ID PGCA_BOVIN Reviewed; 2364 AA.
AC P13608; P79117; Q28159; Q6XL66;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 27-MAR-2024, entry version 184.
DE RecName: Full=Aggrecan core protein;
DE AltName: Full=Cartilage-specific proteoglycan core protein;
DE Short=CSPCP;
DE Flags: Precursor;
GN Name=ACAN; Synonyms=AGC1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=9308898; DOI=10.1006/abbi.1997.0261;
RA Hering T.M., Kollar J., Huynh T.D.;
RT "Complete coding sequence of bovine aggrecan: comparative structural
RT analysis.";
RL Arch. Biochem. Biophys. 345:259-270(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16167996; DOI=10.1111/j.1365-2052.2005.01340.x;
RA Cavanagh J.A.L., Tammen I., Hayden M.J., Gill C.A., Nicholas F.W.,
RA Raadsma H.W.;
RT "Characterization of the bovine aggrecan gene: genomic structure and
RT physical and linkage mapping.";
RL Anim. Genet. 36:452-454(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 563-1056.
RX PubMed=2528543; DOI=10.1016/s0021-9258(18)71603-7;
RA Antonsson P., Heinegaard D., Oldberg A.;
RT "The keratan sulfate-enriched region of bovine cartilage proteoglycan
RT consists of a consecutively repeated hexapeptide motif.";
RL J. Biol. Chem. 264:16170-16173(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1609-2113 AND 2151-2364.
RX PubMed=3111460; DOI=10.1042/bj2430255;
RA Oldberg A., Antonsson P., Heinegaard D.;
RT "The partial amino acid sequence of bovine cartilage proteoglycan, deduced
RT from a cDNA clone, contains numerous Ser-Gly sequences arranged in
RT homologous repeats.";
RL Biochem. J. 243:255-259(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2114-2150 (ISOFORM 1).
RC TISSUE=Cartilage;
RX PubMed=8349621; DOI=10.1016/s0021-9258(19)85345-0;
RA Fueloep C., Walcz E., Valyon M., Glant T.T.;
RT "Expression of alternatively spliced epidermal growth factor-like domains
RT in aggrecans of different species. Evidence for a novel module.";
RL J. Biol. Chem. 268:17377-17383(1993).
RN [6]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=6489519; DOI=10.1016/0014-5793(84)80907-2;
RA Perin J.-P., Bonnet F., Jolles J., Jolles P.;
RT "Sequence data concerning the protein core of the cartilage proteoglycan
RT monomers. Characterization of a sequence allowing the synthesis of an
RT oligonucleotide probe.";
RL FEBS Lett. 176:37-42(1984).
RN [7]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=3530809; DOI=10.1016/0014-5793(86)81343-6;
RA Perin J.-P., Bonnet F., Jolles P.;
RT "Structural relationship between link proteins and proteoglycan monomers.";
RL FEBS Lett. 206:73-77(1986).
RN [8]
RP PROTEIN SEQUENCE OF 152-157; 210-230; 482-506; 566-584; 631-641; 660-684;
RP 2161-2167; 2276-2291; 2298-2307 AND 2318-2334.
RX PubMed=2022637; DOI=10.1016/s0021-9258(18)92961-3;
RA Sandy J.D., Boynton R.E., Flannery C.R.;
RT "Analysis of the catabolism of aggrecan in cartilage explants by
RT quantitation of peptides from the three globular domains.";
RL J. Biol. Chem. 266:8198-8205(1991).
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 -!- INTERACTION:
CC P13608; Q9UNA0: ADAMTS5; Xeno; NbExp=2; IntAct=EBI-6259246, EBI-2808663;
CC P13608; P49747: COMP; Xeno; NbExp=2; IntAct=EBI-6259246, EBI-2531022;
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=P13608-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P13608-2; Sequence=VSP_003072;
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 N-linked and O-
CC linked (about 40) oligosaccharides.
CC -!- PTM: The keratan sulfate contents differ considerably between adult and
CC fetal bovine proteoglycans.
CC -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC {ECO:0000305}.
