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Chondroitin sulfate proteoglycan 4 (Chondroitin sulfate proteoglycan NG2) (HSN tumor-specific antigen)

 CSPG4_RAT               Reviewed;        2326 AA.
Q00657;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
18-JUL-2018, entry version 146.
RecName: Full=Chondroitin sulfate proteoglycan 4;
AltName: Full=Chondroitin sulfate proteoglycan NG2;
AltName: Full=HSN tumor-specific antigen;
Flags: Precursor;
Name=Cspg4; Synonyms=Ng2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-47; 1011-1016 AND
1466-1477, SUBCELLULAR LOCATION, TOPOLOGY, AND GLYCOSYLATION.
TISSUE=Neuron;
PubMed=1906475; DOI=10.1083/jcb.114.2.359;
Nishiyama A., Dahlin K.J., Prince J.T., Johnstone S.R., Stallcup W.B.;
"The primary structure of NG2, a novel membrane-spanning
proteoglycan.";
J. Cell Biol. 114:359-371(1991).
[2]
SEQUENCE REVISION TO 2047-2096.
Nishiyama A., Dahlin K.J., Prince J.T., Johnstone S.R., Stallcup W.B.;
J. Cell Biol. 145:1115-1115(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 556-573 AND
657-667.
PubMed=8077056; DOI=10.1002/ijc.2910580514;
Leger O., Johnson-Leger C., Jackson E., Coles B., Dean C.;
"The chondroitin sulfate proteoglycan NG2 is a tumour-specific antigen
on the chemically induced rat chondrosarcoma HSN.";
Int. J. Cancer 58:700-705(1994).
[4]
INTERACTION WITH COL6A2, AND SUBCELLULAR LOCATION.
PubMed=2269670; DOI=10.1083/jcb.111.6.3177;
Stallcup W.B., Dahlin K., Healy P.;
"Interaction of the NG2 chondroitin sulfate proteoglycan with type VI
collagen.";
J. Cell Biol. 111:3177-3188(1990).
[5]
INTERACTION WITH COL6A2, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=8305732; DOI=10.1091/mbc.4.11.1097;
Nishiyama A., Stallcup W.B.;
"Expression of NG2 proteoglycan causes retention of type VI collagen
on the cell surface.";
Mol. Biol. Cell 4:1097-1108(1993).
[6]
SUBCELLULAR LOCATION.
PubMed=8590808; DOI=10.1091/mbc.6.12.1819;
Nishiyama A., Lin X.-H., Stallcup W.B.;
"Generation of truncated forms of the NG2 proteoglycan by cell surface
proteolysis.";
Mol. Biol. Cell 6:1819-1832(1995).
[7]
INTERACTION WITH COL5A1; COL6A2; TNC AND LAMININ-1.
PubMed=8824254; DOI=10.1074/jbc.271.42.26110;
Burg M.A., Tillet E., Timpl R., Stallcup W.B.;
"Binding of the NG2 proteoglycan to type VI collagen and other
extracellular matrix molecules.";
J. Biol. Chem. 271:26110-26116(1996).
[8]
INTERACTION WITH COL6A2, GLYCOSYLATION, DOMAIN, AND FUNCTION.
PubMed=9281375; DOI=10.1006/excr.1997.3674;
Burg M.A., Nishiyama A., Stallcup W.B.;
"A central segment of the NG2 proteoglycan is critical for the ability
of glioma cells to bind and migrate toward type VI collagen.";
Exp. Cell Res. 235:254-264(1997).
[9]
INTERACTION WITH COL5A1 AND COL6A2, AND DOMAIN.
PubMed=9099729; DOI=10.1074/jbc.272.16.10769;
Tillet E., Ruggiero F., Nishiyama A., Stallcup W.B.;
"The membrane-spanning proteoglycan NG2 binds to collagens V and VI
through the central nonglobular domain of its core protein.";
J. Biol. Chem. 272:10769-10776(1997).
[10]
INTERACTION WITH FGF2 AND PDGFA.
