AGRG6_MOUSE
ID AGRG6_MOUSE Reviewed; 1165 AA.
AC Q6F3F9; Q811E4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Adhesion G-protein coupled receptor G6;
DE AltName: Full=Developmentally regulated G-protein-coupled receptor {ECO:0000303|PubMed:15189448};
DE AltName: Full=G-protein coupled receptor 126;
DE Contains:
DE RecName: Full=ADGRG6 N-terminal fragment {ECO:0000303|PubMed:24082093, ECO:0000303|PubMed:25695270};
DE Short=ADGRG6-NTF;
DE Contains:
DE RecName: Full=ADGRG6 C-terminal fragment {ECO:0000303|PubMed:24082093, ECO:0000303|PubMed:25695270};
DE Short=ADGRG6-CTF;
DE Flags: Precursor;
GN Name=Adgrg6 {ECO:0000312|MGI:MGI:1916151}; Synonyms=Dreg, Gm222, Gpr126;
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], PROTEIN SEQUENCE OF 441-447 AND 811-814,
RP PROTEOLYTIC PROCESSING, AND TISSUE SPECIFICITY.
RX PubMed=15189448; DOI=10.1111/j.1356-9597.2004.00743.x;
RA Moriguchi T., Haraguchi K., Ueda N., Okada M., Furuya T., Akiyama T.;
RT "DREG, a developmentally regulated G protein-coupled receptor containing
RT two conserved proteolytic cleavage sites.";
RL Genes Cells 9:549-560(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 965-1165.
RC STRAIN=FVB/N-3; 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 [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-314.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1135 AND SER-1138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=21124978; DOI=10.1371/journal.pone.0014047;
RA Waller-Evans H., Proemel S., Langenhan T., Dixon J., Zahn D.,
RA Colledge W.H., Doran J., Carlton M.B., Davies B., Aparicio S.A., Grosse J.,
RA Russ A.P.;
RT "The orphan adhesion-GPCR GPR126 is required for embryonic development in
RT the mouse.";
RL PLoS ONE 5:E14047-E14047(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21613327; DOI=10.1242/dev.062224;
RA Monk K.R., Oshima K., Joers S., Heller S., Talbot W.S.;
RT "Gpr126 is essential for peripheral nerve development and myelination in
RT mammals.";
RL Development 138:2673-2680(2011).
RN [7]
RP FUNCTION.
RX PubMed=24227709; DOI=10.1523/jneurosci.1809-13.2013;
RA Mogha A., Benesh A.E., Patra C., Engel F.B., Schoeneberg T., Liebscher I.,
RA Monk K.R.;
RT "Gpr126 functions in Schwann cells to control differentiation and
RT myelination via G-protein activation.";
RL J. Neurosci. 33:17976-17985(2013).
RN [8]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION (ADGRG6 N-TERMINAL
RP FRAGMENT).
RX PubMed=24082093; DOI=10.1073/pnas.1304837110;
RA Patra C., van Amerongen M.J., Ghosh S., Ricciardi F., Sajjad A.,
RA Novoyatleva T., Mogha A., Monk K.R., Muehlfeld C., Engel F.B.;
RT "Organ-specific function of adhesion G protein-coupled receptor GPR126 is
RT domain-dependent.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:16898-16903(2013).
RN [9]
RP INTERACTION WITH LAMININ-2/LAMININ-211, AND FUNCTION (ADGRG6 N-TERMINAL
RP FRAGMENT).
RX PubMed=25695270; DOI=10.1016/j.neuron.2014.12.057;
RA Petersen S.C., Luo R., Liebscher I., Giera S., Jeong S.J., Mogha A.,
RA Ghidinelli M., Feltri M.L., Schoeneberg T., Piao X., Monk K.R.;
RT "The adhesion GPCR GPR126 has distinct, domain-dependent functions in
RT Schwann cell development mediated by interaction with laminin-211.";
RL Neuron 85:755-769(2015).
RN [10]
RP INTERACTION WITH PRNP, AND FUNCTION.
RX PubMed=27501152; DOI=10.1038/nature19312;
RA Kueffer A., Lakkaraju A.K., Mogha A., Petersen S.C., Airich K.,
RA Doucerain C., Marpakwar R., Bakirci P., Senatore A., Monnard A.,
RA Schiavi C., Nuvolone M., Grosshans B., Hornemann S., Bassilana F.,
RA Monk K.R., Aguzzi A.;
RT "The prion protein is an agonistic ligand of the G protein-coupled receptor
RT Adgrg6.";
RL Nature 536:464-468(2016).
