PGCA_CHICK
ID PGCA_CHICK Reviewed; 2109 AA.
AC P07898; Q90810; Q90820; Q90991; Q91047;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 169.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=White leghorn; TISSUE=Embryo;
RX PubMed=8226878; DOI=10.1016/s0021-9258(19)49491-x;
RA Li H., Schwartz N.B., Vertel B.M.;
RT "cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core
RT protein and identification of a stop codon in the aggrecan gene associated
RT with the chondrodystrophy, nanomelia.";
RL J. Biol. Chem. 268:23504-23511(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Cartilage;
RX PubMed=1339285; DOI=10.1042/bj2880903;
RA Chandrasekaran L., Tanzer M.L.;
RT "Molecular cloning of chicken aggrecan. Structural analyses.";
RL Biochem. J. 288:903-910(1992).
RN [3]
RP ERRATUM OF PUBMED:1339285.
RX PubMed=8280087; DOI=10.1042/bj2960885b;
RA Chandrasekaran L., Tanzer M.L.;
RL Biochem. J. 296:885-887(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1042-1559 (ISOFORMS 1/2).
RC TISSUE=Embryo;
RX PubMed=1694853; DOI=10.1016/s0021-9258(19)38510-2;
RA Krueger R.C. Jr., Fields T.A., Mensch J.R. Jr., Schwartz N.B.;
RT "Chick cartilage chondroitin sulfate proteoglycan core protein. II.
RT Nucleotide sequence of cDNA clone and localization of the S103L epitope.";
RL J. Biol. Chem. 265:12088-12097(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1492-1610.
RC STRAIN=White leghorn; TISSUE=Chondrocyte;
RX PubMed=7827752; DOI=10.1016/0945-053x(94)90195-3;
RA Primorac D., Stover M.L., Clark S.H., Rowe D.W.;
RT "Molecular basis of nanomelia, a heritable chondrodystrophy of chicken.";
RL Matrix Biol. 14:297-305(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1693-2109 (ISOFORM 2).
RX PubMed=3460082; DOI=10.1073/pnas.83.14.5081;
RA Sai S., Tanaka T., Kosher R.A., Tanzer M.L.;
RT "Cloning and sequence analysis of a partial cDNA for chicken cartilage
RT proteoglycan core protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:5081-5085(1986).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1894-2109.
RX PubMed=3170613; DOI=10.1016/s0021-9258(19)37663-x;
RA Tanaka T., Har-El R., Tanzer M.L.;
RT "Partial structure of the gene for chicken cartilage proteoglycan core
RT protein.";
RL J. Biol. Chem. 263:15831-15835(1988).
RN [8]
RP PROTEIN SEQUENCE OF 718-736; 998-1023 AND 1247-1275, AND GLYCOSYLATION AT
RP THR-728; SER-1006; SER-1010; SER-1016; SER-1249; SER-1253; SER-1259;
RP SER-1263 AND SER-1269.
RX PubMed=2365711; DOI=10.1016/s0021-9258(19)38509-6;
RA Krueger R.C. Jr., Fields T.A., Hildreth J. IV, Schwartz N.B.;
RT "Chick cartilage chondroitin sulfate proteoglycan core protein. I.
RT Generation and characterization of peptides and specificity for
RT glycosaminoglycan attachment.";
RL J. Biol. Chem. 265:12075-12087(1990).
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 -!- 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=P07898-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P07898-2; Sequence=VSP_003073;
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:2365711}.
CC -!- DISEASE: Note=Defects in ACAN are the cause of nanomelia, a lethal
CC connective tissue disorder affecting cartilage development
CC (chondrodystrophy) characterized by shortened and malformed limbs.
CC Aggrecan is truncated at its C-terminus in the CS-2 binding domain and
CC is not anymore secreted from the chondrocytes.
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; L21913; AAB19128.1; -; mRNA.
DR EMBL; M88101; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M38187; AAA48731.1; -; mRNA.
DR EMBL; S74657; AAC60751.1; -; Genomic_DNA.
DR EMBL; S74656; AAC60751.1; JOINED; Genomic_DNA.
