NEO1_MOUSE
ID NEO1_MOUSE Reviewed; 1493 AA.
AC P97798;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Neogenin;
DE Flags: Precursor;
GN Name=Neo1; Synonyms=Ngn;
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], AND ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=9264410; DOI=10.1038/sj.onc.1201225;
RA Keeling S.L., Gad J.M., Cooper H.M.;
RT "Mouse neogenin, a DCC-like molecule, has four splice variants and is
RT expressed widely in the adult mouse and during embryogenesis.";
RL Oncogene 15:691-700(1997).
RN [2]
RP INTERACTION WITH RGMA.
RX PubMed=17389603; DOI=10.1074/jbc.m610901200;
RA Conrad S., Genth H., Hofmann F., Just I., Skutella T.;
RT "Neogenin-RGMa signaling at the growth cone is bone morphogenetic protein-
RT independent and involves RhoA, ROCK, and PKC.";
RL J. Biol. Chem. 282:16423-16433(2007).
RN [3]
RP INTERACTION WITH MYO10.
RX PubMed=17237772; DOI=10.1038/ncb1535;
RA Zhu X.J., Wang C.Z., Dai P.G., Xie Y., Song N.N., Liu Y., Du Q.S., Mei L.,
RA Ding Y.Q., Xiong W.C.;
RT "Myosin X regulates netrin receptors and functions in axonal path-
RT finding.";
RL Nat. Cell Biol. 9:184-192(2007).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221 AND ASN-501.
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 [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221; ASN-501 AND ASN-670.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1209; SER-1225; THR-1229;
RP SER-1464 AND SER-1467, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Testis;
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 883-1134 IN COMPLEX WITH HUMAN
RP RGMB, AND FUNCTION.
RX PubMed=23744777; DOI=10.1126/science.1232322;
RA Bell C.H., Healey E., van Erp S., Bishop B., Tang C., Gilbert R.J.,
RA Aricescu A.R., Pasterkamp R.J., Siebold C.;
RT "Structure of the repulsive guidance molecule (RGM)-neogenin signaling
RT hub.";
RL Science 341:77-80(2013).
CC -!- FUNCTION: Multi-functional cell surface receptor regulating cell
CC adhesion in many diverse developmental processes, including neural tube
CC and mammary gland formation, myogenesis and angiogenesis. Receptor for
CC members of the BMP, netrin, and repulsive guidance molecule (RGM)
CC families. Netrin-Neogenin interactions result in a chemoattractive axon
CC guidance response and cell-cell adhesion, the interaction between
CC NEO1/Neogenin and RGMa and RGMb induces a chemorepulsive response.
CC {ECO:0000269|PubMed:23744777}.
CC -!- SUBUNIT: Interacts with BMP2, BMP4, BMP6, and BMP7 (By similarity).
CC Interacts with RGMA and RGMB. Interacts with MYO10. {ECO:0000250,
CC ECO:0000269|PubMed:17237772, ECO:0000269|PubMed:17389603,
CC ECO:0000269|PubMed:23744777}.
CC -!- INTERACTION:
CC P97798; F8VQB6: Myo10; NbExp=3; IntAct=EBI-774991, EBI-6445959;
CC P97798; Q6NW40: RGMB; Xeno; NbExp=2; IntAct=EBI-774991, EBI-16155464;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P97798-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P97798-2; Sequence=VSP_002594;
CC Name=3;
CC IsoId=P97798-3; Sequence=VSP_002595;
CC Name=4;
CC IsoId=P97798-4; Sequence=VSP_002596;
CC Name=5;
CC IsoId=P97798-5; Sequence=VSP_002597;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously throughout the mid to late
CC stages of gestation and in adult tissues. Strong expression is observed
CC in the ventral region of the ventricular zone of the 15.5 dpc mouse
CC neural tube, as well as in the ventricular zones of the mesencephalon
CC and rhombencephalon. Isoform 3 and isoform 4 are expressed at higher
CC level compared to other isoforms between 11.5 dpc and 16.5 dpc.
CC -!- DOMAIN: The Fibronectin repeats 5 and 6 mediate interaction with RGM
CC family molecules.
CC -!- MISCELLANEOUS: [Isoform 3]: Expression developmentally regulated.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Expression developmentally regulated.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Expression developmentally regulated.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. DCC family.
CC {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; Y09535; CAA70727.1; -; mRNA.
DR PDB; 4BQ6; X-ray; 2.30 A; A/B=883-1133.
DR PDB; 4BQ7; X-ray; 6.60 A; A/B=883-1133.
DR PDB; 4BQ8; X-ray; 2.80 A; A=883-1083.
DR PDB; 4BQ9; X-ray; 2.91 A; A/B=883-1083.
DR PDB; 4BQB; X-ray; 2.70 A; A/B/C/D=883-1133.
DR PDB; 4BQC; X-ray; 3.20 A; A/B=883-1133.
DR PDB; 4PLN; X-ray; 3.20 A; C/D=765-980.
DR PDB; 4UI2; X-ray; 3.15 A; A=883-1133.
