PGCA_RAT
ID PGCA_RAT Reviewed; 2124 AA.
AC P07897;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Aggrecan core protein;
DE AltName: Full=Cartilage-specific proteoglycan core protein;
DE Short=CSPCP;
DE Flags: Precursor;
GN Name=Acan; Synonyms=Agc, Agc1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=3693370; DOI=10.1016/s0021-9258(18)45444-0;
RA Doege K., Sasaki M., Horigan E., Hassell J.R., Yamada Y.;
RT "Complete primary structure of the rat cartilage proteoglycan core protein
RT deduced from cDNA clones.";
RL J. Biol. Chem. 262:17757-17767(1987).
RN [2]
RP ERRATUM OF PUBMED:3693370, AND SEQUENCE REVISION TO 698.
RA Doege K., Sasaki M., Horigan E., Hassell J.R., Yamada Y.;
RL J. Biol. Chem. 263:10040-10040(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1856-2124 (ISOFORM 1).
RX PubMed=2424893; DOI=10.1016/s0021-9258(19)83883-8;
RA Doege K., Fernandez P., Hassell J.R., Sasaki M., Yamada Y.;
RT "Partial cDNA sequence encoding a globular domain at the C-terminus of the
RT rat cartilage proteoglycan.";
RL J. Biol. Chem. 261:8108-8111(1986).
RN [4]
RP PROTEIN SEQUENCE OF 20-83 AND 88-386, AND GLYCOSYLATION AT ASN-126 AND
RP ASN-333.
RX PubMed=3693371; DOI=10.1016/s0021-9258(18)45445-2;
RA Neame P.J., Christner J.E., Baker J.R.;
RT "Cartilage proteoglycan aggregates. The link protein and proteoglycan
RT amino-terminal globular domains have similar structures.";
RL J. Biol. Chem. 262:17768-17778(1987).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1909-2037 IN COMPLEX WITH TNR,
RP DISULFIDE BOND, AND CALCIUM-BINDING SITES.
RX PubMed=15296743; DOI=10.1016/j.str.2004.05.021;
RA Lundell A., Olin A.I., Morgelin M., al-Karadaghi S., Aspberg A.,
RA Logan D.T.;
RT "Structural basis for interactions between tenascins and lectican C-type
RT lectin domains: evidence for a crosslinking role for tenascins.";
RL Structure 12:1495-1506(2004).
CC -!- FUNCTION: This proteoglycan is a major component of extracellular
CC matrix of cartilagenous tissues. A major function of this protein is to
CC resist compression in cartilage. It binds avidly to hyaluronic acid via
CC an N-terminal globular region. May play a regulatory role in the matrix
CC assembly of the cartilage.
CC -!- SUBUNIT: Interacts with FBLN1 and COMP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P07897-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P07897-2; Sequence=VSP_039196;
CC -!- DOMAIN: Two globular domains, G1 and G2, comprise the N-terminus of the
CC proteoglycan, while another globular region, G3, makes up the C-
CC terminus. G1 contains Link domains and thus consists of three
CC disulfide-bonded loop structures designated as the A, B, B' motifs. G2
CC is similar to G1. The keratan sulfate (KS) and the chondroitin sulfate
CC (CS) attachment domains lie between G2 and G3.
CC -!- PTM: Contains mostly chondroitin sulfate, but also keratan sulfate
CC chains, N-linked and O-linked oligosaccharides.
CC {ECO:0000269|PubMed:3693371}.
CC -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan 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; J03485; AAA21000.1; -; mRNA.
DR EMBL; M13518; AAA41836.1; -; mRNA.
DR PIR; A92623; A28452.
DR RefSeq; NP_071526.1; NM_022190.1.
DR PDB; 1TDQ; X-ray; 2.60 A; B=1909-2037.
DR PDBsum; 1TDQ; -.
DR AlphaFoldDB; P07897; -.
DR SMR; P07897; -.
DR BioGRID; 248701; 1.
DR IntAct; P07897; 2.
DR MINT; P07897; -.
DR STRING; 10116.ENSRNOP00000042691; -.
DR GlyGen; P07897; 9 sites.
DR iPTMnet; P07897; -.
DR PaxDb; P07897; -.
DR PRIDE; P07897; -.
DR GeneID; 58968; -.
DR UCSC; RGD:68358; rat. [P07897-1]
DR CTD; 176; -.
DR RGD; 68358; Acan.
DR eggNOG; ENOG502QUX8; Eukaryota.
DR InParanoid; P07897; -.
DR OrthoDB; 156064at2759; -.
DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR Reactome; R-RNO-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-RNO-2022857; Keratan sulfate degradation.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR EvolutionaryTrace; P07897; -.
DR PRO; PR:P07897; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0072534; C:perineuronal net; IDA:RGD.
DR GO; GO:0098966; C:perisynaptic extracellular matrix; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0001502; P:cartilage condensation; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0007417; P:central nervous system development; IEP:RGD.