PubMed=10358027; DOI=10.1074/jbc.274.24.16831;
Goretzki L., Burg M.A., Grako K.A., Stallcup W.B.;
"High-affinity binding of basic fibroblast growth factor and platelet-
derived growth factor-AA to the core protein of the NG2
proteoglycan.";
J. Biol. Chem. 274:16831-16837(1999).
[11]
INTERACTION WITH PLG, AND FUNCTION.
PubMed=10889192; DOI=10.1074/jbc.M002290200;
Goretzki L., Lombardo C.R., Stallcup W.B.;
"Binding of the NG2 proteoglycan to kringle domains modulates the
functional properties of angiostatin and plasmin(ogen).";
J. Biol. Chem. 275:28625-28633(2000).
[12]
INTERACTION WITH MPDZ.
PubMed=10967549;
DOI=10.1002/1097-4644(20001101)79:2<213::AID-JCB50>3.0.CO;2-G;
Barritt D.S., Pearn M.T., Zisch A.H., Lee S.S., Javier R.T.,
Pasquale E.B., Stallcup W.B.;
"The multi-PDZ domain protein MUPP1 is a cytoplasmic ligand for the
membrane-spanning proteoglycan NG2.";
J. Cell. Biochem. 79:213-224(2000).
[13]
MUTAGENESIS OF SER-999 AND SER-1342, SUBCELLULAR LOCATION,
GLYCOSYLATION AT SER-999, AND FUNCTION.
PubMed=11493670;
Stallcup W.B., Dahlin-Huppe K.;
"Chondroitin sulfate and cytoplasmic domain-dependent membrane
targeting of the NG2 proteoglycan promotes retraction fiber formation
and cell polarization.";
J. Cell Sci. 114:2315-2325(2001).
[14]
IDENTIFICATION OF CSPG REPEATS.
PubMed=12220645; DOI=10.1016/S0014-5793(02)03195-2;
Staub E., Hinzmann B., Rosenthal A.;
"A novel repeat in the melanoma-associated chondroitin sulfate
proteoglycan defines a new protein family.";
FEBS Lett. 527:114-118(2002).
[15]
DOMAINS, AND FUNCTION.
PubMed=12514214;
Ughrin Y.M., Chen Z.J., Levine J.M.;
"Multiple regions of the NG2 proteoglycan inhibit neurite growth and
induce growth cone collapse.";
J. Neurosci. 23:175-186(2003).
[16]
PHOSPHORYLATION AT THR-2256, INTERACTION WITH PRKCA, SUBCELLULAR
LOCATION, MUTAGENESIS OF THR-2256; THR-2265 AND THR-2278, AND
FUNCTION.
PubMed=15504744; DOI=10.1074/jbc.M411045200;
Makagiansar I.T., Williams S., Dahlin-Huppe K., Fukushi J.,
Mustelin T., Stallcup W.B.;
"Phosphorylation of NG2 proteoglycan by protein kinase C-alpha
regulates polarized membrane distribution and cell motility.";
J. Biol. Chem. 279:55262-55270(2004).
[17]
INTERACTION WITH LGALS3; ITGB1 AND ITGA3, AND FUNCTION.
PubMed=15181153; DOI=10.1091/mbc.E04-03-0236;
Fukushi J., Makagiansar I.T., Stallcup W.B.;
"NG2 proteoglycan promotes endothelial cell motility and angiogenesis
via engagement of galectin-3 and alpha3beta1 integrin.";
Mol. Biol. Cell 15:3580-3590(2004).
-!- FUNCTION: Proteoglycan playing a role in cell proliferation and
migration which stimulates endothelial cells motility during
microvascular morphogenesis. May also inhibit neurite outgrowth
and growth cone collapse during axon regeneration. Cell surface
receptor for collagen alpha 2(VI) which may confer cells ability
to migrate on that substrate. Binds through its extracellular N-
terminus growth factors, extracellular matrix proteases modulating
their activity. May regulate MPP16-dependent degradation and
invasion of type I collagen participating in melanoma cells
invasion properties. May modulate the plasminogen system by
enhancing plasminogen activation and inhibiting angiostatin.
