ID   PGCA_MOUSE              Reviewed;        2132 AA.
AC   Q61282; E9QLS9; Q64021;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 190.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Cartilage;
RX   PubMed=7806222; DOI=10.1006/geno.1994.1396;
RA   Walcz E., Deak F., Erhardt P., Coulter S.N., Fueloep C., Horvath P.,
RA   Doege K.J., Glant T.T.;
RT   "Complete coding sequence, deduced primary structure, chromosomal
RT   localization, and structural analysis of murine aggrecan.";
RL   Genomics 22:364-371(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 211-326.
RC   STRAIN=129/Sv;
RX   PubMed=7920633; DOI=10.1038/ng0694-154;
RA   Watanabe H., Kimata K., Line S., Strong D., Gao L.-Y., Kozak C.A.,
RA   Yamada Y.;
RT   "Mouse cartilage matrix deficiency (cmd) caused by a 7 bp deletion in the
RT   aggrecan gene.";
RL   Nat. Genet. 7:154-157(1994).
RN   [4]
RP   INTERACTION WITH FBLN1.
RX   PubMed=10400671; DOI=10.1074/jbc.274.29.20444;
RA   Aspberg A., Adam S., Kostka G., Timpl R., Heinegaard D.;
RT   "Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and
RT   versican.";
RL   J. Biol. Chem. 274:20444-20449(1999).
RN   [5]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=7524681; DOI=10.1016/0167-4781(94)90220-8;
RA   Glumoff V., Savontaus M., Vehanen J., Vuorio E.;
RT   "Analysis of aggrecan and tenascin gene expression in mouse skeletal
RT   tissues by northern and in situ hybridization using species specific cDNA
RT   probes.";
RL   Biochim. Biophys. Acta 1219:613-622(1994).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 COMP (By similarity). Interacts with FBLN1.
CC       {ECO:0000250, ECO:0000269|PubMed:10400671}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in cartilage tissues.
CC       {ECO:0000269|PubMed:7524681}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in chondrocytes throughout the
CC       developing skeleton in a pattern very similar but not identical to
CC       those of type II and IX collagen. In the newborn mouse skeleton it is
CC       expressed essentially in a mutually exclusive manner with tenascin,
CC       which is expressed osteoblasts, periosteal and perichondrial cells, and
CC       in cells at articular surfaces. {ECO:0000269|PubMed:7524681}.
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   -!- DISEASE: Note=Defects in Acan are the cause of cartilage matrix
CC       deficiency (CMD). CMD is an autosomal recessive syndrome characterized
CC       by cleft palate, short limbs, tail and snout. Mutation in strain CMD
CC       causes absence of aggrecan by truncation of the protein (mutation in
CC       the G1 domain).
CC   -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Aggrecan;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_283";
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DR   EMBL; L07049; AAC37670.1; -; mRNA.
DR   EMBL; AC110520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; S73722; AAB32160.1; -; Genomic_DNA.
DR   EMBL; S73721; AAB32160.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS21377.1; -.
DR   PIR; A55182; A55182.
DR   RefSeq; NP_031450.2; NM_007424.2.
DR   AlphaFoldDB; Q61282; -.
DR   SMR; Q61282; -.
DR   BioGRID; 198020; 5.
DR   STRING; 10090.ENSMUSP00000032835; -.
DR   GlyConnect; 2114; 2 N-Linked glycans (1 site).
DR   GlyCosmos; Q61282; 9 sites, 2 glycans.
DR   GlyGen; Q61282; 16 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; Q61282; -.
DR   PhosphoSitePlus; Q61282; -.
DR   MaxQB; Q61282; -.
DR   PaxDb; 10090-ENSMUSP00000032835; -.
DR   PeptideAtlas; Q61282; -.
DR   ProteomicsDB; 288181; -.
DR   Antibodypedia; 4288; 605 antibodies from 33 providers.
DR   DNASU; 11595; -.
DR   Ensembl; ENSMUST00000032835.7; ENSMUSP00000032835.6; ENSMUSG00000030607.8.
DR   GeneID; 11595; -.
DR   KEGG; mmu:11595; -.
DR   UCSC; uc009hxw.1; mouse.
DR   AGR; MGI:99602; -.
DR   CTD; 176; -.
DR   MGI; MGI:99602; Acan.
DR   VEuPathDB; HostDB:ENSMUSG00000030607; -.
DR   eggNOG; ENOG502QUX8; Eukaryota.
DR   GeneTree; ENSGT00940000155971; -.
DR   HOGENOM; CLU_000303_2_0_1; -.
DR   InParanoid; Q61282; -.
DR   OMA; EDWIVTQ; -.
