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Chondroitin sulfate proteoglycan 4 (Chondroitin sulfate proteoglycan NG2) (Melanoma chondroitin sulfate proteoglycan) (Melanoma-associated chondroitin sulfate proteoglycan)

 CSPG4_HUMAN             Reviewed;        2322 AA.
Q6UVK1; D3DW77; Q92675;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
12-SEP-2018, entry version 136.
RecName: Full=Chondroitin sulfate proteoglycan 4;
AltName: Full=Chondroitin sulfate proteoglycan NG2;
AltName: Full=Melanoma chondroitin sulfate proteoglycan;
AltName: Full=Melanoma-associated chondroitin sulfate proteoglycan;
Flags: Precursor;
Name=CSPG4; Synonyms=MCSP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Melanoma;
PubMed=8790396; DOI=10.1073/pnas.93.18.9710;
Pluschke G., Vanek M., Evans A., Dittmar T., Schmid P., Itin P.,
Filardo E.J., Reisfeld R.A.;
"Molecular cloning of a human melanoma-associated chondroitin sulfate
proteoglycan.";
Proc. Natl. Acad. Sci. U.S.A. 93:9710-9715(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Melanoma;
PubMed=15210734; DOI=10.1083/jcb.200403174;
Yang J., Price M.A., Neudauer C.L., Wilson C., Ferrone S., Xia H.,
Iida J., Simpson M.A., McCarthy J.B.;
"Melanoma chondroitin sulfate proteoglycan enhances FAK and ERK
activation by distinct mechanisms.";
J. Cell Biol. 165:881-891(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
INTERACTION WITH ITGA4.
PubMed=9488735; DOI=10.1074/jbc.273.10.5955;
Iida J., Meijne A.M.L., Oegema T.R. Jr., Yednock T.A., Kovach N.L.,
Furcht L.T., McCarthy J.B.;
"A role of chondroitin sulfate glycosaminoglycan binding site in
alpha4beta1 integrin-mediated melanoma cell adhesion.";
J. Biol. Chem. 273:5955-5962(1998).
[6]
INTERACTION WITH BCAR1; CDC42 AND ACK1, AND FUNCTION.
PubMed=10587647; DOI=10.1038/70302;
Eisenmann K.M., McCarthy J.B., Simpson M.A., Keely P.J., Guan J.-L.,
Tachibana K., Lim L., Manser E., Furcht L.T., Iida J.;
"Melanoma chondroitin sulphate proteoglycan regulates cell spreading
through Cdc42, Ack-1 and p130cas.";
Nat. Cell Biol. 1:507-513(1999).
[7]
INTERACTION WITH MMP16, AND FUNCTION.
PubMed=11278606; DOI=10.1074/jbc.M010053200;
Iida J., Pei D., Kang T., Simpson M.A., Herlyn M., Furcht L.T.,
McCarthy J.B.;
"Melanoma chondroitin sulfate proteoglycan regulates matrix
metalloproteinase-dependent human melanoma invasion into type I
collagen.";
J. Biol. Chem. 276:18786-18794(2001).
[8]
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).
[9]
INTERACTION WITH ITGA3; ITGB1 AND LGALS3.
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).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2075.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
-!- 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:10587647,
ECO:0000269|PubMed:11278606, ECO:0000269|PubMed:15210734}.
-!- SUBUNIT: Interacts with the first PDZ domain of MPDZ. Interacts
with PRKCA. Binds TNC, laminin-1, COL5A1 and COL6A2. Interacts
with PLG and angiostatin. Binds FGF2 and PDGFA. Interacts with
GRIP1, GRIP2 and GRIA2. Forms a ternary complex with GRIP1 and
GRIA2 (By similarity). Interacts with LGALS3 and the integrin
composed of ITGB1 and ITGA3. Interacts with ITGA4 through its
chondroitin sulfate glycosaminoglycan. Interacts with BCAR1, CDC42
and ACK1. Interacts with MMP16. {ECO:0000250,
ECO:0000269|PubMed:10587647, ECO:0000269|PubMed:11278606,
ECO:0000269|PubMed:15181153, ECO:0000269|PubMed:9488735}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q00657}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q00657}; Extracellular side
{ECO:0000250|UniProtKB:Q00657}. Apical cell membrane
{ECO:0000250|UniProtKB:Q00657}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q00657}; Extracellular side
{ECO:0000250|UniProtKB:Q00657}. Cell projection, lamellipodium
membrane {ECO:0000250|UniProtKB:Q00657}; Single-pass type I
membrane protein {ECO:0000250|UniProtKB:Q00657}; Extracellular
side {ECO:0000250|UniProtKB:Q00657}. Cell surface
{ECO:0000250|UniProtKB:Q00657}. Note=Localized at the apical
plasma membrane it relocalizes to the lamellipodia of astrocytoma
upon phosphorylation by PRKCA. Localizes to the retraction fibers.