Functions also as a signal transducing protein by binding through
its cytoplasmic C-terminus scaffolding and signaling proteins. May
promote retraction fiber formation and cell polarization through
Rho GTPase activation. May stimulate alpha-4, beta-1 integrin-
mediated adhesion and spreading by recruiting and activating a
signaling cascade through CDC42, ACK1 and BCAR1. May activate FAK
and ERK1/ERK2 signaling cascades. {ECO:0000269|PubMed:10889192,
ECO:0000269|PubMed:11493670, ECO:0000269|PubMed:12514214,
ECO:0000269|PubMed:15181153, ECO:0000269|PubMed:15504744,
ECO:0000269|PubMed:8305732, ECO:0000269|PubMed:9281375}.
-!- SUBUNIT: Interacts with GRIP1, GRIP2 and GRIA2. Forms a ternary
complex with GRIP1 and GRIA2. Interacts with ITGA4 through its
chondroitin sulfate glycosaminoglycan. Interacts with BCAR1, CDC42
and ACK1. Interacts with MMP16 (By similarity). Interacts with the
first PDZ domain of MPDZ. Interacts with PRKCA. Interacts with
LGALS3 and the integrin composed of ITGB1 and ITGA3. Binds TNC,
laminin-1, COL5A1 and COL6A2. Interacts with PLG and angiostatin.
Binds FGF2 and PDGFA. {ECO:0000250, ECO:0000269|PubMed:10358027,
ECO:0000269|PubMed:10889192, ECO:0000269|PubMed:10967549,
ECO:0000269|PubMed:15181153, ECO:0000269|PubMed:15504744,
ECO:0000269|PubMed:2269670, ECO:0000269|PubMed:8305732,
ECO:0000269|PubMed:8824254, ECO:0000269|PubMed:9099729,
ECO:0000269|PubMed:9281375}.
-!- INTERACTION:
Q24008:inaD (xeno); NbExp=3; IntAct=EBI-4306655, EBI-195326;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15504744,
ECO:0000269|PubMed:1906475}; Single-pass type I membrane protein
{ECO:0000269|PubMed:1906475}; Extracellular side
{ECO:0000269|PubMed:1906475}. Apical cell membrane
{ECO:0000269|PubMed:15504744}; Single-pass type I membrane protein
{ECO:0000269|PubMed:1906475}; Extracellular side
{ECO:0000269|PubMed:1906475}. Cell projection, lamellipodium
membrane {ECO:0000269|PubMed:15504744}; Single-pass type I
membrane protein {ECO:0000269|PubMed:1906475}; Extracellular side
{ECO:0000269|PubMed:1906475}. Cell surface
{ECO:0000269|PubMed:2269670, ECO:0000269|PubMed:8305732,
ECO:0000269|PubMed:8590808}. Note=Localizes to the plasma membrane
of oligodendrocytes (By similarity). Localized at the apical
plasma membrane it relocalizes to the lamellipodia of astrocytoma
upon phosphorylation by PRKCA (PubMed:15504744). Localizes to the
retraction fibers (PubMed:11493670). A fraction may undergo cell
surface proteolysis and secretion. {ECO:0000250|UniProtKB:Q8VHY0,
ECO:0000269|PubMed:11493670, ECO:0000269|PubMed:15504744}.
-!- TISSUE SPECIFICITY: Neural cells and also extraneural tissues,
especially in the developing mesenchyme.
-!- DEVELOPMENTAL STAGE: The level of expression is highest on
immature, proliferating cells and decreases as these cells
differentiate.
-!- PTM: N-glycosylated.
