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Q61282 (PGCA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aggrecan core protein
Alternative name(s):
Cartilage-specific proteoglycan core protein
Short name=CSPCP
Gene names
Name:Acan
Synonyms:Agc, Agc1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length2132 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 structure

Interacts with COMP By similarity. Interacts with FBLN1. Ref.4

Subcellular location

Secreted › extracellular space › extracellular matrix By similarity.

Tissue specificity

Specifically expressed in cartilage tissues. Ref.5

Developmental stage

Expressed in chondrocytes throughout the developing skeleton in a pattern very similar but not identical to those of type II and IX collagen. In the newborn mouse skeleton it is expressed essentially in a mutually exclusive manner with tenascin, which is expressed osteoblasts, periosteal and perichondrial cells, and in cells at articular surfaces. Ref.5

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.

Post-translational modification

Contains mostly chondroitin sulfate, but also keratan sulfate chains, N-linked and O-linked oligosaccharides.

Involvement in disease

Defects in Acan are the cause of cartilage matrix deficiency (CMD). CMD is an autosomal recessive syndrome characterized by cleft palate, short limbs, tail and snout. Mutation in strain CMD causes absence of aggrecan by truncation of the protein (mutation in the G1 domain).

Sequence similarities

Belongs to the aggrecan/versican proteoglycan family.

Contains 1 C-type lectin domain.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Contains 4 Link domains.

Contains 1 Sushi (CCP/SCR) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 21322113Aggrecan core protein
PRO_0000017507

Regions

Domain34 – 147114Ig-like V-type
Domain153 – 24896Link 1
Domain254 – 35097Link 2
Domain487 – 58296Link 3
Domain588 – 68497Link 4
Domain1918 – 2044127C-type lectin
Domain2047 – 210761Sushi
Region48 – 14093G1-A
Region152 – 24796G1-B
Region253 – 34997G1-B'
Region486 – 58095G2-B
Region587 – 68296G2-B'
Region685 – 803119KS
Region805 – 1231427CS-1
Region1232 – 1917686CS-2
Region1917 – 2132216G3
Motif1171 – 11733Cell attachment site Potential

Sites

Metal binding19831Calcium 1 By similarity
Metal binding19871Calcium 1 By similarity
Metal binding19871Calcium 3 By similarity
Metal binding20071Calcium 2 By similarity
Metal binding20091Calcium 2 By similarity
Metal binding20101Calcium 1 By similarity
Metal binding20161Calcium 1; via carbonyl oxygen By similarity
Metal binding20161Calcium 2 By similarity
Metal binding20171Calcium 1 By similarity
Metal binding20171Calcium 3 By similarity
Metal binding20301Calcium 2 By similarity
Metal binding20311Calcium 2 By similarity
Metal binding20311Calcium 2; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation1261N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential
Glycosylation3331N-linked (GlcNAc...) Potential
Glycosylation3711O-linked (Xyl...) (keratan sulfate) By similarity
Glycosylation3761O-linked (Xyl...) (keratan sulfate) By similarity
Glycosylation3871N-linked (GlcNAc...) Potential
Glycosylation6111N-linked (GlcNAc...) Potential
Glycosylation6671N-linked (GlcNAc...) Potential
Glycosylation16751N-linked (GlcNAc...) Potential
Disulfide bond51 ↔ 133 By similarity
Disulfide bond175 ↔ 246 By similarity
Disulfide bond199 ↔ 220 By similarity
Disulfide bond273 ↔ 348 By similarity
Disulfide bond297 ↔ 318 By similarity
Disulfide bond509 ↔ 580 By similarity
Disulfide bond533 ↔ 554 By similarity
Disulfide bond607 ↔ 682 By similarity
Disulfide bond631 ↔ 652 By similarity
Disulfide bond1922 ↔ 1933 By similarity
Disulfide bond1950 ↔ 2042 By similarity
Disulfide bond2018 ↔ 2034 By similarity
Disulfide bond2049 ↔ 2092 By similarity
Disulfide bond2078 ↔ 2105 By similarity

Experimental info

Sequence conflict4821R → H in AAC37670. Ref.1
Sequence conflict5151V → I in AAC37670. Ref.1
Sequence conflict5681G → R in AAC37670. Ref.1
Sequence conflict6961G → E in AAC37670. Ref.1
Sequence conflict1701 – 17022TP → IS in AAC37670. Ref.1
Sequence conflict17051F → S in AAC37670. Ref.1
Sequence conflict17291I → V in AAC37670. Ref.1
Sequence conflict19381H → P in AAC37670. Ref.1
Sequence conflict21191S → T in AAC37670. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q61282 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 17298662D95E1921

