Primary Information |
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| BoMiProt ID | Bomi3767 |
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| Protein Name | Aggrecan core protein/Cartilage-specific proteoglycan core protein |
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| Organism | Bos taurus |
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| Uniprot ID | P13608 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_776406.1 |
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| Aminoacid Length | 2364 |
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| Molecular Weight | 246362 |
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| FASTA Sequence |
Download |
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| Gene Name | ACAN/AGC1 |
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| Gene ID | 280985 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein 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. |
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| Biochemical Properties | The bovine aggrecan sequence, which is a composite of new sequence data and previously published incomplete sequences, is 2327 residues in length. Although there is significant conservation of G1, G2, and G3 globular domains between species, there are differences in the length of the interglobular domain, in the number of KS domain hexapeptide repeats and CS domain repeats, and in alternative splicing within the G3 domain. The bovine aggrecan KS domain contains 24 repeats of a hexapeptide motif. The largely uncharacterized CS-1 domain of bovine aggrecan was found to contain 27 variable repeats of a 21-residue consensus sequence. A notable feature of the bovine CS-1 domain is in the distribution of single Ser-Gly dipeptides, the majority of which are separated by 7 or 8 amino acids, compared to the human, where discrete pairs of Ser-Gly dipeptides are separated by 13 amino acids. The CS-2 domain contains a total of six "homology domains" with 4 complete and 2 partial approximately 100-residue repeats. |
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| PTMs | Disulphide bond, Glycosylation |
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| Linking IDs | Bomi3767 |
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| Bibliography | 1.Hering TM, Kollar J, Huynh TD. Complete coding sequence of bovine aggrecan: comparative structural analysis. Arch Biochem Biophys. 1997 Sep 15;345(2):259-70. doi: 10.1006/abbi.1997.0261. Erratum in: Arch Biochem Biophys 1999 Jul 1;367(1):151. PMID: 9308898. 2.Hering, T. M., Kollar, J., & Huynh, T. D. (1997). Complete coding sequence of bovine aggrecan: comparative structural analysis. Archives of biochemistry and biophysics, 345(2), 259–270. https://doi.org/10.1006/abbi.1997.0261 |
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| Protein 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. |
|---|
| Biochemical Properties | The bovine aggrecan sequence, which is a composite of new sequence data and previously published incomplete sequences, is 2327 residues in length. Although there is significant conservation of G1, G2, and G3 globular domains between species, there are differences in the length of the interglobular domain, in the number of KS domain hexapeptide repeats and CS domain repeats, and in alternative splicing within the G3 domain. The bovine aggrecan KS domain contains 24 repeats of a hexapeptide motif. The largely uncharacterized CS-1 domain of bovine aggrecan was found to contain 27 variable repeats of a 21-residue consensus sequence. A notable feature of the bovine CS-1 domain is in the distribution of single Ser-Gly dipeptides, the majority of which are separated by 7 or 8 amino acids, compared to the human, where discrete pairs of Ser-Gly dipeptides are separated by 13 amino acids. The CS-2 domain contains a total of six "homology domains" with 4 complete and 2 partial approximately 100-residue repeats. |
