DCC_MOUSE
ID DCC_MOUSE Reviewed; 1447 AA.
AC P70211; G3X9X6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Netrin receptor DCC;
DE AltName: Full=Tumor suppressor protein DCC;
DE Flags: Precursor;
GN Name=Dcc;
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] (ISOFORMS A; B AND C).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8570174;
RA Cooper H.M., Armes P., Britto J., Gad J., Wilks A.F.;
RT "Cloning of the mouse homologue of the deleted in colorectal cancer gene
RT (mDCC) and its expression in the developing mouse embryo.";
RL Oncogene 11:2243-2254(1995).
RN [2]
RP SEQUENCE REVISION.
RA Cooper H.M.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
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 INTERACTION WITH PTK2/FAK1.
RX PubMed=15494734; DOI=10.1038/nn1329;
RA Li W., Lee J., Vikis H.G., Lee S.H., Liu G., Aurandt J., Shen T.L.,
RA Fearon E.R., Guan J.L., Han M., Rao Y., Hong K., Guan K.L.;
RT "Activation of FAK and Src are receptor-proximal events required for netrin
RT signaling.";
RL Nat. Neurosci. 7:1213-1221(2004).
RN [6]
RP INTERACTION WITH DSCAM.
RX PubMed=18585357; DOI=10.1016/j.cell.2008.05.030;
RA Ly A., Nikolaev A., Suresh G., Zheng Y., Tessier-Lavigne M., Stein E.;
RT "DSCAM is a netrin receptor that collaborates with DCC in mediating turning
RT responses to netrin-1.";
RL Cell 133:1241-1254(2008).
RN [7]
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).
RN [8]
RP INTERACTION WITH CBLN4.
RX PubMed=22220752; DOI=10.1111/j.1471-4159.2012.07648.x;
RA Wei P., Pattarini R., Rong Y., Guo H., Bansal P.K., Kusnoor S.V.,
RA Deutch A.Y., Parris J., Morgan J.I.;
RT "The Cbln family of proteins interact with multiple signaling pathways.";
RL J. Neurochem. 121:717-729(2012).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=28250456; DOI=10.1038/ng.3804;
RA Jamuar S.S., Schmitz-Abe K., D'Gama A.M., Drottar M., Chan W.M., Peeva M.,
RA Servattalab S., Lam A.N., Delgado M.R., Clegg N.J., Zayed Z.A., Dogar M.A.,
RA Alorainy I.A., Jamea A.A., Abu-Amero K., Griebel M., Ward W., Lein E.S.,
RA Markianos K., Barkovich A.J., Robson C.D., Grant P.E., Bosley T.M.,
RA Engle E.C., Walsh C.A., Yu T.W.;
RT "Biallelic mutations in human DCC cause developmental split-brain
RT syndrome.";
RL Nat. Genet. 49:606-612(2017).
RN [10]
RP INTERACTION WITH CBLN4.
RX PubMed=29782851; DOI=10.1016/j.brainres.2018.05.022;
RA Rong Y., Bansal P.K., Wei P., Guo H., Correia K., Parris J., Morgan J.I.;
RT "Glycosylation of Cblns attenuates their receptor binding.";
RL Brain Res. 1694:129-139(2018).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1410-1445 IN COMPLEX WITH MYO10,
RP AND INTERACTION WITH MYO10.
RX PubMed=21321230; DOI=10.1073/pnas.1016567108;
RA Wei Z., Yan J., Lu Q., Pan L., Zhang M.;
RT "Cargo recognition mechanism of myosin X revealed by the structure of its
RT tail MyTH4-FERM tandem in complex with the DCC P3 domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:3572-3577(2011).
CC -!- FUNCTION: Receptor for netrin required for axon guidance. Mediates axon
CC attraction of neuronal growth cones in the developing nervous system
CC upon ligand binding. Its association with UNC5 proteins may trigger
CC signaling for axon repulsion. It also acts as a dependence receptor
CC required for apoptosis induction when not associated with netrin
CC ligand. Implicated as a tumor suppressor gene.
CC -!- SUBUNIT: Interacts with the cytoplasmic part of UNC5A, UNC5B, UNC5C and
CC probably UNC5D (By similarity). Interacts with MAPK1 (By similarity).
