GenomeNet

Database: UniProt
Entry: Q28343
LinkDB: Q28343
Original site: Q28343 
ID   PGCA_CANLF              Reviewed;        2333 AA.
AC   Q28343; Q28310;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   10-APR-2019, entry version 137.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Glant T.T., Adams M.E., Kwok S.X.F., Huang D., Fueloep C.;
RT   "Complete coding sequence and deduced amino acid sequence of aggrecan
RT   of canine cartilage.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 774-833.
RC   TISSUE=Cartilage;
RX   PubMed=7827755; DOI=10.1016/0945-053X(94)90198-8;
RA   Barry F.P., Neame P.J., Sasse J., Pearson D.;
RT   "Length variation in the keratan sulfate domain of mammalian
RT   aggrecan.";
RL   Matrix Biol. 14:323-328(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1830-2333.
RA   Adams M.E., Kowk S.X.F., Huang D., Glant T.T., Fullop C.;
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2082-2118.
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).
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   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
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 keratan sulfate
CC       chains, N-linked and O-linked oligosaccharides. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC       {ECO:0000305}.
DR   EMBL; U65989; AAB06238.2; -; mRNA.
DR   EMBL; S74662; AAC60527.1; -; mRNA.
DR   EMBL; L07054; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; I46998; I46998.
DR   UniGene; Cfa.3605; -.
DR   ProteinModelPortal; Q28343; -.
DR   SMR; Q28343; -.
DR   STRING; 9612.ENSCAFP00000016949; -.
DR   PaxDb; Q28343; -.
DR   PRIDE; Q28343; -.
DR   eggNOG; ENOG410IJP2; Eukaryota.
DR   eggNOG; ENOG410XRES; LUCA.
DR   HOGENOM; HOG000168421; -.
DR   HOVERGEN; HBG007982; -.
DR   InParanoid; Q28343; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; 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: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; 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   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; PS00290; IG_MHC; 1.
DR   PROSITE; PS01241; LINK_1; 4.
DR   PROSITE; PS50963; LINK_2; 4.
DR   PROSITE; PS50923; SUSHI; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Complete proteome; 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   2333       Aggrecan core protein.
FT                                /FTId=PRO_0000017503.
FT   DOMAIN       34    147       Ig-like V-type.
FT   DOMAIN      153    248       Link 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN      253    350       Link 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN      496    591       Link 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN      597    693       Link 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN     2081   2117       EGF-like; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     2130   2245       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN     2248   2308       Sushi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   REGION       48    140       G1-A.
FT   REGION      152    247       G1-B.
FT   REGION      253    349       G1-B'.
FT   REGION      495    589       G2-B.
FT   REGION      596    691       G2-B'.
FT   REGION      694    816       KS.
FT   REGION      819   1394       CS-1.
FT   REGION     1395   2079       CS-2.
FT   REGION     2080   2333       G3.
FT   METAL      2184   2184       Calcium 1. {ECO:0000250}.
FT   METAL      2188   2188       Calcium 1. {ECO:0000250}.
FT   METAL      2188   2188       Calcium 3. {ECO:0000250}.
FT   METAL      2208   2208       Calcium 2. {ECO:0000250}.
FT   METAL      2210   2210       Calcium 2. {ECO:0000250}.
FT   METAL      2211   2211       Calcium 1. {ECO:0000250}.
FT   METAL      2217   2217       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL      2217   2217       Calcium 2. {ECO:0000250}.
FT   METAL      2218   2218       Calcium 1. {ECO:0000250}.
FT   METAL      2218   2218       Calcium 3. {ECO:0000250}.
FT   METAL      2231   2231       Calcium 2. {ECO:0000250}.
FT   METAL      2232   2232       Calcium 2. {ECO:0000250}.
FT   METAL      2232   2232       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    444    444       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    620    620       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    676    676       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    747    747       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    518    589       {ECO:0000250}.
FT   DISULFID    542    563       {ECO:0000250}.
FT   DISULFID    616    691       {ECO:0000250}.
FT   DISULFID    640    661       {ECO:0000250}.
FT   DISULFID   2085   2096       {ECO:0000250}.
FT   DISULFID   2090   2105       {ECO:0000250}.
FT   DISULFID   2107   2116       {ECO:0000250}.
FT   DISULFID   2123   2134       {ECO:0000250}.
FT   DISULFID   2151   2243       {ECO:0000250}.
FT   DISULFID   2219   2235       {ECO:0000250}.
FT   DISULFID   2250   2293       {ECO:0000250}.
FT   DISULFID   2279   2306       {ECO:0000250}.