CC -!- FUNCTION: G-protein coupled receptor which is activated by type IV
CC collagen, a major constituent of the basement membrane. Essential for
CC normal differentiation of promyelinating Schwann cells and for normal
CC myelination of axons these functions are mediated via G-protein-
CC signaling pathways (PubMed:24227709, PubMed:21613327). Regulates also
CC neural, cardiac and ear development via G-protein- and/or N-terminus-
CC dependent signaling. May act as a receptor for PRNP which may promote
CC myelin homeostasis (PubMed:27501152). {ECO:0000250|UniProtKB:C6KFA3,
CC ECO:0000250|UniProtKB:Q86SQ4, ECO:0000269|PubMed:21613327,
CC ECO:0000269|PubMed:24227709, ECO:0000269|PubMed:27501152}.
CC -!- FUNCTION: [ADGRG6 N-terminal fragment]: Plays an important role in
CC heart developmention (PubMed:24082093). Necessary and sufficient for
CC axon sorting by Schwann cells independently of the ADGRG6-CTF
CC (PubMed:25695270). {ECO:0000269|PubMed:24082093,
CC ECO:0000269|PubMed:25695270}.
CC -!- SUBUNIT: Interacts with Laminin-2; this interaction stabilizes the
CC receptor in an inactive state (PubMed:25695270). Laminin-2
CC polymerization could facilitate ADGRG6-NTF removal, thereby exposing
CC the tethered agonist to drive myelination (PubMed:25695270). Interacts
CC with PRNP (PubMed:27501152). {ECO:0000269|PubMed:25695270,
CC ECO:0000269|PubMed:27501152}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86SQ4};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the heart, somite and
CC otic vesicle during embryogenesis and in adult lung.
CC {ECO:0000269|PubMed:15189448, ECO:0000269|PubMed:24082093}.
CC -!- PTM: Proteolytically cleaved into 2 conserved sites: one in the GPS
CC domain (S1 site) and the other in the middle of the extracellular
CC domain (S2 site). The proteolytic cleavage at S1 site generates an N-
CC terminal fragment (NTF) and a seven-transmembrane-containing C-terminal
CC fragment (CTF). The membrane-bound CTF can act as an independent
CC receptor and the soluble NTF can act as a ligand or coreceptor. Furin
CC is involved in the cleavage of the S2 site generating a soluble
CC fragment. Processing at the GPS domain occurred independent of and
CC probably prior to the cleavage at the S2 site. Proteolytic cleavage is
CC required for activation of the receptor (By similarity).
CC {ECO:0000250|UniProtKB:Q86SQ4}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice die during organogenesis. Mutant
CC embryos show signs of myocardial wall thinning, hypotrabeculation,
CC defective mitochondrial and circulatory failure.
CC {ECO:0000269|PubMed:21124978, ECO:0000269|PubMed:24082093}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
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DR EMBL; AB183545; BAD27570.1; -; mRNA.
DR EMBL; BC046534; AAH46534.1; -; mRNA.
DR CCDS; CCDS35848.1; -.
DR RefSeq; NP_001002268.1; NM_001002268.3.
DR AlphaFoldDB; Q6F3F9; -.
DR SMR; Q6F3F9; -.
DR STRING; 10090.ENSMUSP00000043055; -.
DR GlyGen; Q6F3F9; 23 sites.
DR iPTMnet; Q6F3F9; -.
DR PhosphoSitePlus; Q6F3F9; -.
DR CPTAC; non-CPTAC-3685; -.
DR MaxQB; Q6F3F9; -.
DR PaxDb; Q6F3F9; -.
DR PeptideAtlas; Q6F3F9; -.
DR PRIDE; Q6F3F9; -.
DR ProteomicsDB; 282039; -.
DR Antibodypedia; 1571; 216 antibodies from 28 providers.
DR Ensembl; ENSMUST00000041168; ENSMUSP00000043055; ENSMUSG00000039116.
DR GeneID; 215798; -.
DR KEGG; mmu:215798; -.
DR UCSC; uc007elk.1; mouse.
DR CTD; 57211; -.
DR MGI; MGI:1916151; Adgrg6.
DR VEuPathDB; HostDB:ENSMUSG00000039116; -.
DR eggNOG; KOG3714; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000155621; -.
DR HOGENOM; CLU_002753_3_3_1; -.
DR InParanoid; Q6F3F9; -.
DR OMA; SNLSCDV; -.
DR OrthoDB; 148879at2759; -.
DR PhylomeDB; Q6F3F9; -.
DR TreeFam; TF321769; -.
DR Reactome; R-MMU-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination.
DR BioGRID-ORCS; 215798; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Adgrg6; mouse.
DR PRO; PR:Q6F3F9; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6F3F9; protein.
DR Bgee; ENSMUSG00000039116; Expressed in otolith organ and 191 other tissues.
DR ExpressionAtlas; Q6F3F9; baseline and differential.
DR Genevisible; Q6F3F9; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
DR GO; GO:0050840; F:extracellular matrix binding; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0043236; F:laminin binding; IMP:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0019933; P:cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0060347; P:heart trabecula formation; IMP:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR GO; GO:0022011; P:myelination in peripheral nervous system; IMP:UniProtKB.