CC Interacts with NTN1 (By similarity). Interacts with DSCAM
CC (PubMed:18585357). Interacts with PTK2/FAK1 (PubMed:15494734).
CC Interacts with MYO10 (PubMed:21321230). Interacts with CBLN4; this
CC interaction can be competed by NTN1 (PubMed:22220752, PubMed:29782851).
CC Interacts with SIAH1 and SIAH2 (By similarity).
CC {ECO:0000250|UniProtKB:P43146, ECO:0000250|UniProtKB:Q63155,
CC ECO:0000269|PubMed:15494734, ECO:0000269|PubMed:18585357,
CC ECO:0000269|PubMed:21321230, ECO:0000269|PubMed:22220752,
CC ECO:0000269|PubMed:29782851}.
CC -!- INTERACTION:
CC P70211; Q9ERC8: Dscam; NbExp=4; IntAct=EBI-1798863, EBI-1798601;
CC P70211; P56671: Maz; NbExp=3; IntAct=EBI-1798863, EBI-1809712;
CC P70211; P56270: MAZ; Xeno; NbExp=2; IntAct=EBI-1798863, EBI-1809742;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=A;
CC IsoId=P70211-1; Sequence=Displayed;
CC Name=C;
CC IsoId=P70211-2; Sequence=VSP_002501;
CC Name=B;
CC IsoId=P70211-3; Sequence=VSP_018807;
CC -!- TISSUE SPECIFICITY: In the embryo, expressed at high levels in the
CC developing brain and neural tube. In the embryo, expressed in
CC developing neurons of the telencephalic cortical plate and in
CC developing brainstem nuclei (PubMed:28250456). In adult, highly
CC expressed in brain with very low levels found in testis, heart and
CC thymus. Isoform C is expressed only in the embryo.
CC {ECO:0000269|PubMed:28250456}.
CC -!- DEVELOPMENTAL STAGE: Low levels in early gestation. Highest levels
CC expressed during mid gestation. Levels decrease in late gestation and
CC remain at this level in the adult.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its
CC subsequent proteasomal degradation. {ECO:0000250|UniProtKB:P43146}.
CC -!- MISCELLANEOUS: [Isoform B]: Produced by alternative initiation at Met-
CC 85 of isoform A. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. DCC family.
CC {ECO:0000305}.
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DR EMBL; X85788; CAA59786.1; -; mRNA.
DR EMBL; AC105957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC136637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC163492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC167547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC167548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC167549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466528; EDL09563.1; -; Genomic_DNA.
DR CCDS; CCDS29336.1; -. [P70211-1]
DR RefSeq; NP_031857.2; NM_007831.3. [P70211-1]
DR RefSeq; XP_006525651.1; XM_006525588.3. [P70211-2]
DR PDB; 3PZD; X-ray; 2.50 A; B=1410-1445.
DR PDB; 4PLO; X-ray; 2.90 A; B=721-942.
DR PDBsum; 3PZD; -.
DR PDBsum; 4PLO; -.
DR AlphaFoldDB; P70211; -.
DR SMR; P70211; -.
DR BioGRID; 199064; 7.
DR DIP; DIP-46587N; -.
DR IntAct; P70211; 13.
DR MINT; P70211; -.
DR STRING; 10090.ENSMUSP00000110593; -.
DR GlyConnect; 2534; 3 N-Linked glycans (2 sites).
DR GlyGen; P70211; 7 sites, 3 N-linked glycans (2 sites).
DR iPTMnet; P70211; -.
DR PhosphoSitePlus; P70211; -.
DR jPOST; P70211; -.
DR MaxQB; P70211; -.
DR PaxDb; P70211; -.
DR PeptideAtlas; P70211; -.
DR PRIDE; P70211; -.
DR ProteomicsDB; 279833; -. [P70211-1]
DR ProteomicsDB; 279834; -. [P70211-2]
DR ProteomicsDB; 279835; -. [P70211-3]
DR Antibodypedia; 3710; 304 antibodies from 39 providers.
DR DNASU; 13176; -.
