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Aggrecan core protein (Cartilage-specific proteoglycan core protein) (CSPCP)

 PGCA_BOVIN              Reviewed;        2364 AA.
P13608; P79117; Q28159; Q6XL66;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 3.
20-JUN-2018, entry version 164.
RecName: Full=Aggrecan core protein;
AltName: Full=Cartilage-specific proteoglycan core protein;
Short=CSPCP;
Flags: Precursor;
Name=ACAN; Synonyms=AGC1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=9308898; DOI=10.1006/abbi.1997.0261;
Hering T.M., Kollar J., Huynh T.D.;
"Complete coding sequence of bovine aggrecan: comparative structural
analysis.";
Arch. Biochem. Biophys. 345:259-270(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=16167996; DOI=10.1111/j.1365-2052.2005.01340.x;
Cavanagh J.A.L., Tammen I., Hayden M.J., Gill C.A., Nicholas F.W.,
Raadsma H.W.;
"Characterization of the bovine aggrecan gene: genomic structure and
physical and linkage mapping.";
Anim. Genet. 36:452-454(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 563-1056.
PubMed=2528543;
Antonsson P., Heinegaard D., Oldberg A.;
"The keratan sulfate-enriched region of bovine cartilage proteoglycan
consists of a consecutively repeated hexapeptide motif.";
J. Biol. Chem. 264:16170-16173(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1609-2113 AND 2151-2364.
PubMed=3111460; DOI=10.1042/bj2430255;
Oldberg A., Antonsson P., Heinegaard D.;
"The partial amino acid sequence of bovine cartilage proteoglycan,
deduced from a cDNA clone, contains numerous Ser-Gly sequences
arranged in homologous repeats.";
Biochem. J. 243:255-259(1987).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 2114-2150 (ISOFORM 1).
TISSUE=Cartilage;
PubMed=8349621;
Fueloep C., Walcz E., Valyon M., Glant T.T.;
"Expression of alternatively spliced epidermal growth factor-like
domains in aggrecans of different species. Evidence for a novel
module.";
J. Biol. Chem. 268:17377-17383(1993).
[6]
PARTIAL PROTEIN SEQUENCE.
PubMed=6489519; DOI=10.1016/0014-5793(84)80907-2;
Perin J.-P., Bonnet F., Jolles J., Jolles P.;
"Sequence data concerning the protein core of the cartilage
proteoglycan monomers. Characterization of a sequence allowing the
synthesis of an oligonucleotide probe.";
FEBS Lett. 176:37-42(1984).
[7]
PARTIAL PROTEIN SEQUENCE.
PubMed=3530809; DOI=10.1016/0014-5793(86)81343-6;
Perin J.-P., Bonnet F., Jolles P.;
"Structural relationship between link proteins and proteoglycan
monomers.";
FEBS Lett. 206:73-77(1986).
[8]
PROTEIN SEQUENCE OF 152-157; 210-230; 482-506; 566-584; 631-641;
660-684; 2161-2167; 2276-2291; 2298-2307 AND 2318-2334.
PubMed=2022637;
Sandy J.D., Boynton R.E., Flannery C.R.;
"Analysis of the catabolism of aggrecan in cartilage explants by
quantitation of peptides from the three globular domains.";
J. Biol. Chem. 266:8198-8205(1991).
-!- FUNCTION: This proteoglycan is a major component of extracellular
matrix of cartilagenous tissues. A major function of this protein
is to resist compression in cartilage. It binds avidly to
hyaluronic acid via an N-terminal globular region. May play a
regulatory role in the matrix assembly of the cartilage.
-!- SUBUNIT: Interacts with FBLN1 and COMP. {ECO:0000250}.
-!- INTERACTION:
Q9UNA0:ADAMTS5 (xeno); NbExp=2; IntAct=EBI-6259246, EBI-2808663;
P49747:COMP (xeno); NbExp=2; IntAct=EBI-6259246, EBI-2531022;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P13608-1; Sequence=Displayed;
Name=2;
IsoId=P13608-2; Sequence=VSP_003072;
-!- DOMAIN: Two globular domains, G1 and G2, comprise the N-terminus
of the proteoglycan, while another globular region, G3, makes up
the C-terminus. G1 contains Link domains and thus consists of
three disulfide-bonded loop structures designated as the A, B, B'
motifs. G2 is similar to G1. The keratan sulfate (KS) and the
chondroitin sulfate (CS) attachment domains lie between G2 and G3.