DR GO; GO:0060591; P:chondroblast differentiation; IEP:RGD.
DR GO; GO:0002063; P:chondrocyte development; ISO:RGD.
DR GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0010259; P:multicellular organism aging; IEP:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:RGD.
DR GO; GO:0001503; P:ossification; IEP:RGD.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; ISO:RGD.
DR GO; GO:0010447; P:response to acidic pH; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0009629; P:response to gravity; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0009314; P:response to radiation; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR GO; GO:0021510; P:spinal cord development; IEP:RGD.
DR CDD; cd00033; CCP; 1.
DR CDD; cd03588; CLECT_CSPGs; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.100.10; -; 5.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033987; CSPG_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR000538; Link_dom.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 1.
DR Pfam; PF07686; V-set; 1.
DR Pfam; PF00193; Xlink; 4.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SMART; SM00445; LINK; 4.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF56436; SSF56436; 5.
DR SUPFAM; SSF57535; SSF57535; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
DR PROSITE; PS01241; LINK_1; 4.
DR PROSITE; PS50963; LINK_2; 4.
DR PROSITE; PS50923; SUSHI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Immunoglobulin domain;
KW Lectin; Metal-binding; Proteoglycan; Reference proteome; Repeat; Secreted;
KW Signal; Sushi.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:3693371"
FT CHAIN 20..2124
FT /note="Aggrecan core protein"
FT /id="PRO_0000017508"
FT DOMAIN 34..147
FT /note="Ig-like V-type"
FT DOMAIN 153..248
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 254..350
FT /note="Link 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 487..582
FT /note="Link 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 588..684
FT /note="Link 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 1910..2036
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 2039..2099
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 48..140
FT /note="G1-A"
FT REGION 152..247
FT /note="G1-B"
FT REGION 253..349
FT /note="G1-B'"
FT REGION 434..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..580
FT /note="G2-B"
FT REGION 587..682
FT /note="G2-B'"
FT REGION 685..798
FT /note="KS"
FT REGION 731..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..1226
FT /note="CS-1"
FT REGION 1100..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1225..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1909
FT /note="CS-2"
FT REGION 1295..1455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1723..1913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1910..2124
FT /note="G3"
FT COMPBIAS 768..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1602..1661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1766..1789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1797..1913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1975
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 1979
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 1979
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 1999
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 2001
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 2002
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 2008
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 2008
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 2009
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 2009
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 2022
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 2023
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3693371"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3693371"
FT CARBOHYD 371
FT /note="O-linked (Xyl...) (keratan sulfate) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 376
FT /note="O-linked (Xyl...) (keratan sulfate) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1842
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..133
FT /evidence="ECO:0000250"
FT DISULFID 175..246
FT /evidence="ECO:0000250"
FT DISULFID 199..220
FT /evidence="ECO:0000250"
FT DISULFID 273..348
FT /evidence="ECO:0000250"