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| PTMs | Disulphide bond, Glycosylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|P13608|PGCA_BOVIN Aggrecan core protein OS=Bos taurus OX=9913 GN=ACAN PE=1 SV=3
MTTLLLVFVTLRVITAAISVEVSEPDNSLSVSIPEPSPLRVLLGSSLTIPCYFIDPMHPV
TTAPSTAPLAPRIKWSRISKEKEVVLLVATEGRVRVNSAYQDKVTLPNYPAIPSDATLEI
QNMRSN*126DSGILRCEVMHGIEDSQATLEVVVKGIVFHYRAISTRYTLDFDRAQRACLQNSA
IIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKDEFPGVRTYGIRDTN*239E
TYDVYCFAEEMEGEVFYATSPEKFTFQEAANECRRLGARLATTGQLYLAWQGGMDMCSAG
WLADRSVRYPISKARPNCGGNLLGVRTVYLHAN*333QTGYPDPSSRYDAICYTGEDFVDIPES
FFGVGGEEDIT*371IQTVT*376WPDVELPLPRN*387ITEGEARGSVILTAKPDFEVSPTAPEPEEPFTF
VPEVRATAFPEVENRTEEATRPWAFPRESTPGLGAPTAFTSEDLVVQVTLAPGAAEVPGQ
PRLPGGVVFHYRPGSSRYSLTFEEAKQACLRTGAIIASPEQLQAAYEAGYEQCDAGWLQD
QTVRYPIVSPRTPCVGDKDSSPGVRTYGVRPPSETYDVYCYVDRLEGEVFFATRLEQFTF
WEAQEFCESQN*611ATLATTGQLYAAWSRGLDKCYAGWLADGSLRYPIVTPRPACGGDKPGVR
TVYLYPN*667QTGLLDPLSRHHAFCFRGVSAAPSPEEEEGSAPTAGPDVEEWMVTQVGPGVAA
VPIGEETTAIPGFTVEPENKTEWELAYTPAGTLPLPGIPPTWPPTGEATEEHTEGPSATE
VPSASEKPFPSEEPFPPEEPFPSEKPFPPEELFPSEKPFPSEKPFPSEEPFPSEKPFPPE
ELFPSEKPIPSEEPFPSEEPFPSEKPFPPEEPFPSEKPIPSEEPFPSEKPFPSEEPFPSE
EPSTLSAPVPSRTELPSSGEVSGVPEISGDFTGSGEISGHLDFSGQPSGESASGLPSEDL
DSSGLTSTVGSGLPVESGLPSGEEERITWTSAPKVDRLPSGGEGPEVSGVEDISGLPSGG
EVHLEISASGVEDISGLPSGGEVHLEISASGVEDLSRIPSGEGPEISASGVEDISGLPSG
EEGHLEISASGVEDLSGIPSGEGPEVSASGVEDLIGLPSGEGPEVSASGVEDLSRLPSGE
GPEVSASGVEDLSGLPSGEGPEVSVSGVEDLSRLPSGEGPEVSASGVEDLSRLPSGEGPE
ISVSGVEDISILPSGEGPEVSASGVEDLSVLPSGEGHLEISTSGVEDLSVLPSGEGHLET
SSGVEDISRLPSGEGPEVSASGVEDLSVLPSGEDHLEISASGVEDLGVLPSGEDHLEISA
SGVEDISRLPSGEGPEVSASGVEDLSVLPSGEGHLEISASGVEDLSRLPSGGEDHLETSA
SGVGDLSGLPSGREGLEISASGAGDLSGLTSGKEDLTGSASGALDLGRIPSVTLGSGQAP
EASGLPSGFSGEYSGVDLESGPSSGLPDFSGLPSGFPTVSLVDTTLVEVVTATTAGELEG
RGTIDISGAGETSGLPFSELDISGGASGLSSGAELSGQASGSPDISGETSGLFGVSGQPS
GFPDISGETSGLLEVSGQPSGFYGEISGVTELSGLASGQPEISGEASGILSGLGPPFGIT
DLSGEAPGIPDLSGQPSGLPEFSGTASGIPDLVSSAVSGSGESSGITFVDTSLVEVTPTT
FKEEEGLGSVELSGLPSGELGVSGTSGLADVSGLSSGAIDSSGFTSQPPEFSGLPSGVTE
VSGEASGAESGSSLPSGAYDSSGLPSGFPTVSFVDRTLVESVTQAPTAQEAGEGPSGILE
LSGAPSGAPDMSGDHLGSLDQSGLQSGLVEPSGEPASTPYFSGDFSGTTDVSGESSAATS
TSGEASGLPEVTLITSELVEGVTEPTVSQELGQRPPVTYTPQLFESSGEASASGDVPRFP
GSGVEVSSVPESSGETSAYPEAEVGASAAPEASGGASGSPNLSETTSTFHEADLEGTSGL
GVSGSPSAFPEGPTEGLATPEVSGESTTAFDVSVEASGSPSATPLASGDRTDTSGDLSGH
TSGLDIVISTTIPESEWTQQTQRPAEARLEIESSSPVHSGEESQTADTATSPTDASIPAS
AGGTDDSEATTTDIDECLSSPCLNGATCVDAIDSFTCLCLPSYQGDVCEIQKLCEEGWTK
FQGHCYRHFPDRATWVDAESQCRKQQSHLSSIVTPEEQEFVNNNAQDYQWIGLNDKTIEG
DFRWSDGHSLQFENWRPNQPDNFFATGEDCVVMIWHEKGEWNDVPCNYQLPFTCKKGTVA
CGEPPVVEHARIFGQKKDRYEINALVRYQCTEGFIQGHVPTIRCQPSGHWEEPRITCTDP
ATYKRRLQKRSSRPLRRSHPSTAH
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| Predicted Disorder Regions | (692-1981), (2045-2104) |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Linking IDs | |
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| Bibliography | 1.Hering TM, Kollar J, Huynh TD. Complete coding sequence of bovine aggrecan: comparative structural analysis. Arch Biochem Biophys. 1997 Sep 15;345(2):259-70. doi: 10.1006/abbi.1997.0261. Erratum in: Arch Biochem Biophys 1999 Jul 1;367(1):151. PMID: 9308898. 2.Hering, T. M., Kollar, J., & Huynh, T. D. (1997). Complete coding sequence of bovine aggrecan: comparative structural analysis. Archives of biochemistry and biophysics, 345(2), 259–270. https://doi.org/10.1006/abbi.1997.0261 |
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