Localizes to the plasma membrane of oligodendrocytes (By
similarity). {ECO:0000250|UniProtKB:Q00657,
ECO:0000250|UniProtKB:Q8VHY0}.
-!- TISSUE SPECIFICITY: Detected only in malignant melanoma cells.
{ECO:0000269|PubMed:8790396}.
-!- PTM: O-glycosylated; contains glycosaminoglycan chondroitin
sulfate which are required for proper localization and function in
stress fiber formation (By similarity). Involved in interaction
with MMP16 and ITGA4. {ECO:0000250, ECO:0000269|PubMed:16335952}.
-!- PTM: Phosphorylation by PRKCA regulates its subcellular location
and function in cell motility. {ECO:0000250}.
-!- MISCELLANEOUS: Valuable marker for several incompletely
differentiated precursor cells.
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EMBL; X96753; CAA65529.1; -; mRNA.
EMBL; AY359468; AAQ62842.1; -; mRNA.
EMBL; AC105020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471136; EAW99239.1; -; Genomic_DNA.
EMBL; CH471136; EAW99240.1; -; Genomic_DNA.
CCDS; CCDS10284.1; -.
RefSeq; NP_001888.2; NM_001897.4.
UniGene; Hs.513044; -.
ProteinModelPortal; Q6UVK1; -.
SMR; Q6UVK1; -.
BioGrid; 107846; 13.
IntAct; Q6UVK1; 16.
MINT; Q6UVK1; -.
STRING; 9606.ENSP00000312506; -.
iPTMnet; Q6UVK1; -.
PhosphoSitePlus; Q6UVK1; -.
BioMuta; CSPG4; -.
DMDM; 296434468; -.
EPD; Q6UVK1; -.
MaxQB; Q6UVK1; -.
PaxDb; Q6UVK1; -.
PeptideAtlas; Q6UVK1; -.
PRIDE; Q6UVK1; -.
ProteomicsDB; 67431; -.
Ensembl; ENST00000308508; ENSP00000312506; ENSG00000173546.
GeneID; 1464; -.
KEGG; hsa:1464; -.
UCSC; uc002baw.3; human.
CTD; 1464; -.
DisGeNET; 1464; -.
EuPathDB; HostDB:ENSG00000173546.7; -.
GeneCards; CSPG4; -.
H-InvDB; HIX0026925; -.
H-InvDB; HIX0038117; -.
H-InvDB; HIX0172852; -.
H-InvDB; HIX0177623; -.
H-InvDB; HIX0177624; -.
HGNC; HGNC:2466; CSPG4.
HPA; CAB016189; -.
HPA; HPA002951; -.
HPA; HPA042785; -.
HPA; HPA050008; -.
MIM; 601172; gene.
neXtProt; NX_Q6UVK1; -.
OpenTargets; ENSG00000173546; -.
PharmGKB; PA26963; -.
eggNOG; KOG3597; Eukaryota.
eggNOG; ENOG410XQ29; LUCA.
GeneTree; ENSGT00550000074429; -.
HOGENOM; HOG000170195; -.
HOVERGEN; HBG081360; -.
InParanoid; Q6UVK1; -.
KO; K08115; -.
OMA; EPFWEAH; -.
OrthoDB; EOG091G00BN; -.
PhylomeDB; Q6UVK1; -.
TreeFam; TF316876; -.
Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
Reactome; R-HSA-2022923; Dermatan sulfate biosynthesis.
Reactome; R-HSA-2024101; CS/DS degradation.
Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
Reactome; R-HSA-3595172; Defective CHST3 causes SEDCJD.
Reactome; R-HSA-3595174; Defective CHST14 causes EDS, musculocontractural type.
Reactome; R-HSA-3595177; Defective CHSY1 causes TPBS.
Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
SignaLink; Q6UVK1; -.
ChiTaRS; CSPG4; human.
GeneWiki; CSPG4; -.
GenomeRNAi; 1464; -.
PRO; PR:Q6UVK1; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000173546; Expressed in 166 organ(s), highest expression level in tendon.
CleanEx; HS_CSPG4; -.
Genevisible; Q6UVK1; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; HDA:UniProtKB.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; IEA:Ensembl.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0030206; P:chondroitin sulfate biosynthetic process; TAS:Reactome.
GO; GO:0030207; P:chondroitin sulfate catabolic process; TAS:Reactome.
GO; GO:0030208; P:dermatan sulfate biosynthetic process; TAS:Reactome.
GO; GO:0008347; P:glial cell migration; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:Ensembl.