DR PDB; 6Z3M; X-ray; 5.50 A; E/F/K/L/Q/R=883-1134.
DR PDBsum; 4BQ6; -.
DR PDBsum; 4BQ7; -.
DR PDBsum; 4BQ8; -.
DR PDBsum; 4BQ9; -.
DR PDBsum; 4BQB; -.
DR PDBsum; 4BQC; -.
DR PDBsum; 4PLN; -.
DR PDBsum; 4UI2; -.
DR PDBsum; 6Z3M; -.
DR AlphaFoldDB; P97798; -.
DR BMRB; P97798; -.
DR SMR; P97798; -.
DR DIP; DIP-32026N; -.
DR IntAct; P97798; 5.
DR MINT; P97798; -.
DR STRING; 10090.ENSMUSP00000063656; -.
DR GlyConnect; 2440; 1 N-Linked glycan (1 site). [P97798-4]
DR GlyConnect; 2441; 1 N-Linked glycan (1 site). [P97798-5]
DR GlyGen; P97798; 8 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; P97798; -.
DR PhosphoSitePlus; P97798; -.
DR SwissPalm; P97798; -.
DR jPOST; P97798; -.
DR MaxQB; P97798; -.
DR PaxDb; P97798; -.
DR PeptideAtlas; P97798; -.
DR PRIDE; P97798; -.
DR ProteomicsDB; 287373; -. [P97798-1]
DR ProteomicsDB; 287374; -. [P97798-2]
DR ProteomicsDB; 287375; -. [P97798-3]
DR ProteomicsDB; 287376; -. [P97798-4]
DR ProteomicsDB; 287377; -. [P97798-5]
DR MGI; MGI:1097159; Neo1.
DR eggNOG; KOG4221; Eukaryota.
DR InParanoid; P97798; -.
DR PhylomeDB; P97798; -.
DR ChiTaRS; Neo1; mouse.
DR PRO; PR:P97798; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P97798; protein.
DR GO; GO:0044295; C:axonal growth cone; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0097708; C:intracellular vesicle; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098797; C:plasma membrane protein complex; ISO:MGI.
DR GO; GO:0070700; F:BMP receptor binding; IPI:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; IDA:MGI.
DR GO; GO:0039706; F:co-receptor binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IPI:MGI.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:MGI.
DR GO; GO:0007520; P:myoblast fusion; IMP:MGI.
DR GO; GO:0048681; P:negative regulation of axon regeneration; IMP:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:0050709; P:negative regulation of protein secretion; IDA:MGI.
DR GO; GO:0001764; P:neuron migration; IBA:GO_Central.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IGI:MGI.
DR GO; GO:0009306; P:protein secretion; IDA:MGI.
DR GO; GO:0048679; P:regulation of axon regeneration; IGI:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR CDD; cd00063; FN3; 6.
DR Gene3D; 2.60.40.10; -; 10.
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; IPR033024; Neogenin.
DR InterPro; IPR010560; Neogenin_C.
DR PANTHER; PTHR44170:SF14; PTHR44170:SF14; 1.
DR Pfam; PF00041; fn3; 6.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF06583; Neogenin_C; 1.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..1493
FT /note="Neogenin"
FT /id="PRO_0000015044"
FT TOPO_DOM 37..1136
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1137..1157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1158..1493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 63..158
FT /note="Ig-like C2-type 1"
FT DOMAIN 163..249
FT /note="Ig-like C2-type 2"
FT DOMAIN 254..347
FT /note="Ig-like C2-type 3"
FT DOMAIN 352..437
FT /note="Ig-like C2-type 4"
FT DOMAIN 472..566
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 572..662
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 667..762
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 772..862
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 887..986
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 988..1085
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1072..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1229
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92859"
FT MOD_RES 1436
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92859"
FT MOD_RES 1464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92859"