DR   OrthoDB; 5402504at2759; -.
DR   PhylomeDB; Q61282; -.
DR   TreeFam; TF332134; -.
DR   Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR   Reactome; R-MMU-2022857; Keratan sulfate degradation.
DR   Reactome; R-MMU-3000178; ECM proteoglycans.
DR   BioGRID-ORCS; 11595; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Acan; mouse.
DR   PRO; PR:Q61282; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q61282; Protein.
DR   Bgee; ENSMUSG00000030607; Expressed in humerus cartilage element and 83 other cell types or tissues.
DR   ExpressionAtlas; Q61282; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0072534; C:perineuronal net; ISO:MGI.
DR   GO; GO:0098966; C:perisynaptic extracellular matrix; IDA:SynGO.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; ISO:MGI.
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; IMP:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR   GO; GO:0002063; P:chondrocyte development; IMP:MGI.
DR   GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR   GO; GO:0010001; P:glial cell differentiation; IBA:GO_Central.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; IBA:GO_Central.
DR   GO; GO:0030166; P:proteoglycan biosynthetic process; IMP:MGI.
DR   GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR   CDD; cd00033; CCP; 1.
DR   CDD; cd03588; CLECT_CSPGs; 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; 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; 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   PANTHER; PTHR22804:SF42; AGGRECAN CORE PROTEIN; 1.
DR   PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 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; 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; SSF48726; Immunoglobulin; 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.
DR   Genevisible; Q61282; MM.
PE   1: Evidence at protein level;
KW   Calcium; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Immunoglobulin domain; Lectin; Metal-binding; Proteoglycan;
KW   Reference proteome; Repeat; Secreted; Signal; Sushi.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..2132
FT                   /note="Aggrecan core protein"
FT                   /id="PRO_0000017507"
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          1918..2044
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DOMAIN          2047..2107
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          486..580
FT                   /note="G2-B"
FT   REGION          587..682
FT                   /note="G2-B'"
FT   REGION          685..803
FT                   /note="KS"
FT   REGION          737..1079
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          805..1231
FT                   /note="CS-1"
FT   REGION          1108..1239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1232..1917
FT                   /note="CS-2"
FT   REGION          1299..1465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1491..1538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1586..1671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1782..1838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1861..1914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1917..2132
FT                   /note="G3"
FT   MOTIF           1171..1173
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        778..804
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        829..843
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        851..869
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        896..948
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        974..1007
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1014..1028
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1144..1164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1325..1465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1497..1533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1610..1671
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1782..1797
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1805..1833
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1983
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         1987
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         1987
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         2007
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         2009
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         2010
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         2016
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         2016
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         2017
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         2017