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; Disulfide bond; Glycoprotein;
Membrane; Phosphoprotein; Polymorphism; Proteoglycan;
Reference proteome; Repeat; Signal; Tissue remodeling; Transducer;
Transmembrane; Transmembrane helix.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 2322 Chondroitin sulfate proteoglycan 4.
/FTId=PRO_0000041962.
TOPO_DOM 30 2224 Extracellular.
{ECO:0000250|UniProtKB:Q00657}.
TRANSMEM 2225 2245 Helical. {ECO:0000255}.
TOPO_DOM 2246 2322 Cytoplasmic.
{ECO:0000250|UniProtKB:Q00657}.
DOMAIN 30 192 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 202 380 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
REPEAT 428 523 CSPG 1. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 553 645 CSPG 2. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 662 764 CSPG 3. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 783 878 CSPG 4. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 898 989 CSPG 5. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1018 1110 CSPG 6. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1126 1216 CSPG 7. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1238 1337 CSPG 8. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1356 1449 CSPG 9. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1473 1563 CSPG 10. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1581 1679 CSPG 11. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1704 1803 CSPG 12. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1832 1924 CSPG 13. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 1941 2029 CSPG 14. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REPEAT 2038 2147 CSPG 15. {ECO:0000255|PROSITE-
ProRule:PRU01201,
ECO:0000269|PubMed:12220645}.
REGION 30 639 Globular or compact configuration
stabilized by disulfide bonds.
REGION 30 639 Neurite growth inhibition. {ECO:0000250}.
REGION 574 1040 Interaction with COL6A2. {ECO:0000250}.
REGION 631 1446 Interaction with COL5A1. {ECO:0000250}.
REGION 1586 2221 Neurite growth inhibition. {ECO:0000250}.
REGION 1587 2221 Cysteine-containing.
MOTIF 2320 2322 PDZ-binding.
COMPBIAS 639 1586 Gly/Ser-rich (glycosaminoglycan
attachment domain).
MOD_RES 2252 2252 Phosphothreonine; by PKC/PRKCA.
{ECO:0000250|UniProtKB:Q00657}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 348 348 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 427 427 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 685 685 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 772 772 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 995 995 O-linked (Xyl...) (chondroitin sulfate)
serine. {ECO:0000250}.
CARBOHYD 1131 1131 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1202 1202 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1364 1364 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1449 1449 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1645 1645 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1909 1909 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2016 2016 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2034 2034 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2040 2040 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2075 2075 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
DISULFID 169 192 {ECO:0000255|PROSITE-ProRule:PRU00122}.
DISULFID 354 380 {ECO:0000255|PROSITE-ProRule:PRU00122}.
VARIANT 1703 1703 R -> H (in dbSNP:rs8023621).
/FTId=VAR_061733.
CONFLICT 5 6 PR -> RG (in Ref. 1; CAA65529 and 2;
AAQ62842). {ECO:0000305}.
CONFLICT 477 478 RH -> HY (in Ref. 1; CAA65529).
{ECO:0000305}.
CONFLICT 486 486 P -> L (in Ref. 1; CAA65529).
{ECO:0000305}.
CONFLICT 631 631 R -> C (in Ref. 1; CAA65529).
{ECO:0000305}.
CONFLICT 715 717 QGA -> HST (in Ref. 1; CAA65529).
{ECO:0000305}.
CONFLICT 942 942 H -> L (in Ref. 1; CAA65529).
{ECO:0000305}.
CONFLICT 1208 1208 R -> E (in Ref. 1; CAA65529).
{ECO:0000305}.
CONFLICT 1405 1405 A -> P (in Ref. 1; CAA65529).
{ECO:0000305}.
CONFLICT 1557 1557 R -> P (in Ref. 1; CAA65529).
{ECO:0000305}.