DR EMBL; M13993; AAA48720.1; -; mRNA.
DR EMBL; J04028; AAA48719.1; -; Genomic_DNA.
DR PIR; I50421; I50421.
DR AlphaFoldDB; P07898; -.
DR SMR; P07898; -.
DR STRING; 9031.ENSGALP00000037775; -.
DR iPTMnet; P07898; -.
DR PaxDb; P07898; -.
DR VEuPathDB; HostDB:geneid_395798; -.
DR eggNOG; ENOG502QUX8; Eukaryota.
DR InParanoid; P07898; -.
DR PhylomeDB; P07898; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:0001501; P:skeletal system development; IBA:GO_Central.
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; 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 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; SM00445; LINK; 4.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF56436; SSF56436; 5.
DR SUPFAM; SSF57535; SSF57535; 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..2109
FT /note="Aggrecan core protein"
FT /id="PRO_0000017504"
FT DOMAIN 34..143
FT /note="Ig-like V-type"
FT DOMAIN 149..244
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 250..347
FT /note="Link 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 520..615
FT /note="Link 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 621..717
FT /note="Link 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT REPEAT 1363..1382
FT /note="1"
FT REPEAT 1383..1402
FT /note="2"
FT REPEAT 1403..1422
FT /note="3"
FT REPEAT 1423..1442
FT /note="4"
FT REPEAT 1443..1462
FT /note="5"
FT REPEAT 1463..1482
FT /note="6"
FT REPEAT 1483..1502
FT /note="7"
FT REPEAT 1503..1522
FT /note="8"
FT REPEAT 1523..1542
FT /note="9"
FT REPEAT 1543..1562
FT /note="10"
FT REPEAT 1563..1582
FT /note="11"
FT REPEAT 1583..1602
FT /note="12"
FT REPEAT 1603..1622
FT /note="13"
FT REPEAT 1623..1642
FT /note="14"
FT REPEAT 1643..1662
FT /note="15"
FT REPEAT 1663..1682
FT /note="16"
FT REPEAT 1683..1702
FT /note="17"
FT REPEAT 1703..1722
FT /note="18"
FT REPEAT 1723..1742
FT /note="19"
FT DOMAIN 1855..1892
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1901..2019
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 2022..2082
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 48..137
FT /note="G1-A"
FT REGION 148..243
FT /note="G1-B"
FT REGION 249..346
FT /note="G1-B'"
FT REGION 519..613
FT /note="G2-B"
FT REGION 620..715
FT /note="G2-B'"
FT REGION 718..803
FT /note="KS"
FT REGION 743..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..1264
FT /note="CS-1"
FT REGION 904..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1265..1742
FT /note="CS-2"
FT REGION 1363..1742
FT /note="19 X 20 AA tandem repeats of E-[TA]-S-T-[ADHIFSRVT]-
FT [YQLRH]-E-[IVTAG]-[SR]-[GS]-E-[SAT]-[SP]-[AG]-[FYL]-P-[EA]-
FT [TIV]-[SRTG]-[IVT]"
FT REGION 1371..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1645..1716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1746..1820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1893..2109
FT /note="G3"
FT COMPBIAS 753..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1645..1672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1679..1713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1760..1784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1804..1820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1958