DR GO; GO:0014037; P:Schwann cell differentiation; ISO:MGI.
DR CDD; cd00041; CUB; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR Gene3D; 2.60.220.50; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR001759; Pentraxin-related.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00159; PTX; 1.
DR SUPFAM; SSF111418; SSF111418; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS51828; PTX_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1165
FT /note="Adhesion G-protein coupled receptor G6"
FT /id="PRO_0000303888"
FT CHAIN 31..440
FT /note="ADGRG6 N-terminal fragment"
FT /evidence="ECO:0000305|PubMed:15189448"
FT /id="PRO_0000438598"
FT CHAIN 441..1165
FT /note="ADGRG6 C-terminal fragment"
FT /evidence="ECO:0000305|PubMed:15189448"
FT /id="PRO_0000438599"
FT TOPO_DOM 31..832
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 833..853
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 854..873
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 874..894
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 895..899
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 900..920
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 921..940
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 941..961
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 962..994
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 995..1015
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1016..1039
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1040..1060
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1061..1062
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1063..1083
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1084..1165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..149
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 154..356
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT DOMAIN 770..822
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 41..822
FT /note="Inhibits receptor signaling in absence of type IV
FT collagen"
FT /evidence="ECO:0000250|UniProtKB:C6KFA3"
FT REGION 41..355
FT /note="Mediates interaction with type IV collagen"
FT /evidence="ECO:0000250|UniProtKB:C6KFA3"
FT REGION 446..807
FT /note="Mediates interaction with laminin-2"
FT /evidence="ECO:0000269|PubMed:25695270"
FT REGION 1126..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 812..820
FT /note="STACHEL"
FT /evidence="ECO:0000250|UniProtKB:Q86SQ4"
FT SITE 440..441
FT /note="Cleavage; by furin like-convertase"
FT /evidence="ECO:0000269|PubMed:15489334"
FT SITE 810..811
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:15489334"
FT MOD_RES 1135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
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 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 746
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 41..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 94..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 186..254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
SQ SEQUENCE 1165 AA; 129721 MW; B5CC5CDEAA42CB50 CRC64;
MMFDTLGKRC CPWRLKPSAL LFLFVLCVTC VPLSVCGCGS CRLVLSNPSG TFTSPCYPND
YPNTQSCSWT LRAPAGYIIQ ITFNDFDIEE APNCIYDSLS LDNGESQTKF CGATAKGLSF
NSSVNEMHVS FSSDFSIQKK GFNASYIRVA VSLRNQKVIL PQTLDAYQVS VAKSISIPEL
KAFTLCFEAS KVGNEGGDWT AFSYSDESLT QLLSLEKASN GYFLSISGSR CLLNNALPVK
DKEDIFTENL EQLCLVWNNS WGSIGINFKK NYETVPCDST ISAVVPGDGT LLLGSDRDEV
ASLRGSIYNF RLWNFTMDLK ALSNLSCSVS GNVIDWHNDF WSISTQALKA EGNLSCGSYL
IQLPAAELTN CSELGTLCQD GIMYRISVVI HNDFNHPEVK VQTKVAEWLN STFQNWNYTV
YVVNISFHQK VGEDRMKVKR DIMDDDKRLV LWALLVYNAT NNVSLNEEKI KQKLMTNNAS
LEDGLRLCEV DVNQLGMCSA LEDPDGFSWP ATLPSVYKQP CPNKPGFFMT RACLSNGTST
FWGPVDTSNC SRQSNEVANE ILNQTGDGQN LTSANINSIV EKVKRIVNKE ENIDITLGST
LMNIFSNILS SSDSDLLESS TEALKTIDEL AFKIDLNSTP HVNIETQNLA LGVSSLIPGT
NAPSNFSIGL PSNNESYFQM DFGNGQTDPL ASVILPPNLL ENLSPEDSVL VRRAQFTFFN
KTGLFQDVGS QRKVLVSYVM ACSIGNITIQ NLKDPVQIKI KHTRTQEVHH PICAFWDMNK
NKSFGGWNTS GCVAHSDLDA GETICLCSHF THFGVLMDLP RSASQIDGRN TKVLTFITYI
GCGISAIFSA ATLLTYVAFE KLRRDYPSKI LMNLSSALLF LNLIFLLDGW VTSFGVAGLC
TAVAALLHFF LLATFTWMGL EAIHMYIALV KVFNTYIHRY ILKFCIIGWG LPALVVSIIL
VSRRQNEVYG KESYGKDQDD EFCWIQDPVV FYVSCAGYFG VMFFLNVAMF IVVMVQICGR
NGKRSNRTLR EEVLRNLRSV VSLTFLLGMT WGFAFFAWGP LNIPFMYLFS IFNSLQGLFI
FIFHCAMKEN VQKQWRRHLC CGRFRLADNS DWSKTATNII KKSSDNLGKS LSSSSIGSNS
TYLTSKSKSS STTYFKRNSH SDNFS