FT DISULFID 297..318
FT /evidence="ECO:0000250"
FT DISULFID 509..580
FT /evidence="ECO:0000250"
FT DISULFID 533..554
FT /evidence="ECO:0000250"
FT DISULFID 607..682
FT /evidence="ECO:0000250"
FT DISULFID 631..652
FT /evidence="ECO:0000250"
FT DISULFID 1914..1925
FT /evidence="ECO:0000250"
FT DISULFID 1942..2034
FT /evidence="ECO:0000269|PubMed:15296743"
FT DISULFID 2010..2026
FT /evidence="ECO:0000269|PubMed:15296743"
FT DISULFID 2041..2084
FT /evidence="ECO:0000250"
FT DISULFID 2070..2097
FT /evidence="ECO:0000250"
FT VAR_SEQ 1909
FT /note="A -> ADIDECLSSPCLNGATCVDALDTFTCLCLPSYRGDLCEI (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:3693370"
FT /id="VSP_039196"
FT CONFLICT 38
FT /note="P -> W (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="T -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="I -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="N -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="T -> A (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 275..276
FT /note="TV -> RL (in Ref. 1; AAA21000)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="T -> H (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="W -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="L -> V (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 1919..1921
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 1924..1933
FT /evidence="ECO:0007829|PDB:1TDQ"
FT HELIX 1935..1944
FT /evidence="ECO:0007829|PDB:1TDQ"
FT HELIX 1955..1965
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 1969..1974
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 1976..1978
FT /evidence="ECO:0007829|PDB:1TDQ"
FT TURN 2005..2007
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 2008..2013
FT /evidence="ECO:0007829|PDB:1TDQ"
FT TURN 2015..2019
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 2021..2025
FT /evidence="ECO:0007829|PDB:1TDQ"
FT STRAND 2030..2036
FT /evidence="ECO:0007829|PDB:1TDQ"
SQ SEQUENCE 2124 AA; 221118 MW; E30BBE61593A34B1 CRC64;
MTTLLLVFVT LRVIAAVISE EVPDHDNSLS VSIPQPSPLK ALLGTSLTIP CYFIDPMHPV
TTAPSTAPLT PRIKWSRVSK EKEVVLLVAT EGQVRVNSIY QDKVSLPNYP AIPSDATLEI
QNLRSNDSGI YRCEVMHGIE DSEATLEVIV KGIVFHYRAI STRYTLDFDR AQRACLQNSA
IIATPEQLQA AYEDGFHQCD AGWLADQTVR YPIHTPREGC YGDKDEFPGV RTYGIRDTNE
TYDVYCFAEE MEGEVFYATS PEKFTFQEAA NECRTVGARL ATTGQLYLAW QGGMDMCSAG
WLADRSVRYP ISKARPNCGG NLLGVRTVYL HANQTGYPDP SSRYDAICYT GEDFVDIPEN
FFGVGGEEDI TIQTVTWPDL ELPLPRNITE GEARGNVILT AKPIFDMSPT VSEPGEALTL
APEVGTTVFP EAGERTEKTT RPWGFPEEAT RGPDSATAFA SEDLVVRVTI SPGAVEVPGQ
PRLPGGVVFH YRPGSTRYSL TFEEAQQACI RTGAAIASPE QLQAAYEAGY EQCDAGWLQD
QTVRYPIVSP RTPCVGDKDS SPGVRTYGVR PSSETYDVYC YVDKLEGEVF FATQMEQFTF
QEAQAFCAAQ NATLASTGQL YAAWSQGLDK CYAGWLADGT LRYPIVNPRP ACGGDKPGVR
TVYLYPNQTG LPDPLSKHHA FCFRGVSVVP SPGGTPTSPS DIEDWIVTRV EPGVDAVPLE
PETTEVPYFT TEPEKQTEWE PAYTPVGTSP LPGIPPTWLP TVPAAEEHTE SPSASQEPSA
SQVPSTSEEP YTPSLAVPSG TELPSSGDTS GAPDLSGDFT GSTDTSGRLD SSGEPSGGSE
SGLPSGDLDS SGLGPTVSSG LPVESGSASG DGEIPWSSTP TVDRLPSGGE SLEGSASASG
TGDLSGLPSG GEITETSASG TEEISGLPSG GDDLETSTSG IDGASVLPTG RGGLETSASG
VEDLSGLPSG EEGSETSTSG IEDISVLPTG ESPETSASGV GDLSGLPSGG ESLETSASGV
EDVTQLPTER GGLETSASGI EDITVLPTGR ENLETSASGV EDVSGLPSGK EGLETSASGI
EDISVFPTEA EGLETSASGG YVSGIPSGED GTETSTSGVE GVSGLPSGGE GLETSASGVE
DLGLPTRDSL ETSASGVDVT GYPSGREDTE TSVPGVGDDL SGLPSGQEGL ETSASGAEDL
GGLPSGKEDL VGSASGALDF GKLPSGTLGS GQTPEASGLP SGFSGEYSGV DIGSGPSSGL
PDFSGLPSGF PTVSLVDSTL VEVITATTAS ELEGRGTISV SGSGEESGPP LSELDSSADI
SGLPSGTELS GQTSGSLDVS GETSGFFDVS GQPFGSSGTG EGTSGIPEVS GQAVRSPDTT
EISELSGLSS GQPDVSGEGS GILFGSGQSS GITSVSGETS GISDLSGQPS GFPVLSGTTP
GTPDLASGAM SGSGDSSGIT FVDTSLIEVT PTTFREEEGL GSVELSGLPS GETDLSGTSG
MVDVSGQSSG AIDSSGLISP TPEFSGLPSG VAEVSGEVSG VETGSSLSSG AFDGSGLVSG
FPTVSLVDRT LVESITLAPT AQEAGEGPSS ILEFSGAHSG TPDISGDLSG SLDQSTWQPG
WTEASTEPPS SPYFSGDFSS TTDASGESIT APTGSGETSG LPEVTLITSE LVEGVTEPTV
SQELGHGPSM TYTPRLFEAS GEASASGDLG GPVTIFPGSG VEASVPEGSS DPSAYPEAGV
GVSAAPEASS QLSEFPDLHG ITSASRETDL EMTTPGTEVS SNPWTFQEGT REGSAAPEVS
GESSTTSDID AGTSGVPFAT PMTSGDRTEI SGEWSDHTSE VNVTVSTTVP ESRWAQSTQH
PTETLQEIGS PNPSYSGEET QTAETAKSLT DTPTLASPEG SGETESTAAD QEQCEEGWTK
FQGHCYRHFP DRETWVDAER RCREQQSHLS SIVTPEEQEF VNKNAQDYQW IGLNDRTIEG
DFRWSDGHSL QFEKWRPNQP DNFFATGEDC VVMIWHERGE WNDVPCNYQL PFTCKKGTVA
CGEPPAVEHA RTLGQKKDRY EISSLVRYQC TEGFVQRHVP TIRCQPSADW EEPRITCTDP
NTYKHRLQKR TMRPTRRSRP SMAH