-!- PTM: O-glycosylated; contains glycosaminoglycan chondroitin
sulfate which are required for proper localization and function in
stress fiber formation. Involved in interaction with MMP16 and
ITGA4.
-!- PTM: Phosphorylation by PRKCA regulates its subcellular location
and function in cell motility. {ECO:0000269|PubMed:15504744}.
-!- MISCELLANEOUS: Valuable marker for several incompletely
differentiated precursor cells.
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EMBL; X56541; CAA39884.2; -; mRNA.
PIR; S16025; A61208.
RefSeq; NP_112284.1; NM_031022.1.
UniGene; Rn.10381; -.
ProteinModelPortal; Q00657; -.
SMR; Q00657; -.
BioGrid; 249551; 1.
IntAct; Q00657; 1.
STRING; 10116.ENSRNOP00000023326; -.
iPTMnet; Q00657; -.
PhosphoSitePlus; Q00657; -.
PaxDb; Q00657; -.
PRIDE; Q00657; -.
GeneID; 81651; -.
KEGG; rno:81651; -.
UCSC; RGD:619942; rat.
CTD; 1464; -.
RGD; 619942; Cspg4.
eggNOG; KOG3597; Eukaryota.
eggNOG; ENOG410XQ29; LUCA.
HOGENOM; HOG000170195; -.
HOVERGEN; HBG081360; -.
InParanoid; Q00657; -.
KO; K08115; -.
PhylomeDB; Q00657; -.
PRO; PR:Q00657; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:RGD.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0005518; F:collagen binding; IPI:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IMP:RGD.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
GO; GO:0016322; P:neuron remodeling; IDA:RGD.
GO; GO:0010226; P:response to lithium ion; IEP:RGD.
GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR039005; CSPG_rpt.
InterPro; IPR001791; Laminin_G.
Pfam; PF00054; Laminin_G_1; 1.
Pfam; PF02210; Laminin_G_2; 1.
SMART; SM00282; LamG; 2.
SUPFAM; SSF49899; SSF49899; 2.
PROSITE; PS51854; CSPG; 15.
PROSITE; PS50025; LAM_G_DOMAIN; 2.
1: Evidence at protein level;
Angiogenesis; Cell membrane; Cell projection; Complete proteome;
Developmental protein; Differentiation; Direct protein sequencing;
Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Proteoglycan;
Reference proteome; Repeat; Signal; Tissue remodeling; Transducer;
Transmembrane; Transmembrane helix.
SIGNAL 1 29 {ECO:0000269|PubMed:1906475}.
CHAIN 30 2326 Chondroitin sulfate proteoglycan 4.
/FTId=PRO_0000026695.
TOPO_DOM 30 2225 Extracellular.
{ECO:0000269|PubMed:1906475}.
TRANSMEM 2226 2250 Helical. {ECO:0000255}.
TOPO_DOM 2251 2326 Cytoplasmic.
{ECO:0000269|PubMed:1906475}.
DOMAIN 30 193 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 203 381 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
REPEAT 429 524 CSPG 1. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 554 646 CSPG 2. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 663 765 CSPG 3. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 784 882 CSPG 4. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 902 993 CSPG 5. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1022 1114 CSPG 6. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1130 1220 CSPG 7. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1242 1341 CSPG 8. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1360 1453 CSPG 9. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1477 1567 CSPG 10. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1585 1683 CSPG 11. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1708 1807 CSPG 12. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1836 1928 CSPG 13. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1945 2033 CSPG 14. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 2042 2151 CSPG 15. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REGION 30 640 Globular or compact configuration
stabilized by disulfide bonds.
REGION 30 640 Neurite growth inhibition.
REGION 575 1044 Interaction with COL6A2.
REGION 632 1450 Interaction with COL5A1.
REGION 1590 2225 Neurite growth inhibition.
REGION 1591 2225 Cysteine-containing.
MOTIF 2324 2326 PDZ-binding.
COMPBIAS 640 1590 Gly/Ser-rich (glycosaminoglycan
attachment domain).