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DR EMBL; U76615; AAB38524.1; -; mRNA.
DR EMBL; AY226875; AAP44492.1; -; Genomic_DNA.
DR EMBL; AY226858; AAP44492.1; JOINED; Genomic_DNA.
DR EMBL; AY226859; AAP44492.1; JOINED; Genomic_DNA.
DR EMBL; AY226860; AAP44492.1; JOINED; Genomic_DNA.
DR EMBL; AY226861; AAP44492.1; JOINED; Genomic_DNA.
DR EMBL; AY226862; AAP44492.1; JOINED; Genomic_DNA.
DR EMBL; AY226863; AAP44492.1; JOINED; Genomic_DNA.
DR EMBL; AY226864; AAP44492.1; JOINED; Genomic_DNA.
DR EMBL; AY226865; AAP44492.1; JOINED; Genomic_DNA.
DR EMBL; AY226866; AAP44492.1; JOINED; Genomic_DNA.
DR EMBL; AY226867; AAP44492.1; JOINED; Genomic_DNA.
DR EMBL; AY226868; AAP44492.1; JOINED; Genomic_DNA.
DR EMBL; AY226871; AAP44492.1; JOINED; Genomic_DNA.
DR EMBL; AY226872; AAP44492.1; JOINED; Genomic_DNA.
DR EMBL; AY226873; AAP44492.1; JOINED; Genomic_DNA.
DR EMBL; AY226874; AAP44492.1; JOINED; Genomic_DNA.
DR EMBL; L07053; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A29164; A29164.
DR PIR; A34234; A39808.
DR PIR; B29164; B29164.
DR PIR; S74144; S74144.
DR PIR; T42630; T42630.
DR RefSeq; NP_776406.1; NM_173981.2. [P13608-2]
DR AlphaFoldDB; P13608; -.
DR SMR; P13608; -.
DR IntAct; P13608; 3.
DR STRING; 9913.ENSBTAP00000021512; -.
DR BindingDB; P13608; -.
DR ChEMBL; CHEMBL4295716; -.
DR GlyCosmos; P13608; 8 sites, No reported glycans.
DR PaxDb; 9913-ENSBTAP00000021512; -.
DR PeptideAtlas; P13608; -.
DR GeneID; 280985; -.
DR KEGG; bta:280985; -.
DR CTD; 176; -.
DR eggNOG; ENOG502QUX8; Eukaryota.
DR InParanoid; P13608; -.
DR OrthoDB; 5402504at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0072534; C:perineuronal net; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0010001; P:glial cell differentiation; IBA:GO_Central.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR CDD; cd00033; CCP; 1.
DR CDD; cd03588; CLECT_CSPGs; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd05900; Ig_Aggrecan; 1.
DR CDD; cd03517; Link_domain_CSPGs_modules_1_3; 2.
DR CDD; cd03520; Link_domain_CSPGs_modules_2_4; 2.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
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 PANTHER; PTHR22804:SF42; AGGRECAN CORE PROTEIN; 1.
DR PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1.
DR Pfam; PF00008; EGF; 1.
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; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SMART; SM00445; LINK; 4.
