO; GO:0003184; P:pulmonary valve morphogenesis; IGI:BHF-UCL.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:0035385; P:Roundabout signaling pathway; ISS:UniProtKB.
DR GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IGI:BHF-UCL.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 8.
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; IPR013106; Ig_V-set.
DR InterPro; IPR032986; Robo1.
DR PANTHER; PTHR12231:SF243; PTHR12231:SF243; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SMART; SM00406; IGv; 3.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Chemotaxis; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Neurogenesis; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1612
FT /note="Roundabout homolog 1"
FT /id="PRO_0000031034"
FT TOPO_DOM 20..858
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 859..879
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 880..1612
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..125
FT /note="Ig-like C2-type 1"
FT DOMAIN 131..218
FT /note="Ig-like C2-type 2"
FT DOMAIN 223..307
FT /note="Ig-like C2-type 3"
FT DOMAIN 312..407
FT /note="Ig-like C2-type 4"
FT DOMAIN 416..502
FT /note="Ig-like C2-type 5"
FT DOMAIN 524..618
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 637..734
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 739..835
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1045..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1515..1538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1551..1582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 901
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT MOD_RES 909
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT MOD_RES 999
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT MOD_RES 1016
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT MOD_RES 1034
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT MOD_RES 1075
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT MOD_RES 1201
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT MOD_RES 1258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 781
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 788
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 152..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 244..291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 333..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 437..486
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1612 AA; 176407 MW; 5F2988C544796B4B CRC64;
MIAEPAHFYL FGLICLCSGS RLRQEDFPPR IVEHPSDLIV SKGEPATLNC KAEGRPTPTI
EWYKGGERVE TDKDDPRSHR MLLPSGSLFF LRIVHGRKSR PDEGVYICVA RNYLGEAVSH
NASLEVAILR DDFRQNPSDV MVAVGEPAVM ECQPPRGHPE PTISWKKDGS PLDDKDERIT
IRGGKLMITY TRKSDAGKYV CVGTNMVGER ESEVAELTVL ERPSFVKRPS NLAVTVDDSA
EFKCEARGDP VPTVRWRKDD GELPKSRYEI RDDHTLKIRK VTAGDMGSYT CVAENMVGKA
EASATLTVQE PPHFVVKPRD QVVALGRTVT FQCEATGNPQ PAIFWRREGS QNLLFSYQPP
QSSSRFSVSQ TGDLTITNVQ RSDVGYYICQ TLNVAGSIIT KAYLEVTDVI ADRPPPVIRQ
GPVNQTVAVD GTLILSCVAT GSPAPTILWR KDGVLVSTQD SRIKQLESGV LQIRYAKLGD
TGRYTCTAST PSGEATWSAY IEVQEFGVPV QPPRPTDPNL IPSAPSKPEV TDVSKNTVTL
SWQPNLNSGA TPTSYIIEAF SHASGSSWQT AAENVKTETF AIKGLKPNAI YLFLVRAANA
YGISDPSQIS DPVKTQDVPP TSQGVDHKQV QRELGNVVLH LHNPTILSSS SVEVHWTVDQ
QSQYIQGYKI LYRPSGASHG ESEWLVFEVR TPTKNSVVIP DLRKGVNYEI KARPFFNEFQ
GADSEIKFAK TLEEAPSAPP RSVTVSKNDG NGTAILVTWQ PPPEDTQNGM VQEYKVWCLG
NETKYHINKT VDGSTFSVVI PSLVPGIRYS VEVAASTGAG PGVKSEPQFI QLDSHGNPVS
PEDQVSLAQQ ISDVVRQPAF IAGIGAACWI ILMVFSIWLY RHRKKRNGLT STYAGIRKVP
SFTFTPTVTY QRGGEAVSSG GRPGLLNISE PATQPWLADT WPNTGNNHND CSINCCTAGN
GNSDSNLTTY SRPADCIANY NNQLDNKQTN LMLPESTVYG DVDLSNKINE MKTFNSPNLK
DGRFVNPSGQ PTPYATTQLI QANLSNNMNN GAGDSSEKHW KPPGQQKPEV APIQYNIMEQ
NKLNKDYRAN DTIPPTIPYN QSYDQNTGGS YNSSDRGSST SGSQGHKKGA RTPKAPKQGG
MNWADLLPPP PAHPPPHSNS EEYNMSVDES YDQEMPCPVP PAPMYLQQDE LQEEEDERGP
TPPVRGAASS PAAVSYSHQS TATLTPSPQE ELQPMLQDCP EDLGHMPHPP DRRRQPVSPP
PPPRPISPPH TYGYISGPLV SDMDTDAPEE EEDEADMEVA KMQTRRLLLR GLEQTPASSV
GDLESSVTGS MINGWGSASE EDNISSGRSS VSSSDGSFFT DADFAQAVAA AAEYAGLKVA
RRQMQDAAGR RHFHASQCPR PTSPVSTDSN MSAVVIQKAR PAKKQKHQPG HLRREAYADD
LPPPPVPPPA IKSPTVQSKA QLEVRPVMVP KLASIEARTD RSSDRKGGSY KGREALDGRQ
VTDLRTNPSD PREAQEQPND GKGRGTRQPK RDLPPAKTHL GQEDILPYCR PTFPTSNNPR
DPSSSSSMSS RGSGSRQREQ ANVGRRNMAE MQVLGGFERG DENNEELEET ES
