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Database: UniProt
Entry: P13608
LinkDB: P13608
Original site: P13608 
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   16-JAN-2019, entry version 166.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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;
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,
RT   deduced from a cDNA clone, contains numerous Ser-Gly sequences
RT   arranged in 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;
RA   Fueloep C., Walcz E., Valyon M., Glant T.T.;
RT   "Expression of alternatively spliced epidermal growth factor-like
RT   domains in aggrecans of different species. Evidence for a novel
RT   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
RT   proteoglycan monomers. Characterization of a sequence allowing the
RT   synthesis of an 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
RT   monomers.";
RL   FEBS Lett. 206:73-77(1986).
RN   [8]
RP   PROTEIN SEQUENCE OF 152-157; 210-230; 482-506; 566-584; 631-641;
RP   660-684; 2161-2167; 2276-2291; 2298-2307 AND 2318-2334.
RX   PubMed=2022637;
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
CC       is to resist compression in cartilage. It binds avidly to
CC       hyaluronic acid via an N-terminal globular region. May play a
CC       regulatory role in the matrix assembly of the cartilage.
CC   -!- SUBUNIT: Interacts with FBLN1 and COMP. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9UNA0:ADAMTS5 (xeno); NbExp=2; IntAct=EBI-6259246, EBI-2808663;
CC       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
CC       of the proteoglycan, while another globular region, G3, makes up
CC       the C-terminus. G1 contains Link domains and thus consists of
CC       three disulfide-bonded loop structures designated as the A, B, B'
CC       motifs. G2 is similar to G1. The keratan sulfate (KS) and the
CC       chondroitin sulfate (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
CC       adult and fetal bovine proteoglycans.
CC   -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC       {ECO:0000305}.
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   UniGene; Bt.4953; -.
DR   UniGene; Bt.92700; -.
DR   ProteinModelPortal; P13608; -.
DR   SMR; P13608; -.
DR   IntAct; P13608; 3.
DR   STRING; 9913.ENSBTAP00000021512; -.
DR   PaxDb; P13608; -.
DR   PeptideAtlas; P13608; -.
DR   PRIDE; P13608; -.
DR   GeneID; 280985; -.
DR   KEGG; bta:280985; -.
DR   CTD; 176; -.
DR   eggNOG; ENOG410IJP2; Eukaryota.
DR   eggNOG; ENOG410XRES; LUCA.
DR   HOVERGEN; HBG007982; -.
DR   InParanoid; P13608; -.
DR   KO; K06792; -.
DR   OrthoDB; 156064at2759; -.
DR   PMAP-CutDB; P13608; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
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; IPR013032; EGF-like_CS.
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; 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; 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; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Immunoglobulin domain; Lectin;
KW   Metal-binding; Proteoglycan; Reference proteome; Repeat; Secreted;
KW   Signal; Sushi.
FT   SIGNAL        1     16       {ECO:0000255}.
FT   CHAIN        17   2364       Aggrecan core protein.
FT                                /FTId=PRO_0000017502.
FT   DOMAIN       25    147       Ig-like V-type.
FT   DOMAIN      153    248       Link 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN      254    350       Link 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN      487    582       Link 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN      588    684       Link 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   REPEAT      774    779       1.
FT   REPEAT      780    785       2.
FT   REPEAT      786    791       3.
FT   REPEAT      792    797       4.
FT   REPEAT      798    803       5.
FT   REPEAT      804    809       6.
FT   REPEAT      810    815       7.
FT   REPEAT      816    821       8.
FT   REPEAT      822    827       9.
FT   REPEAT      828    833       10.
FT   REPEAT      834    839       11.
FT   REPEAT      840    845       12.
FT   REPEAT      846    851       13.
FT   REPEAT      852    857       14.
FT   REPEAT      858    863       15.
FT   REPEAT      864    869       16.
FT   REPEAT      870    875       17.
FT   REPEAT      876    881       18.
FT   REPEAT      882    887       19.
FT   REPEAT      888    893       20.
FT   REPEAT      894    899       21.
FT   REPEAT      900    905       22.
FT   DOMAIN     2113   2149       EGF-like; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2161   2276       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN     2279   2339       Sushi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   REGION      774    905       22 X 6 AA tandem repeats of E-[EKGV]-
FT                                [PL]-[FSI]-[PAT]-[STPL].
FT   REGION     1433   2112       CS-2.
FT   REGION     2114   2364       G3.
FT   METAL      2215   2215       Calcium 1. {ECO:0000250}.
FT   METAL      2219   2219       Calcium 1. {ECO:0000250}.
FT   METAL      2219   2219       Calcium 3. {ECO:0000250}.
FT   METAL      2239   2239       Calcium 2. {ECO:0000250}.
FT   METAL      2241   2241       Calcium 2. {ECO:0000250}.
FT   METAL      2242   2242       Calcium 1. {ECO:0000250}.
FT   METAL      2248   2248       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL      2248   2248       Calcium 2. {ECO:0000250}.
FT   METAL      2249   2249       Calcium 1. {ECO:0000250}.
FT   METAL      2249   2249       Calcium 3. {ECO:0000250}.
FT   METAL      2262   2262       Calcium 2. {ECO:0000250}.
FT   METAL      2263   2263       Calcium 2. {ECO:0000250}.
FT   METAL      2263   2263       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   CARBOHYD    126    126       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    239    239       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    333    333       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    371    371       O-linked (Xyl...) (keratan sulfate)
FT                                threonine. {ECO:0000250}.
FT   CARBOHYD    376    376       O-linked (Xyl...) (keratan sulfate)
FT                                threonine. {ECO:0000250}.
FT   CARBOHYD    387    387       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    611    611       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    667    667       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     51    133       {ECO:0000250}.
FT   DISULFID    175    246       {ECO:0000250}.
FT   DISULFID    199    220       {ECO:0000250}.
FT   DISULFID    273    348       {ECO:0000250}.
FT   DISULFID    297    318       {ECO:0000250}.
FT   DISULFID    509    580       {ECO:0000250}.
FT   DISULFID    533    554       {ECO:0000250}.
FT   DISULFID    607    682       {ECO:0000250}.
FT   DISULFID    631    652       {ECO:0000250}.
FT   DISULFID   2117   2128       {ECO:0000250}.
FT   DISULFID   2122   2137       {ECO:0000250}.
FT   DISULFID   2139   2148       {ECO:0000250}.
FT   DISULFID   2182   2274       {ECO:0000250}.
FT   DISULFID   2250   2266       {ECO:0000250}.
FT   DISULFID   2281   2324       {ECO:0000250}.
FT   DISULFID   2310   2337       {ECO:0000250}.
FT   VAR_SEQ    2114   2150       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:9308898}.
FT                                /FTId=VSP_003072.
FT   CONFLICT    573    576       SETY -> QSET (in Ref. 8; AA sequence).
FT                                {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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