SQ   SEQUENCE   2333 AA;  240576 MW;  8B9ED78F3508B596 CRC64;
     MTTLLWVFVT LRVITAASSE ETSDHDNSLS VSIPEPSPMR VLLGSSLTIP CYFIDPMHPV
     TTAPSTAPLA PRIKWSRITK EKEVVLLVAT EGQVRINSAY QDKVSLPNYP AIPSDATLEI
     QNLRSNDSGI YRCEVMHGIE DSEATLEVVV KGIVFHYRAI STRYTLDFDR AQRACLQNSA
     IIATPEQLQA AYEDGFHQCD AGWLADQTVR YPIHTPREGC YGDKDEFPGV RTYGIRDTNE
     TYDVYCFAEE MEGEVLYATS PEKFTFQEAA NECRRLGARL ATTGQLYLAW QGGMDMCSAG
     WLADRSVRYP ISKARPNCGG NLLGVRTVYL HANQTGYPDP SSRYDAICYT GEDFVDIPEN
     FFGVGGEEDI TIQTVTWPDV ELPLPRNITE GEARGNVILT VKPIFDLSPT APEPEEPFTF
     VPEPEKPFTF ATDVGVTAFP EAENRTGEAT RPWGVPEEST PGPAFTAFTS EDHVVQVTAV
     PGAAEVPGQP RLPGGVVFHY RPGSARYSLT FEEAQQACLR TGAVIASPEQ LQAAYEAGYE
     QCDAGWLQDQ TVRYPIVSPR TPCVGDKDSS PGVRTYGVRP PSETYDVYCY VDKLEGEVFF
     ITRLEQFTFQ EALAFCESHN ATLASTGQLY AAWRQGLDKC YAGWLSDGSL RYPIVTPRPS
     CGGDKPGVRT VYLYPNQTGL PDPLSRHHVF CFRGVSGVPS PGEEEGGTPT PSVVEDWIPT
     QVGPVVPSVP MGEETTAILD FTIEPENQTE WEPAYSPAGT SPLPGIPPTW PPTSTATEES
     TEGPSGTEVP SVSEEPSPSE EPFPWEELST LSPPGPSGTE LPGSGEASGV PEVSGDFTGS
     GEVSGHPDSS GQLSGESASG LPSEDLDSSG LTSAVGSGLA SGDEDRITLS SIPKVEGEGL
     ETSASGVEDL SGLPSGREGL ETSTSGVGDL SGLPSGEGLE VSASGVEDLS GLPSGEGPET
     STSGVGDLSR LPSGEGPEVS ASGVGDLSGL PSGREGLETS TSGVEDLSGL PSGEGPEAST
     SGVGDLSRLP SGEGPEVSAS GVEDLSGLPS GEGLEASASG VGDLSGLPSG EGPEASASGV
     GDLSRLPSGE GPEVSASGVE DLSGLSSGES PEASASGVGD LSGLPSGREG LETSASGVGD
     LSGLPSGEGQ EASASGVEDL SRLPSGEGPE ASASGVGELS GLPSGREGLE TSASGVGDLS
     GLPSGEGPEA FASGVEDLSI LPSGEGPEAS ASGVGDLSGL PSGREGLETS TSGVGDLSGL
     PSGREGLETS TSGVGDLSGL PSGEGPEASA SGIGDISGLP SGREGLETSS SGVEDHPETS
     ASGVEDLSGL PSGVEGHPET SASGVEDLSD LSSGGEGLET SASGAEDLSG FPSGKEDLIG
     SASGALDFGR IPSGTLGSGQ APEASSLPSG FSGEYSGVDF GSGPISGLPD FSGLPSGFPT
     ISLVDTTLVE VITTTSASEL EGRGTIGISG AGETSGLPVS ELDISGAVSG LPSGAELSGQ
     ASGSPDMSGE TSGFFGVSGQ PSGFPDISGG TSGLFEVSGQ PSGFSGETSG VTELSGLYSG
     QPDVSGEASG VPSGSGQPFG MTDLSGETSG VPDISGQPSG LPEFSGTTSG IPDLVSSTMS
     GSGESSGITF VDTSLVEVTP TTFKEKKRLG SVELSGLPSG EVDLSGASGT MDISGQSSGA
     TDSSGLTSHL PKFSGLPSGA AEVSGESSGA EVGSSLPSGT YEGSGNFHPA FPTVFLVDRT
     LVESVTQAPT AQEAGEGPSG ILELSGAHSG APDVSGDHSG SLDLSGMQSG LVEPSGEPSS
     TPYFSGDFSG TMDVTGEPST AMSASGEASG LLEVTLITSE FVEGVTEPTV SQELAQRPPV
     THTPQLFESS GEASASGEIS GATPAFPGSG LEASSVPESS SETSDFPERA VGVSAAPEAS
     GGASGAPDVS EATSTFPEAD VEGASGLGVS GGTSAFPEAP REGSATPEVQ EEPTTSYDVG
     REALGWPSAT PTASGDRIEV SGDLSGHTSG LDVVISTSVP ESEWIQQTQR PAEAHLEIEA
     SSPLHSGEET QTAETATSPT DDASIPTSPS GTDESAPAIP DIDECLSSPC LNGATCVDAI
     DSFTCLCLPS YRGDLCEIDQ ELCEEGWTKF QGHCYRYFPD RESWVDAESR CRAQQSHLSS
     IVTPEEQEFV NNNAQDYQWI GLNDRTIEGD FRWSDGHSLQ FENWRPNQPD NFFVSGEDCV
     VMIWHEKGEW NDVPCNYYLP FTCKKGTVAC GDPPVVEHAR TFGQKKDRYE INSLVRYQCT
     EGFVQRHVPT IRCQPSGHWE KPRITCTDPS TYKRRLQKRS SRAPRRSRPS TAH
//
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