Search by BoMiProt ID - Bomi3767


Primary Information

BoMiProt ID Bomi3767
Protein Name Aggrecan core protein/Cartilage-specific proteoglycan core protein
Organism Bos taurus
Uniprot IdP13608
Milk FractionWhey
Ref Sequence Id NP_776406.1
Aminoacid Length 2364
Molecular Weight 246362
Fasta Sequence https://www.uniprot.org/uniprot/P13608.fasta
Gene Name ACAN/AGC1
Gene Id 280985
Protein Existence Status reviewed

Secondary Information

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.
PTMs Disulphide bond, Glycosylation
Linking IDs Bomi3767
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
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.
PTMs Disulphide bond, Glycosylation
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
Predicted Disorder Regions (692-1981), (2045-2104)
DisProt Annotation
TM Helix Prediction No TM helices
Linking IDs
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