-!- PTM: Contains mostly chondroitin sulfate, but also N-linked and O-
linked (about 40) oligosaccharides.
-!- PTM: The keratan sulfate contents differ considerably between
adult and fetal bovine proteoglycans.
-!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
{ECO:0000305}.
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EMBL; U76615; AAB38524.1; -; mRNA.
EMBL; AY226875; AAP44492.1; -; Genomic_DNA.
EMBL; AY226858; AAP44492.1; JOINED; Genomic_DNA.
EMBL; AY226859; AAP44492.1; JOINED; Genomic_DNA.
EMBL; AY226860; AAP44492.1; JOINED; Genomic_DNA.
EMBL; AY226861; AAP44492.1; JOINED; Genomic_DNA.
EMBL; AY226862; AAP44492.1; JOINED; Genomic_DNA.
EMBL; AY226863; AAP44492.1; JOINED; Genomic_DNA.
EMBL; AY226864; AAP44492.1; JOINED; Genomic_DNA.
EMBL; AY226865; AAP44492.1; JOINED; Genomic_DNA.
EMBL; AY226866; AAP44492.1; JOINED; Genomic_DNA.
EMBL; AY226867; AAP44492.1; JOINED; Genomic_DNA.
EMBL; AY226868; AAP44492.1; JOINED; Genomic_DNA.
EMBL; AY226871; AAP44492.1; JOINED; Genomic_DNA.
EMBL; AY226872; AAP44492.1; JOINED; Genomic_DNA.
EMBL; AY226873; AAP44492.1; JOINED; Genomic_DNA.
EMBL; AY226874; AAP44492.1; JOINED; Genomic_DNA.
EMBL; L07053; -; NOT_ANNOTATED_CDS; mRNA.
PIR; A29164; A29164.
PIR; A34234; A39808.
PIR; B29164; B29164.
PIR; S74144; S74144.
PIR; T42630; T42630.
RefSeq; NP_776406.1; NM_173981.2. [P13608-2]
UniGene; Bt.4953; -.
UniGene; Bt.92700; -.
ProteinModelPortal; P13608; -.
SMR; P13608; -.
IntAct; P13608; 3.
STRING; 9913.ENSBTAP00000021512; -.
PaxDb; P13608; -.
PeptideAtlas; P13608; -.
PRIDE; P13608; -.
GeneID; 280985; -.
KEGG; bta:280985; -.
CTD; 176; -.
eggNOG; ENOG410IJP2; Eukaryota.
eggNOG; ENOG410XRES; LUCA.
HOVERGEN; HBG007982; -.
InParanoid; P13608; -.
KO; K06792; -.
PMAP-CutDB; P13608; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
GO; GO:0005540; F:hyaluronic acid binding; IBA:GO_Central.
GO; GO:0007155; P:cell adhesion; IEA:InterPro.
GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
CDD; cd00033; CCP; 1.
CDD; cd03588; CLECT_CSPGs; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.10.100.10; -; 5.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR033987; CSPG_CTLD.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR000538; Link_dom.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
Pfam; PF00008; EGF; 1.
Pfam; PF00059; Lectin_C; 1.
Pfam; PF00084; Sushi; 1.
Pfam; PF07686; V-set; 1.
Pfam; PF00193; Xlink; 4.
PRINTS; PR01265; LINKMODULE.
SMART; SM00032; CCP; 1.
SMART; SM00034; CLECT; 1.
SMART; SM00181; EGF; 1.
SMART; SM00179; EGF_CA; 1.
SMART; SM00409; IG; 1.
SMART; SM00406; IGv; 1.
SMART; SM00445; LINK; 4.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF56436; SSF56436; 5.