FASTA2,132221,941
        10         20         30         40         50         60 
MTTLLLVFVT LRVIAAVISE EVPDHDNSLS VSIPQPSPLK VLLGSSLTIP CYFIDPMHPV 

        70         80         90        100        110        120 
TTAPSTAPLT PRIKWSRVSK EKEVVLLVAT EGQVRVNSIY QDKVSLPNYP AIPSDATLEI 

       130        140        150        160        170        180 
QNLRSNDSGI YRCEVMHGIE DSEATLEVIV KGIVFHYRAI STRYTLDFDR AQRACLQNSA 

       190        200        210        220        230        240 
IIATPEQLQA AYEDGFHQCD AGWLADQTVR YPIHTPREGC YGDKDEFPGV RTYGIRDTNE 

       250        260        270        280        290        300 
TYDVYCFAEE MEGEVFYATS PEKFTFQEAA NECRRLGARL ATTGQLYLAW QGGMDMCSAG 

       310        320        330        340        350        360 
WLADRSVRYP ISKARPNCGG NLLGVRTVYL HANQTGYPDP SSRYDAICYT GEDFVDIPEN 

       370        380        390        400        410        420 
FFGVGGEDDI TIQTVTWPDL ELPLPRNVTE GEALGSVILT AKPIFDLSPT ISEPGEALTL 

       430        440        450        460        470        480 
APEVGSTAFP EAEERTGEAT RPWGFPAEVT RGPDSATAFA SEDLVVRVTI SPGAAEVPGQ 

       490        500        510        520        530        540 
PRLPGGVVFH YRPGSTRYSL TFEEAQQACM HTGAVIASPE QLQAAYEAGY EQCDAGWLQD 

       550        560        570        580        590        600 
QTVRYPIVSP RTPCVGDKDS SPGVRTYGVR PSSETYDVYC YVDKLEGEVF FATRLEQFTF 

       610        620        630        640        650        660 
QEARAFCAAQ NATLASTGQL YAAWSQGLDK CYAGWLADGT LRYPIITPRP ACGGDKPGVR 

       670        680        690        700        710        720 
TVYLYPNQTG LPDPLSKHHA FCFRGVSVAP SPGEEGGSTP TSPSDIEDWI VTQVGPGVDA 

       730        740        750        760        770        780 
VPLEPKTTEV PYFTTEPRKQ TEWEPAYTPV GTSPQPGIPP TWLPTLPAAE EHTESPSASE 

       790        800        810        820        830        840 
EPSASAVPST SEEPYTSSFA VPSMTELPGS GEASGAPDLS GDFTGSGDAS GRLDSSGQPS 

       850        860        870        880        890        900 
GGIESGLPSG DLDSSGLSPT VSSGLPVESG SASGDGEVPW SHTPTVGRLP SGGESPEGSA 

       910        920        930        940        950        960 
SASGTGDLSG LPSGGEITET STSGAEETSG LPSGGDGLET STSGVDDVSG IPTGREGLET 

       970        980        990       1000       1010       1020 
SASGVEDLSG LPSGEEGSET STSGIEDISV LPTGGESLET SASGVGDLSG LPSGGESLET 

      1030       1040       1050       1060       1070       1080 
SASGAEDVTQ LPTERGGLET SASGVEDITV LPTGRESLET SASGVEDVSG LPSGREGLET 

      1090       1100       1110       1120       1130       1140 
SASGIEDISV FPTEAEGLDT SASGGYVSGI PSGGDGTETS ASGVEDVSGL PSGGEGLETS 

      1150       1160       1170       1180       1190       1200 
ASGVEDLGPS TRDSLETSAS GVDVTGFPSG RGDPETSVSG VGDDFSGLPS GKEGLETSAS 

      1210       1220       1230       1240       1250       1260 
GAEDLSGLPS GKEDLVGSAS GALDFGKLPP GTLGSGQTPE VNGFPSGFSG EYSGADIGSG 

      1270       1280       1290       1300       1310       1320 
PSSGLPDFSG LPSGFPTVSL VDSTLVEVIT ATTSSELEGR GTIGISGSGE VSGLPLGELD 