SEQUENCE 2322 AA; 250537 MW; 0B4F39AFC5ADD3CA CRC64;
MQSGPRPPLP APGLALALTL TMLARLASAA SFFGENHLEV PVATALTDID LQLQFSTSQP
EALLLLAAGP ADHLLLQLYS GRLQVRLVLG QEELRLQTPA ETLLSDSIPH TVVLTVVEGW
ATLSVDGFLN ASSAVPGAPL EVPYGLFVGG TGTLGLPYLR GTSRPLRGCL HAATLNGRSL
LRPLTPDVHE GCAEEFSASD DVALGFSGPH SLAAFPAWGT QDEGTLEFTL TTQSRQAPLA
FQAGGRRGDF IYVDIFEGHL RAVVEKGQGT VLLHNSVPVA DGQPHEVSVH INAHRLEISV
DQYPTHTSNR GVLSYLEPRG SLLLGGLDAE ASRHLQEHRL GLTPEATNAS LLGCMEDLSV
NGQRRGLREA LLTRNMAAGC RLEEEEYEDD AYGHYEAFST LAPEAWPAME LPEPCVPEPG
LPPVFANFTQ LLTISPLVVA EGGTAWLEWR HVQPTLDLME AELRKSQVLF SVTRGARHGE
LELDIPGAQA RKMFTLLDVV NRKARFIHDG SEDTSDQLVL EVSVTARVPM PSCLRRGQTY
LLPIQVNPVN DPPHIIFPHG SLMVILEHTQ KPLGPEVFQA YDPDSACEGL TFQVLGTSSG
LPVERRDQPG EPATEFSCRE LEAGSLVYVH RGGPAQDLTF RVSDGLQASP PATLKVVAIR
PAIQIHRSTG LRLAQGSAMP ILPANLSVET NAVGQDVSVL FRVTGALQFG ELQKQGAGGV
EGAEWWATQA FHQRDVEQGR VRYLSTDPQH HAYDTVENLA LEVQVGQEIL SNLSFPVTIQ
RATVWMLRLE PLHTQNTQQE TLTTAHLEAT LEEAGPSPPT FHYEVVQAPR KGNLQLQGTR
LSDGQGFTQD DIQAGRVTYG ATARASEAVE DTFRFRVTAP PYFSPLYTFP IHIGGDPDAP
VLTNVLLVVP EGGEGVLSAD HLFVKSLNSA SYLYEVMERP RHGRLAWRGT QDKTTMVTSF
TNEDLLRGRL VYQHDDSETT EDDIPFVATR QGESSGDMAW EEVRGVFRVA IQPVNDHAPV
QTISRIFHVA RGGRRLLTTD DVAFSDADSG FADAQLVLTR KDLLFGSIVA VDEPTRPIYR
FTQEDLRKRR VLFVHSGADR GWIQLQVSDG QHQATALLEV QASEPYLRVA NGSSLVVPQG
GQGTIDTAVL HLDTNLDIRS GDEVHYHVTA GPRWGQLVRA GQPATAFSQQ DLLDGAVLYS
HNGSLSPRDT MAFSVEAGPV HTDATLQVTI ALEGPLAPLK LVRHKKIYVF QGEAAEIRRD
QLEAAQEAVP PADIVFSVKS PPSAGYLVMV SRGALADEPP SLDPVQSFSQ EAVDTGRVLY
LHSRPEAWSD AFSLDVASGL GAPLEGVLVE LEVLPAAIPL EAQNFSVPEG GSLTLAPPLL
RVSGPYFPTL LGLSLQVLEP PQHGALQKED GPQARTLSAF SWRMVEEQLI RYVHDGSETL
TDSFVLMANA SEMDRQSHPV AFTVTVLPVN DQPPILTTNT GLQMWEGATA PIPAEALRST
DGDSGSEDLV YTIEQPSNGR VVLRGAPGTE VRSFTQAQLD GGLVLFSHRG TLDGGFRFRL
SDGEHTSPGH FFRVTAQKQV LLSLKGSQTL TVCPGSVQPL SSQTLRASSS AGTDPQLLLY
RVVRGPQLGR LFHAQQDSTG EALVNFTQAE VYAGNILYEH EMPPEPFWEA HDTLELQLSS
PPARDVAATL AVAVSFEAAC PQRPSHLWKN KGLWVPEGQR ARITVAALDA SNLLASVPSP
QRSEHDVLFQ VTQFPSRGQL LVSEEPLHAG QPHFLQSQLA AGQLVYAHGG GGTQQDGFHF
RAHLQGPAGA SVAGPQTSEA FAITVRDVNE RPPQPQASVP LRLTRGSRAP ISRAQLSVVD
PDSAPGEIEY EVQRAPHNGF LSLVGGGLGP VTRFTQADVD SGRLAFVANG SSVAGIFQLS
MSDGASPPLP MSLAVDILPS AIEVQLRAPL EVPQALGRSS LSQQQLRVVS DREEPEAAYR
LIQGPQYGHL LVGGRPTSAF SQFQIDQGEV VFAFTNFSSS HDHFRVLALA RGVNASAVVN
VTVRALLHVW AGGPWPQGAT LRLDPTVLDA GELANRTGSV PRFRLLEGPR HGRVVRVPRA
RTEPGGSQLV EQFTQQDLED GRLGLEVGRP EGRAPGPAGD SLTLELWAQG VPPAVASLDF
ATEPYNAARP YSVALLSVPE AARTEAGKPE SSTPTGEPGP MASSPEPAVA KGGFLSFLEA
NMFSVIIPMC LVLLLLALIL PLLFYLRKRN KTGKHDVQVL TAKPRNGLAG DTETFRKVEP
GQAIPLTAVP GQGPPPGGQP DPELLQFCRT PNPALKNGQY WV


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