SUPFAM; SSF57535; SSF57535; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS01241; LINK_1; 4.
PROSITE; PS50963; LINK_2; 4.
PROSITE; PS50923; SUSHI; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Complete proteome;
Direct protein sequencing; Disulfide bond; EGF-like domain;
Extracellular matrix; Glycoprotein; Immunoglobulin domain; Lectin;
Metal-binding; Proteoglycan; Reference proteome; Repeat; Secreted;
Signal; Sushi.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 2364 Aggrecan core protein.
/FTId=PRO_0000017502.
DOMAIN 25 147 Ig-like V-type.
DOMAIN 153 248 Link 1. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
DOMAIN 254 350 Link 2. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
DOMAIN 487 582 Link 3. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
DOMAIN 588 684 Link 4. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
REPEAT 774 779 1.
REPEAT 780 785 2.
REPEAT 786 791 3.
REPEAT 792 797 4.
REPEAT 798 803 5.
REPEAT 804 809 6.
REPEAT 810 815 7.
REPEAT 816 821 8.
REPEAT 822 827 9.
REPEAT 828 833 10.
REPEAT 834 839 11.
REPEAT 840 845 12.
REPEAT 846 851 13.
REPEAT 852 857 14.
REPEAT 858 863 15.
REPEAT 864 869 16.
REPEAT 870 875 17.
REPEAT 876 881 18.
REPEAT 882 887 19.
REPEAT 888 893 20.
REPEAT 894 899 21.
REPEAT 900 905 22.
DOMAIN 2113 2149 EGF-like; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2161 2276 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 2279 2339 Sushi. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
REGION 774 905 22 X 6 AA tandem repeats of E-[EKGV]-
[PL]-[FSI]-[PAT]-[STPL].
REGION 1433 2112 CS-2.
REGION 2114 2364 G3.
METAL 2215 2215 Calcium 1. {ECO:0000250}.
METAL 2219 2219 Calcium 1. {ECO:0000250}.
METAL 2219 2219 Calcium 3. {ECO:0000250}.
METAL 2239 2239 Calcium 2. {ECO:0000250}.
METAL 2241 2241 Calcium 2. {ECO:0000250}.
METAL 2242 2242 Calcium 1. {ECO:0000250}.
METAL 2248 2248 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 2248 2248 Calcium 2. {ECO:0000250}.
METAL 2249 2249 Calcium 1. {ECO:0000250}.
METAL 2249 2249 Calcium 3. {ECO:0000250}.
METAL 2262 2262 Calcium 2. {ECO:0000250}.
METAL 2263 2263 Calcium 2. {ECO:0000250}.
METAL 2263 2263 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 239 239 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 371 371 O-linked (Xyl...) (keratan sulfate)
threonine. {ECO:0000250}.
CARBOHYD 376 376 O-linked (Xyl...) (keratan sulfate)
threonine. {ECO:0000250}.
CARBOHYD 387 387 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 611 611 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 667 667 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 51 133 {ECO:0000250}.
DISULFID 175 246 {ECO:0000250}.
DISULFID 199 220 {ECO:0000250}.
DISULFID 273 348 {ECO:0000250}.
DISULFID 297 318 {ECO:0000250}.
DISULFID 509 580 {ECO:0000250}.
DISULFID 533 554 {ECO:0000250}.
DISULFID 607 682 {ECO:0000250}.
DISULFID 631 652 {ECO:0000250}.
DISULFID 2117 2128 {ECO:0000250}.
DISULFID 2122 2137 {ECO:0000250}.
DISULFID 2139 2148 {ECO:0000250}.
DISULFID 2182 2274 {ECO:0000250}.
DISULFID 2250 2266 {ECO:0000250}.
DISULFID 2281 2324 {ECO:0000250}.
DISULFID 2310 2337 {ECO:0000250}.
VAR_SEQ 2114 2150 Missing (in isoform 2).
{ECO:0000303|PubMed:9308898}.
/FTId=VSP_003072.
CONFLICT 573 576 SETY -> QSET (in Ref. 8; AA sequence).
{ECO:0000305}.
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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San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




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