DR Ensembl; ENSMUST00000073379; ENSMUSP00000073094; ENSMUSG00000060534. [P70211-2]
DR Ensembl; ENSMUST00000114943; ENSMUSP00000110593; ENSMUSG00000060534. [P70211-1]
DR GeneID; 13176; -.
DR KEGG; mmu:13176; -.
DR UCSC; uc008fop.1; mouse. [P70211-1]
DR UCSC; uc008foq.1; mouse. [P70211-2]
DR CTD; 1630; -.
DR MGI; MGI:94869; Dcc.
DR VEuPathDB; HostDB:ENSMUSG00000060534; -.
DR eggNOG; KOG4221; Eukaryota.
DR GeneTree; ENSGT00940000158867; -.
DR HOGENOM; CLU_004256_0_0_1; -.
DR InParanoid; P70211; -.
DR OMA; KVYTSMM; -.
DR PhylomeDB; P70211; -.
DR TreeFam; TF321506; -.
DR Reactome; R-MMU-373752; Netrin-1 signaling.
DR Reactome; R-MMU-418885; DCC mediated attractive signaling.
DR Reactome; R-MMU-418889; Caspase activation via Dependence Receptors in the absence of ligand.
DR BioGRID-ORCS; 13176; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Dcc; mouse.
DR PRO; PR:P70211; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P70211; protein.
DR Bgee; ENSMUSG00000060534; Expressed in cortical plate and 133 other tissues.
DR Genevisible; P70211; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0044295; C:axonal growth cone; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0032584; C:growth cone membrane; ISO:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005042; F:netrin receptor activity; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0033564; P:anterior/posterior axon guidance; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0033563; P:dorsal/ventral axon guidance; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IMP:SynGO.
DR GO; GO:1901214; P:regulation of neuron death; ISO:MGI.
DR GO; GO:0021965; P:spinal cord ventral commissure morphogenesis; IMP:MGI.
DR CDD; cd00063; FN3; 6.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR033012; DCC.
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; IPR010560; Neogenin_C.
DR PANTHER; PTHR44170:SF8; PTHR44170:SF8; 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; 5.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF49265; SSF49265; 4.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Alternative splicing; Apoptosis;
KW Developmental protein; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Tumor suppressor; Ubl conjugation.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1447
FT /note="Netrin receptor DCC"
FT /id="PRO_0000014745"
FT TOPO_DOM 26..1097
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1098..1122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1123..1447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..135
FT /note="Ig-like C2-type 1"
FT DOMAIN 139..229
FT /note="Ig-like C2-type 2"
FT DOMAIN 234..326
FT /note="Ig-like C2-type 3"
FT DOMAIN 331..416
FT /note="Ig-like C2-type 4"
FT DOMAIN 431..524
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 530..620
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 625..718
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 728..821
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 846..942
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 947..1044
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1126..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1394..1419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1178
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q63155"