MOD_RES 2256 2256 Phosphothreonine; by PKC/PRKCA.
{ECO:0000269|PubMed:15504744}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 349 349 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 428 428 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 686 686 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 773 773 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 999 999 O-linked (Xyl...) (chondroitin sulfate)
serine. {ECO:0000269|PubMed:11493670}.
CARBOHYD 1135 1135 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1206 1206 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1368 1368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1453 1453 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1649 1649 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1913 1913 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2020 2020 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2038 2038 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2044 2044 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2079 2079 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 170 193 {ECO:0000255|PROSITE-ProRule:PRU00122}.
DISULFID 355 381 {ECO:0000255|PROSITE-ProRule:PRU00122}.
MUTAGEN 999 999 S->A: No chondroitin sulfate attachment.
Loss of localization to the retraction
fibers. {ECO:0000269|PubMed:11493670}.
MUTAGEN 1342 1342 S->A: No effect on chondroitin sulfate
attachment.
{ECO:0000269|PubMed:11493670}.
MUTAGEN 2256 2256 T->E: Localized to the lamellipodia.
Increases cell motility independently of
PRKCA activation.
{ECO:0000269|PubMed:15504744}.
MUTAGEN 2256 2256 T->V: Apically localized. Loss of PRKCA-
dependent cell motility.
{ECO:0000269|PubMed:15504744}.
MUTAGEN 2265 2265 T->E: Behaves as wild-type.
{ECO:0000269|PubMed:15504744}.
MUTAGEN 2265 2265 T->V: Behaves as wild-type.
{ECO:0000269|PubMed:15504744}.
MUTAGEN 2278 2278 T->E: Behaves as wild-type.
{ECO:0000269|PubMed:15504744}.
MUTAGEN 2278 2278 T->V: Behaves as wild-type.
{ECO:0000269|PubMed:15504744}.
CONFLICT 1391 1392 LG -> FP (in Ref. 3; AA sequence).
{ECO:0000305}.
SEQUENCE 2326 AA; 251909 MW; FA3E3BCEDB7E5EF5 CRC64;
MLLSPGHPLS APALALILTL ALLVRSTAPA SFFGENHLEV PVPSALTRVD LLLQFSTSQP
EALLLLAAGQ TDHLLLQLQS GHLQVRLALG QNELSLQTPA DTVLSDSTTH TVVLTVSNSW
AVLSVDGVLN TSAPIPKASH LKVPYGLFVG SSGSLDLPYL KGISRPLRGC LHSAILNGRN
LLRPLTPDVH EGCAEEFSAG DEVGLGFSGP HSLAAFPAWS TREEGTLEFT LTTRSQQAPL