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1962
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1962
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1982
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1984
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1985
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1991
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1991
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1992
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1992
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 2005
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 2006
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT SITE 1001
FT /note="Not glycosylated"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 700
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 728
FT /note="O-linked (Xyl...) (keratan sulfate) threonine"
FT /evidence="ECO:0000269|PubMed:2365711"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 801
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1006
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:2365711"
FT CARBOHYD 1010
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:2365711"
FT CARBOHYD 1016
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:2365711"
FT CARBOHYD 1020
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000305"
FT CARBOHYD 1249
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:2365711"
FT CARBOHYD 1253
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:2365711"
FT CARBOHYD 1259
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:2365711"
FT CARBOHYD 1263
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:2365711"
FT CARBOHYD 1269
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:2365711"
FT CARBOHYD 1273
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000305"
FT DISULFID 51..129
FT /evidence="ECO:0000250"
FT DISULFID 171..242
FT /evidence="ECO:0000250"
FT DISULFID 195..216
FT /evidence="ECO:0000250"
FT DISULFID 269..345
FT /evidence="ECO:0000250"
FT DISULFID 293..314
FT /evidence="ECO:0000250"
FT DISULFID 542..613
FT /evidence="ECO:0000250"
FT DISULFID 566..587
FT /evidence="ECO:0000250"
FT DISULFID 640..715
FT /evidence="ECO:0000250"
FT DISULFID 664..685
FT /evidence="ECO:0000250"
FT DISULFID 1859..1870
FT /evidence="ECO:0000250"
FT DISULFID 1864..1879
FT /evidence="ECO:0000250"
FT DISULFID 1881..1890
FT /evidence="ECO:0000250"
FT DISULFID 1897..1908
FT /evidence="ECO:0000250"
FT DISULFID 1925..2017
FT /evidence="ECO:0000250"
FT DISULFID 1993..2009
FT /evidence="ECO:0000250"
FT DISULFID 2024..2067
FT /evidence="ECO:0000250"
FT DISULFID 2053..2080
FT /evidence="ECO:0000250"
FT VAR_SEQ 1856..1892
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1339285,
FT ECO:0000303|PubMed:3460082"
FT /id="VSP_003073"
FT CONFLICT 362
FT /note="E -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 601
FT /note="G -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1000
FT /note="P -> R (in Ref. 2; M88101)"
FT /evidence="ECO:0000305"
FT CONFLICT 1029
FT /note="A -> P (in Ref. 2; M88101)"
FT /evidence="ECO:0000305"
FT CONFLICT 1042..1043
FT /note="VT -> PA (in Ref. 4; AAA48731)"