DR SUPFAM; SSF56436; C-type lectin-like; 5.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50835; IG_LIKE; 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 Alternative splicing; Calcium; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Extracellular matrix; Glycoprotein; Immunoglobulin domain;
KW Lectin; Metal-binding; Proteoglycan; Reference proteome; Repeat; Secreted;
KW Signal; Sushi.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..2364
FT /note="Aggrecan core protein"
FT /id="PRO_0000017502"
FT DOMAIN 25..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 REPEAT 774..779
FT /note="1"
FT REPEAT 780..785
FT /note="2"
FT REPEAT 786..791
FT /note="3"
FT REPEAT 792..797
FT /note="4"
FT REPEAT 798..803
FT /note="5"
FT REPEAT 804..809
FT /note="6"
FT REPEAT 810..815
FT /note="7"
FT REPEAT 816..821
FT /note="8"
FT REPEAT 822..827
FT /note="9"
FT REPEAT 828..833
FT /note="10"
FT REPEAT 834..839
FT /note="11"
FT REPEAT 840..845
FT /note="12"
FT REPEAT 846..851
FT /note="13"
FT REPEAT 852..857
FT /note="14"
FT REPEAT 858..863
FT /note="15"
FT REPEAT 864..869
FT /note="16"
FT REPEAT 870..875
FT /note="17"
FT REPEAT 876..881
FT /note="18"
FT REPEAT 882..887
FT /note="19"
FT REPEAT 888..893
FT /note="20"
FT REPEAT 894..899
FT /note="21"
FT REPEAT 900..905
FT /note="22"
FT DOMAIN 2113..2149
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2161..2276
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 2279..2339
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 749..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..905
FT /note="22 X 6 AA tandem repeats of E-[EKGV]-[PL]-[FSI]-
FT [PAT]-[STPL]"
FT REGION 1052..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..2112
FT /note="CS-2"
FT REGION 1435..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1528..1550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1719..1761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1784..1870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1906..2110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2114..2364
FT /note="G3"
FT COMPBIAS 789..897
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1719..1733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1743..1761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1818..1832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1839..1869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1954..1973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2000..2068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2076..2110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 2239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 2241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 2242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 2249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 2262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 2263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000255"
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 1350
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250|UniProtKB:P16112"
FT CARBOHYD 1387
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250|UniProtKB:P16112"
FT CARBOHYD 1401
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1407
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1411
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1421
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250|UniProtKB:P16112"