FT MOD_RES 1467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 85..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 184..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 281..331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 373..421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 442..461
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002594"
FT VAR_SEQ 863..878
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_002595"
FT VAR_SEQ 1086..1096
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_002596"
FT VAR_SEQ 1279..1331
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_002597"
FT STRAND 773..780
FT /evidence="ECO:0007829|PDB:4PLN"
FT STRAND 785..793
FT /evidence="ECO:0007829|PDB:4PLN"
FT STRAND 795..797
FT /evidence="ECO:0007829|PDB:4PLN"
FT STRAND 801..810
FT /evidence="ECO:0007829|PDB:4PLN"
FT STRAND 813..819
FT /evidence="ECO:0007829|PDB:4PLN"
FT STRAND 823..827
FT /evidence="ECO:0007829|PDB:4PLN"
FT STRAND 835..844
FT /evidence="ECO:0007829|PDB:4PLN"
FT STRAND 852..857
FT /evidence="ECO:0007829|PDB:4PLN"
FT STRAND 889..895
FT /evidence="ECO:0007829|PDB:4BQ6"
FT STRAND 897..899
FT /evidence="ECO:0007829|PDB:4BQ6"
FT STRAND 901..906
FT /evidence="ECO:0007829|PDB:4BQ6"
FT STRAND 921..927
FT /evidence="ECO:0007829|PDB:4BQ6"
FT STRAND 937..948
FT /evidence="ECO:0007829|PDB:4BQ6"
FT STRAND 956..965
FT /evidence="ECO:0007829|PDB:4BQ6"
FT STRAND 968..970
FT /evidence="ECO:0007829|PDB:4BQ6"
FT STRAND 976..979
FT /evidence="ECO:0007829|PDB:4BQ6"
FT STRAND 990..997
FT /evidence="ECO:0007829|PDB:4BQ6"
FT STRAND 1000..1009
FT /evidence="ECO:0007829|PDB:4BQ6"
FT STRAND 1020..1027
FT /evidence="ECO:0007829|PDB:4BQ6"
FT HELIX 1033..1035
FT /evidence="ECO:0007829|PDB:4BQ6"
FT STRAND 1036..1042
FT /evidence="ECO:0007829|PDB:4BQ6"
FT STRAND 1047..1050
FT /evidence="ECO:0007829|PDB:4BQ6"
FT STRAND 1058..1067
FT /evidence="ECO:0007829|PDB:4BQ6"
FT STRAND 1070..1074
FT /evidence="ECO:0007829|PDB:4BQ6"
FT STRAND 1078..1081
FT /evidence="ECO:0007829|PDB:4BQ6"
SQ SEQUENCE 1493 AA; 163160 MW; 441DE919D5E17C0E CRC64;
MAAEREAGRL LCTSSSRRCC PPPPLLLLLP LLLLLGRPAS GAAATKSGPR RQSQGASVRT
FTPFYFLVEP VDTLSVRGSS VILNCSAYSE PSPNIEWKKD GTFLNLESDD RRQLLPDGSL
FISNVVHSKH NKPDEGFYQC VATVDNLGTI VSRTAKLTVA GLPRFTSQPE PSSVYVGNSA
ILNCEVNADL VPFVRWEQNR QPLLLDDRIV KLPSGTLVIS NATEGDGGLY RCIVESGGPP
KFSDEAELKV LQDPEEIVDL VFLMRPSSMM KVTGQSAVLP CVVSGLPAPV VRWMKNEEVL
DTESSGRLVL LAGGCLEISD VTEDDAGTYF CIADNGNKTV EAQAELTVQV PPGFLKQPAN
IYAHESMDIV FECEVTGKPT PTVKWVKNGD VVIPSDNFKI VKEHNLQVLG LVKSDEGFYQ
CIAENDVGNA QAGAQLIILE HDVAIPTLPP TSLTSATTDH LAPATTGPLP SAPRDVVASL
VSTRFIKLTW RTPASDPHGD NLTYSVFYTK EGVDRERVEN TSQPGEMQVT IQNLMPATVY
IFKVMAQNKH GSGESSAPLR VETQPEVQLP GPAPNIRAYA TSPTSITVTW ETPLSGNGEI
QNYKLYYMEK GTDKEQDIDV SSHSYTINGL KKYTEYSFRV VAYNKHGPGV STQDVAVRTL
SDVPSAAPQN LSLEVRNSKS IVIHWQPPSS TTQNGQITGY KIRYRKASRK SDVTETLVTG
TQLSQLIEGL DRGTEYNFRV AALTVNGTGP ATDWLSAETF ESDLDETRVP EVPSSLHVRP
LVTSIVVSWT PPENQNIVVR GYAIGYGIGS PHAQTIKVDY KQRYYTIENL DPSSHYVITL
KAFNNVGEGI PLYESAVTRP HTDTSEVDLF VINAPYTPVP DPTPMMPPVG VQASILSHDT
IRITWADNSL PKHQKITDSR YYTVRWKTNI PANTKYKNAN ATTLSYLVTG LKPNTLYEFS
VMVTKGRRSS TWSMTAHGAT FELVPTSPPK DVTVVSKEGK PRTIIVNWQP PSEANGKITG
YIIYYSTDVN AEIHDWVIEP VVGNRLTHQI QELTLDTPYY FKIQARNSKG MGPMSEAVQF
RTPKADSSDK MPNDQALGSA GKGSRLPDLG SDYKPPMSGS NSPHGSPTSP LDSNMLLVII
VSVGVITIVV VVVIAVFCTR RTTSHQKKKR AACKSVNGSH KYKGNCKDVK PPDLWIHHER
LELKPIDKSP DPNPVMTDTP IPRNSQDITP VDNSMDSNIH QRRNSYRGHE SEDSMSTLAG
RRGMRPKMMM PFDSQPPQPV ISAHPIHSLD NPHHHFHSSS LASPARSHLY HPSSPWPIGT
SMSLSDRANS TESVRNTPST DTMPASSSQT CCTDHQDPEG ATSSSYLASS QEEDSGQSLP
TAHVRPSHPL KSFAVPAIPP PGPPLYDPAL PSTPLLSQQA LEPSTFHSVK TASIGTLGRS
RPPMPVVVPS APEVQETTRM LEDSESSYEP DELTKEMAHL EGLMKDLNAI TTA