AFQAGDKRGN FIYVDIFEGH LRAVVEKGQG TMLLRNSVPV ADGQPHEVSV HIDVHRLEIS
VDQYPTRTFN RGVLSYLEPR GSLLLGGLDT EASRHLQEHR LGLTPGAANI SLVGCIEDFS
VNGRRLGLRD AWLTRDMAAG CRPEEDEYEE EVYGPFEAFS TLAPEAWPVM DLPEPCVPEP
GLPAVFANFT QLLTISPLVV AEGGTAWLEW RHVQPTLDLT EAELRKSQVL FSVSQGARHG
ELELDIPGAQ TRKMFTLLDV VNRKARFVHD GSEDTSDQLM LEVSVTSRAP VPSCLRRGQI
YILPIQVNPV NDPPRIVFPH GSLMVILEHT QKPLGPEIFQ AYDPDSACEG LTIQLLGVSA
SVPVEHRDQP GEPVTEFSCR DLEAGNIVYV HRGGPAQDLT FRVSDGMQAS GPATLKVVAV
RPAIQILHNT GLRLAQGSAA AILPANLSVE TNAVGQDVSV LFRVTGTLQF GELQKQGAGG
VEGTEWWDTL AFHQRDVEQG RVRYLSTDPQ HHTQDTVEDL TLEVQVGQET LSNLSFPVTI
QRATVWMLQL EPLHTQNPHQ ETLTSAHLEA SLEEEGEGGP YPHIFHYELV QAPRRGNLLL
QGTRLSDGQS FSQSDLQAGR VTYRATTRTS EAAEDSFRFR VTSPPHFSPL YTFPIHIGGD
PNAPVLTNVL LMVPEGGEGV LSADHLFVKS LNSASYLYEV MEQPHHGSLA WRDPKGRATP
VTSFTNEDLL HGRLVYQHDD SETIEDDIPF VATRQGEGSG DMAWEEVRGV FRVAIQPVND
HAPVQTISRV FHVARGGQRL LTTDDVAFSD ADSGFSDAQL VLTRKDLLFG SIVAMEEPTR
PIYRFTQEDL RKKQVLFVHS GADHGWLQLQ VSDGQHQATA MLEVQASEPY LHVANSSSLV
VPQGGQGTID TAVLHLDTNL DIRSGNEVHY HVTAGPHWGQ LLRDGQSVTS FSQRDLLDGA
ILYSHNGSLS PQDTLALSVA AGPVHTSTVL QVTIALEGPL APLQLVQHKR IYVFQGEAAE
IRRDQLEVVQ EAVLPADIMF SLRSPPNAGY LVMVSHGASA DGPPSLDPVQ RFSQEAINSG
RVLYLHSRPG AWSDSFSLDV ASGLGDPLEG ISVELEVLPT VIPLDVQNFS VPEGGTRTLA
PPLIQITGPY LGTLPGLVLQ VLEPPQHGAL QKEDRPQDGT LSTFSWREVE EQLIRYVHDG
SETQTDGFIL LANASEMDRQ SQPMAFTITI LPVNDQPPVI TTNTGLQIWE GAIVPIPPEA
LRGIDSDSGP EDLVYTIEQP SNGRIALRVA PDAEAHRFTQ AQLDSGLVLF SHRGALEGGF
HFDLSDGVHT SPGHFFRVVA QKQVLLSLEG SRKLTVCPES VQPLSSQSLS ASSSTGSDPR
HLLYQVVRGP QLGRLLHAQQ GSAEEALVNF TQAEVNAGNI LYEHEISSEP FWEAHDTIGL
LLSSSPARDL AATLAVTVSF DAACPQRPSR LWRNKGLWVP EGQRAKITVA ALDAANLLAS
VPASQRGRHD VLFQITQFPT RGQLLVSEEP LHARRPHFLQ SELTAGQLVY AHGGGGTQQD
GFRFRAHLQG PTGASVAGPQ TSEAFVITVR DVNERPPQPQ ASIPLRITRG SRAPVSRAQL
SVVDPDSAPG EIEYEVQRAP HNGFLSLAGD NTGPVTHFTQ ADVDAGRLAF VANGSSVAGV
FQLSMSDGAS PPIPMSLAVD VLPSTIEVQL RAPLEVPQAL GRSSLSRQQL QVISDREEPD
VAYRLTQGPL YGQVLVGGQP ASAFSQLQVD QGDVVFAFTN FSSSQDHFKV LALARGVNAS
ATVNVTVQAL LHVWAGGPWP QGTTLRLDPT VLDASELANR TGSMPRFRLL EGPRYGRVVR
VSQGRAESRT NQLVEDFTQQ DLEEGRLGLE VGRPEGRSTG PTGDRLTLEL QATGVPPAVA
LLDFATEPYH AAKFYKVTLL SVPEAARTET EKTGKSTPTG QPGQAASSPM PTVAKSGFLG
FLEANMFSVI IPVCLVLLLL ALILPLLFYL RKRNKTGKHD VQVLTAKPRN GLAGDTETFR
KVEPGQAIPL TTVPGQGPPP GGQPDPELLQ FCRTPNPALR NGQYWV


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