FT CARBOHYD 1523
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250|UniProtKB:P16112"
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 2117..2128
FT /evidence="ECO:0000250"
FT DISULFID 2122..2137
FT /evidence="ECO:0000250"
FT DISULFID 2139..2148
FT /evidence="ECO:0000250"
FT DISULFID 2182..2274
FT /evidence="ECO:0000250"
FT DISULFID 2250..2266
FT /evidence="ECO:0000250"
FT DISULFID 2281..2324
FT /evidence="ECO:0000250"
FT DISULFID 2310..2337
FT /evidence="ECO:0000250"
FT VAR_SEQ 2114..2150
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9308898"
FT /id="VSP_003072"
FT CONFLICT 573..576
FT /note="SETY -> QSET (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2364 AA; 246362 MW; 6FF83763420C3D4C CRC64;
MTTLLLVFVT LRVITAAISV EVSEPDNSLS VSIPEPSPLR VLLGSSLTIP CYFIDPMHPV
TTAPSTAPLA PRIKWSRISK EKEVVLLVAT EGRVRVNSAY QDKVTLPNYP AIPSDATLEI
QNMRSNDSGI LRCEVMHGIE DSQATLEVVV KGIVFHYRAI STRYTLDFDR AQRACLQNSA
IIATPEQLQA AYEDGFHQCD AGWLADQTVR YPIHTPREGC YGDKDEFPGV RTYGIRDTNE
TYDVYCFAEE MEGEVFYATS PEKFTFQEAA NECRRLGARL ATTGQLYLAW QGGMDMCSAG
WLADRSVRYP ISKARPNCGG NLLGVRTVYL HANQTGYPDP SSRYDAICYT GEDFVDIPES
FFGVGGEEDI TIQTVTWPDV ELPLPRNITE GEARGSVILT AKPDFEVSPT APEPEEPFTF
VPEVRATAFP EVENRTEEAT RPWAFPREST PGLGAPTAFT SEDLVVQVTL APGAAEVPGQ
PRLPGGVVFH YRPGSSRYSL TFEEAKQACL RTGAIIASPE QLQAAYEAGY EQCDAGWLQD
QTVRYPIVSP RTPCVGDKDS SPGVRTYGVR PPSETYDVYC YVDRLEGEVF FATRLEQFTF
WEAQEFCESQ NATLATTGQL YAAWSRGLDK CYAGWLADGS LRYPIVTPRP ACGGDKPGVR
TVYLYPNQTG LLDPLSRHHA FCFRGVSAAP SPEEEEGSAP TAGPDVEEWM VTQVGPGVAA
VPIGEETTAI PGFTVEPENK TEWELAYTPA GTLPLPGIPP TWPPTGEATE EHTEGPSATE
VPSASEKPFP SEEPFPPEEP FPSEKPFPPE ELFPSEKPFP SEKPFPSEEP FPSEKPFPPE
ELFPSEKPIP SEEPFPSEEP FPSEKPFPPE EPFPSEKPIP SEEPFPSEKP FPSEEPFPSE
EPSTLSAPVP SRTELPSSGE VSGVPEISGD FTGSGEISGH LDFSGQPSGE SASGLPSEDL
DSSGLTSTVG SGLPVESGLP SGEEERITWT SAPKVDRLPS GGEGPEVSGV EDISGLPSGG
EVHLEISASG VEDISGLPSG GEVHLEISAS GVEDLSRIPS GEGPEISASG VEDISGLPSG
EEGHLEISAS GVEDLSGIPS GEGPEVSASG VEDLIGLPSG EGPEVSASGV EDLSRLPSGE
GPEVSASGVE DLSGLPSGEG PEVSVSGVED LSRLPSGEGP EVSASGVEDL SRLPSGEGPE
ISVSGVEDIS ILPSGEGPEV SASGVEDLSV LPSGEGHLEI STSGVEDLSV LPSGEGHLET
SSGVEDISRL PSGEGPEVSA SGVEDLSVLP SGEDHLEISA SGVEDLGVLP SGEDHLEISA
SGVEDISRLP SGEGPEVSAS GVEDLSVLPS GEGHLEISAS GVEDLSRLPS GGEDHLETSA
SGVGDLSGLP SGREGLEISA SGAGDLSGLT SGKEDLTGSA SGALDLGRIP SVTLGSGQAP
EASGLPSGFS GEYSGVDLES GPSSGLPDFS GLPSGFPTVS LVDTTLVEVV TATTAGELEG
RGTIDISGAG ETSGLPFSEL DISGGASGLS SGAELSGQAS GSPDISGETS GLFGVSGQPS
GFPDISGETS GLLEVSGQPS GFYGEISGVT ELSGLASGQP EISGEASGIL SGLGPPFGIT
DLSGEAPGIP DLSGQPSGLP EFSGTASGIP DLVSSAVSGS GESSGITFVD TSLVEVTPTT
FKEEEGLGSV ELSGLPSGEL GVSGTSGLAD VSGLSSGAID SSGFTSQPPE FSGLPSGVTE
VSGEASGAES GSSLPSGAYD SSGLPSGFPT VSFVDRTLVE SVTQAPTAQE AGEGPSGILE
LSGAPSGAPD MSGDHLGSLD QSGLQSGLVE PSGEPASTPY FSGDFSGTTD VSGESSAATS
TSGEASGLPE VTLITSELVE GVTEPTVSQE LGQRPPVTYT PQLFESSGEA SASGDVPRFP
GSGVEVSSVP ESSGETSAYP EAEVGASAAP EASGGASGSP NLSETTSTFH EADLEGTSGL
GVSGSPSAFP EGPTEGLATP EVSGESTTAF DVSVEASGSP SATPLASGDR TDTSGDLSGH
TSGLDIVIST TIPESEWTQQ TQRPAEARLE IESSSPVHSG EESQTADTAT SPTDASIPAS
AGGTDDSEAT TTDIDECLSS PCLNGATCVD AIDSFTCLCL PSYQGDVCEI QKLCEEGWTK
FQGHCYRHFP DRATWVDAES QCRKQQSHLS SIVTPEEQEF VNNNAQDYQW IGLNDKTIEG
DFRWSDGHSL QFENWRPNQP DNFFATGEDC VVMIWHEKGE WNDVPCNYQL PFTCKKGTVA
CGEPPVVEHA RIFGQKKDRY EINALVRYQC TEGFIQGHVP TIRCQPSGHW EEPRITCTDP
ATYKRRLQKR SSRPLRRSHP STAH
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