FT /evidence="ECO:0000305"
FT CONFLICT 1251
FT /note="E -> D (in Ref. 2 and 8)"
FT /evidence="ECO:0000305"
FT CONFLICT 1587
FT /note="I -> T (in Ref. 5; AAC60751)"
FT /evidence="ECO:0000305"
FT CONFLICT 1590
FT /note="I -> V (in Ref. 5; AAC60751)"
FT /evidence="ECO:0000305"
FT CONFLICT 1594
FT /note="T -> S (in Ref. 5; AAC60751)"
FT /evidence="ECO:0000305"
FT CONFLICT 1602..1610
FT /note="IETSTVREI -> VLCRCSVLR (in Ref. 5; AAC60751)"
FT /evidence="ECO:0000305"
FT CONFLICT 1603
FT /note="E -> A (in Ref. 2; M88101)"
FT /evidence="ECO:0000305"
FT CONFLICT 1672
FT /note="S -> G (in Ref. 2; M88101)"
FT /evidence="ECO:0000305"
FT CONFLICT 1796
FT /note="E -> G (in Ref. 2 and 6; AAA48720)"
FT /evidence="ECO:0000305"
FT CONFLICT 1988
FT /note="F -> S (in Ref. 7; AAA48719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2109 AA; 223493 MW; 7F824FD5B3A2ABDA CRC64;
MTTLLLVFVC LQAITTAASA ELSDSSDGLE VKIPEQSPLR VVLGSSLNIP CYFNIPEEED
TNALLTPRIK WSKLSNGTEI VLLVATGGKI RLNAEYREVI SLPNYPAIPT DATLEIKALR
SNHTGIYRCE VMYGIEDRQD TIEVLVKGVV FHYRAISTRY TLNFERAKQA CIQNSAVIAT
PEQLQAAYED GYEQCDAGWL ADQTVRYPIH LPRERCYGDK DEFPGVRTYG VRETDETYDV
YCYAEQMQGK VFYATSPEKF TFQEAFDKCH SLGARLATTG ELYLAWKDGM DMCSAGWLAD
RSVRYPISRA RPNCGGNLVG VRTVYLNPAN QTGYPHPSSR YDAICYSGDD FEALVPGLFT
DEVGTELGSA FTIQTVTQTE VELPLPRNVT EEEARGSIAT LEPMEITATA TELYEAFTVL
PDLFATSVTV ETASPREENV TREEITGIWA VPEEVTTSVS GTAFTTGMAE VSSVEEAIAV
TATPGLESAS PFTIEDHLVQ VTAAPDVALL PRQPISPTGV VFHYRAATSR YAFSFIQAQQ
ACLENNAVIA TPEQLQAAYE AGFDQCDAGW LRDQTVRYPI VNPRSNCVGD KESSPGVRSY
GMRPASETYD VYCYIDRLKG EVFFATQPEQ FTFQEAQLYC ESQNATLASA GQLHAAWKQG
LDRCYPGWLA DGSLRYPIVS PRPACGGDAP GVRTIYQHHN QTGFPDPLSR HHAFCFRALP
SVVEEGVTSL FEEEVMVTQL IPGVEGIPSG EETTVETELS SEPENQTAQG TEVFPTDVSL
LSARPSAFPP ATVIPEETST NASIPEVSGE FPESGEHPTS GEPSASGAPD TSGEPTSVGF
ELSGEQSGIG ESGLPSVDLQ SSGFVPGESG LPSGDVSGLP SGIVDISGLP SAEEEVTVSV
SRIPEVSGMP SGAESSGLHS GFSGEISGTE LISGLPSGEE SGLASGFPTI SLVDSTLVEV
VTAAPGRQEE GKGSIGVSGE EELSGFPSAE WDSSGARGLP SGAETSGEQS GVPELSGEHS
GVPGLSGEAF EVPELSGEHS GVTELSGEHS GLPELSGEPF GVPELSGFPS GLDISGEPSG
APEVSGPVDV SGLTSGVDGS GEVSGVTFIS TSLQEVTTPS VAEAEAKEIL EISGLPSGET
SGMVSGSLDV SGQPSGHIGF GGSASGVLEM SGFPGGAVES SGEASGVEVT SGLASGEESG
LTSGFPTVSL VDTTLVEVVT QTSVAQEVGE GPSGMIEISG FLSGDRGVSG EGSGAVQSSG
LPSGTGDFSG EPSGIPYFSG DISGATDLSG QPSAVTDISG EDSGLPEVTL VTSDLVEVVT
RPTVSQELGG ETAVTFPYVF GPSGEGSASG DLSGGASAEG GIETSTAYEI SGESSAFPET
SIETSTDQEI SGEASAYPEI SVETSTHLET SGETSAYPEI STETSTIQEV SGETSAFPEI
STETSTIQEI SGETSAFPEI RIETSTFQEI SGETSAFPEI RIETSTSQEA RGETSAFPEI
TIEASTVHET SGETSAFPEI SIETSTVHET SGETSAFPEI SIETSTVHEI SGESSAFPEI
RIETSTSQEA RGETSAFPEI TIEASTIQEI SGETSAFPEI SIETSTVREI SGETSAFPEI
RIETSTSQEA RGETSALPEI TIETSTVHET SGEASAFPEI SIETSTRQEA RSEASAYPEV
SIEASTTQEV SGESSAFPEI SVETSTSQEA RGETSAFPEI GIETSTAHEG SGETPGLPAV
STDTAATSLA SGEPSGAPEK ETPDTTSHLI TGVSGETSVP DAVISTSAPD VELAQEPRNT
EETQLEIEPS TPAASGQETE TAAVLDNPHL PATATAALHP ASQEAVDALG PTTEDTDECH
SSPCLNGATC VDGIDSFKCL CLPSYGGDLC EIDLANCEEG WIKFQGHCYR HFEERETWMD
AESRCREHQA HLSSIITPEE QEFVNSHAQD YQWIGLSDRA VENDFRWSDG HSLQFENWRP
NQPDNFFFAG EDCVVMIWHE QGEWNDVPCN YHLPFTCKKG TVACGDPPVV ENARTFGRKK
DRYEINSLVR YQCDHGYIQR HVPTIRCQPN GHWEEPRISC TNPSSYQRRL YKRSPRSRLR
PGVVHRPTH