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         2030
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         2031
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        1150
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P16112"
FT   CARBOHYD        1186
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P16112"
FT   CARBOHYD        1200
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1206
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1210
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1220
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P16112"
FT   CARBOHYD        1322
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P16112"
FT   CARBOHYD        1675
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        1922..1933
FT                   /evidence="ECO:0000250"
FT   DISULFID        1950..2042
FT                   /evidence="ECO:0000250"
FT   DISULFID        2018..2034
FT                   /evidence="ECO:0000250"
FT   DISULFID        2049..2092
FT                   /evidence="ECO:0000250"
FT   DISULFID        2078..2105
FT                   /evidence="ECO:0000250"
FT   CONFLICT        482
FT                   /note="R -> H (in Ref. 1; AAC37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        515
FT                   /note="V -> I (in Ref. 1; AAC37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        568
FT                   /note="G -> R (in Ref. 1; AAC37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        696
FT                   /note="G -> E (in Ref. 1; AAC37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1701..1702
FT                   /note="TP -> IS (in Ref. 1; AAC37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1705
FT                   /note="F -> S (in Ref. 1; AAC37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1729
FT                   /note="I -> V (in Ref. 1; AAC37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1938
FT                   /note="H -> P (in Ref. 1; AAC37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2119
FT                   /note="S -> T (in Ref. 1; AAC37670)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2132 AA;  221941 MW;  17298662D95E1921 CRC64;
     MTTLLLVFVT LRVIAAVISE EVPDHDNSLS VSIPQPSPLK VLLGSSLTIP CYFIDPMHPV
     TTAPSTAPLT PRIKWSRVSK EKEVVLLVAT EGQVRVNSIY QDKVSLPNYP AIPSDATLEI
     QNLRSNDSGI YRCEVMHGIE DSEATLEVIV KGIVFHYRAI STRYTLDFDR AQRACLQNSA
     IIATPEQLQA AYEDGFHQCD AGWLADQTVR YPIHTPREGC YGDKDEFPGV RTYGIRDTNE
     TYDVYCFAEE MEGEVFYATS PEKFTFQEAA NECRRLGARL ATTGQLYLAW QGGMDMCSAG
     WLADRSVRYP ISKARPNCGG NLLGVRTVYL HANQTGYPDP SSRYDAICYT GEDFVDIPEN
     FFGVGGEDDI TIQTVTWPDL ELPLPRNVTE GEALGSVILT AKPIFDLSPT ISEPGEALTL
     APEVGSTAFP EAEERTGEAT RPWGFPAEVT RGPDSATAFA SEDLVVRVTI SPGAAEVPGQ
     PRLPGGVVFH YRPGSTRYSL TFEEAQQACM HTGAVIASPE QLQAAYEAGY EQCDAGWLQD
     QTVRYPIVSP RTPCVGDKDS SPGVRTYGVR PSSETYDVYC YVDKLEGEVF FATRLEQFTF
     QEARAFCAAQ NATLASTGQL YAAWSQGLDK CYAGWLADGT LRYPIITPRP ACGGDKPGVR
     TVYLYPNQTG LPDPLSKHHA FCFRGVSVAP SPGEEGGSTP TSPSDIEDWI VTQVGPGVDA
     VPLEPKTTEV PYFTTEPRKQ TEWEPAYTPV GTSPQPGIPP TWLPTLPAAE EHTESPSASE
     EPSASAVPST SEEPYTSSFA VPSMTELPGS GEASGAPDLS GDFTGSGDAS GRLDSSGQPS
     GGIESGLPSG DLDSSGLSPT VSSGLPVESG SASGDGEVPW SHTPTVGRLP SGGESPEGSA
     SASGTGDLSG LPSGGEITET STSGAEETSG LPSGGDGLET STSGVDDVSG IPTGREGLET
     SASGVEDLSG LPSGEEGSET STSGIEDISV LPTGGESLET SASGVGDLSG LPSGGESLET
     SASGAEDVTQ LPTERGGLET SASGVEDITV LPTGRESLET SASGVEDVSG LPSGREGLET
     SASGIEDISV FPTEAEGLDT SASGGYVSGI PSGGDGTETS ASGVEDVSGL PSGGEGLETS
     ASGVEDLGPS TRDSLETSAS GVDVTGFPSG RGDPETSVSG VGDDFSGLPS GKEGLETSAS
     GAEDLSGLPS GKEDLVGSAS GALDFGKLPP GTLGSGQTPE VNGFPSGFSG EYSGADIGSG
     PSSGLPDFSG LPSGFPTVSL VDSTLVEVIT ATTSSELEGR GTIGISGSGE VSGLPLGELD
     SSADISGLPS GTELSGQASG SPDSSGETSG FFDVSGQPFG SSGVSEETSG IPEISGQPSG
     TPDTTATSGV TELNELSSGQ PDVSGDGSGI LFGSGQSSGI TSVSGETSGI SDLSGQPSGF
     PVFSGTATRT PDLASGTISG SGESSGITFV DTSFVEVTPT TFREEEGLGS VELSGFPSGE
     TELSGTSGTV DVSEQSSGAI DSSGLTSPTP EFSGLPSGVA EVSGEFSGVE TGSSLPSGAF
     DGSGLVSGFP TVSLVDRTLV ESITQAPTAQ EAGEGPSGIL EFSGAHSGTP DISGELSGSL
     DLSTLQSGQM ETSTETPSSP YFSGDFSSTT DVSGESIAAT TGSGESSGLP EVTLNTSELV
     EGVTEPTVSQ ELGHGPSMTY TPRLFEASGD ASASGDLGGA VTNFPGSGIE ASVPEASSDL
     SAYPEAGVGV SAAPEASSKL SEFPDLHGIT SAFHETDLEM TTPSTEVNSN PWTFQEGTRE
     GSAAPEVSGE SSTTSDIDTG TSGVPSATPM ASGDRTEISG EWSDHTSEVN VAISSTITES
     EWAQPTRYPT ETLQEIESPN PSYSGEETQT AETTMSLTDA PTLSSSEGSG ETESTVADQE
     QCEEGWTKFQ GHCYRHFHDR ETWVDAERRC REQQSHLSSI VTPEEQEFVN KNAQDYQWIG
     LNDRTIEGDF RWSDGHSLQF EKWRPNQPDN FFATGEDCVV MIWHERGEWN DVPCNYQLPF
     TCKKGTVACG DPPVVEHART LGQKKDRYEI SSLVRYQCTE GFVQRHVPTI RCQPSGHWEE
     PRITCTDPNT YKHRLQKRSM RPTRRSRPSM AH
//