FT MOD_RES 1187
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q63155"
FT MOD_RES 1267
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q63155"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
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 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 61..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 161..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 261..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 352..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..84
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:8570174"
FT /id="VSP_018807"
FT VAR_SEQ 819..838
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:8570174"
FT /id="VSP_002501"
FT CONFLICT 1138
FT /note="V -> G (in Ref. 1; CAA59786)"
FT /evidence="ECO:0000305"
FT STRAND 732..736
FT /evidence="ECO:0007829|PDB:4PLO"
FT STRAND 741..745
FT /evidence="ECO:0007829|PDB:4PLO"
FT STRAND 757..766
FT /evidence="ECO:0007829|PDB:4PLO"
FT STRAND 769..773
FT /evidence="ECO:0007829|PDB:4PLO"
FT STRAND 780..783
FT /evidence="ECO:0007829|PDB:4PLO"
FT STRAND 791..800
FT /evidence="ECO:0007829|PDB:4PLO"
FT STRAND 808..813
FT /evidence="ECO:0007829|PDB:4PLO"
FT STRAND 848..854
FT /evidence="ECO:0007829|PDB:4PLO"
FT STRAND 856..865
FT /evidence="ECO:0007829|PDB:4PLO"
FT STRAND 880..887
FT /evidence="ECO:0007829|PDB:4PLO"
FT STRAND 896..908
FT /evidence="ECO:0007829|PDB:4PLO"
FT STRAND 915..924
FT /evidence="ECO:0007829|PDB:4PLO"
FT STRAND 935..938
FT /evidence="ECO:0007829|PDB:4PLO"
FT HELIX 1416..1421
FT /evidence="ECO:0007829|PDB:3PZD"
FT HELIX 1425..1443
FT /evidence="ECO:0007829|PDB:3PZD"
SQ SEQUENCE 1447 AA; 158341 MW; F905BE27C991EA42 CRC64;
MENSLGCVWV PKLAFVLFGA SLLSAHLQVT GFQIKPFTSL HFVSEPSDAV TMRGGNVLLN
CSAESDRGVP VIKWKKDGLI LALGMDDRKQ QLPNGSLLIQ NILHSRHHKP DEGLYQCEAS
LADSGSIISR TAKVTVAGPL RFLSQTESIT AFMGDTVLLK CEVIGEPMPT IHWQKNQQDL
NPLPGDSRVV VLPSGALQIS RLQPGDSGVY RCSARNPASI RTGNEAEVRI LSDPGLHRQL
YFLQRPSNVI AIEGKDAVLE CCVSGYPPPS FTWLRGEEVI QLRSKKYSLL GGSNLLISNV
TDDDSGTYTC VVTYKNENIS ASAELTVLVP PWFLNHPSNL YAYESMDIEF ECAVSGKPVP
TVNWMKNGDV VIPSDYFQIV GGSNLRILGV VKSDEGFYQC VAENEAGNAQ SSAQLIVPKP
AIPSSSILPS APRDVLPVLV SSRFVRLSWR PPAEAKGNIQ TFTVFFSREG DNRERALNTT
QPGSLQLTVG NLKPEAMYTF RVVAYNEWGP GESSQPIKVA TQPELQVPGP VENLHAVSTS
PTSILITWEP PAYANGPVQG YRLFCTEVST GKEQNIEVDG LSYKLEGLKK FTEYTLRFLA
YNRYGPGVST DDITVVTLSD VPSAPPQNIS LEVVNSRSIK VSWLPPPSGT QNGFITGYKI
RHRKTTRRGE METLEPNNLW YLFTGLEKGS QYSFQVSAMT VNGTGPPSNW YTAETPENDL
DESQVPDQPS SLHVRPQTNC IIMSWTPPLN PNIVVRGYII GYGVGSPYAE TVRVDSKQRY
YSIERLESSS HYVISLKAFN NAGEGVPLYE SATTRSITDP TDPVDYYPLL DDFPTSGPDV
STPMLPPVGV QAVALTHEAV RVSWADNSVP KNQKTSDVRL YTVRWRTSFS ASAKYKSEDT
TSLSYTATGL KPNTMYEFSV MVTKNRRSST WSMTAHATTY EAAPTSAPKD LTVITREGKP
RAVIVSWQPP LEANGKITAY ILFYTLDKNI PIDDWIMETI SGDRLTHQIM DLSLDTMYYF
RIQARNVKGV GPLSDPILFR TLKVEHPDKM ANDQGRHGDG GYWPVDTNLI DRSTLNEPPI
GQMHPPHGSV TPQKNSNLLV ITVVTVGVLT VLVVVIVAVI CTRRSSAQQR KKRATHSVSK
RKGSQKDLRP PDLWIHHEEM EMKNIEKPTG TDPAGRDSPI QSCQDLTPVS HSQSETQMGS
KSASHSGQDT EDAGSSMSTL ERSLAARRAT RAKLMIPMEA QSSNPAVVSA IPVPTLESAQ
YPGILPSPTC GYPHPQFTLR PVPFPTLSVD RGFGAGRTQS VSEGPTTQQQ PMLPPAQPEH
PSSEEAPSRT IPTACVRPTH PLRSFANPLL PPPMSAIEPK VPYTPLLSQP GPTLPKTHVK
TASLGLAGKA RSPLLPVSVP TAPEVSEESH KPTEDPASVY EQDDLSEQMA SLEGLMKQLN
AITGSAF