      1330       1340       1350       1360       1370       1380 
SSADISGLPS GTELSGQASG SPDSSGETSG FFDVSGQPFG SSGVSEETSG IPEISGQPSG 

      1390       1400       1410       1420       1430       1440 
TPDTTATSGV TELNELSSGQ PDVSGDGSGI LFGSGQSSGI TSVSGETSGI SDLSGQPSGF 

      1450       1460       1470       1480       1490       1500 
PVFSGTATRT PDLASGTISG SGESSGITFV DTSFVEVTPT TFREEEGLGS VELSGFPSGE 

      1510       1520       1530       1540       1550       1560 
TELSGTSGTV DVSEQSSGAI DSSGLTSPTP EFSGLPSGVA EVSGEFSGVE TGSSLPSGAF 

      1570       1580       1590       1600       1610       1620 
DGSGLVSGFP TVSLVDRTLV ESITQAPTAQ EAGEGPSGIL EFSGAHSGTP DISGELSGSL 

      1630       1640       1650       1660       1670       1680 
DLSTLQSGQM ETSTETPSSP YFSGDFSSTT DVSGESIAAT TGSGESSGLP EVTLNTSELV 

      1690       1700       1710       1720       1730       1740 
EGVTEPTVSQ ELGHGPSMTY TPRLFEASGD ASASGDLGGA VTNFPGSGIE ASVPEASSDL 

      1750       1760       1770       1780       1790       1800 
SAYPEAGVGV SAAPEASSKL SEFPDLHGIT SAFHETDLEM TTPSTEVNSN PWTFQEGTRE 

      1810       1820       1830       1840       1850       1860 
GSAAPEVSGE SSTTSDIDTG TSGVPSATPM ASGDRTEISG EWSDHTSEVN VAISSTITES 

      1870       1880       1890       1900       1910       1920 
EWAQPTRYPT ETLQEIESPN PSYSGEETQT AETTMSLTDA PTLSSSEGSG ETESTVADQE 

      1930       1940       1950       1960       1970       1980 
QCEEGWTKFQ GHCYRHFHDR ETWVDAERRC REQQSHLSSI VTPEEQEFVN KNAQDYQWIG 

      1990       2000       2010       2020       2030       2040 
LNDRTIEGDF RWSDGHSLQF EKWRPNQPDN FFATGEDCVV MIWHERGEWN DVPCNYQLPF 

      2050       2060       2070       2080       2090       2100 
TCKKGTVACG DPPVVEHART LGQKKDRYEI SSLVRYQCTE GFVQRHVPTI RCQPSGHWEE 

      2110       2120       2130 
PRITCTDPNT YKHRLQKRSM RPTRRSRPSM AH

« Hide

References

« Hide 'large scale' references
[1]"Complete coding sequence, deduced primary structure, chromosomal localization, and structural analysis of murine aggrecan."
Walcz E., Deak F., Erhardt P., Coulter S.N., Fueloep C., Horvath P., Doege K.J., Glant T.T.
Genomics 22:364-371(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Cartilage.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"Mouse cartilage matrix deficiency (cmd) caused by a 7 bp deletion in the aggrecan gene."
Watanabe H., Kimata K., Line S., Strong D., Gao L.-Y., Kozak C.A., Yamada Y.
Nat. Genet. 7:154-157(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 211-326.
Strain: 129/Sv.
[4]"Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versican."
Aspberg A., Adam S., Kostka G., Timpl R., Heinegaard D.
J. Biol. Chem. 274:20444-20449(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FBLN1.
[5]"Analysis of aggrecan and tenascin gene expression in mouse skeletal tissues by northern and in situ hybridization using species specific cDNA probes."
Glumoff V., Savontaus M., Vehanen J., Vuorio E.
Biochim. Biophys. Acta 1219:613-622(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L07049 mRNA. Translation: AAC37670.1.
AC110520 Genomic DNA. No translation available.
S73722, S73721 Genomic DNA. Translation: AAB32160.1.
IPIIPI00119035.
PIRA55182.
RefSeqNP_031450.2. NM_007424.2.
UniGeneMm.358571.

3D structure databases

ProteinModelPortalQ61282.
SMRQ61282. Positions 1920-2045.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000032835.

PTM databases

PhosphoSiteQ61282.

Proteomic databases

PaxDbQ61282.
PRIDEQ61282.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032835; ENSMUSP00000032835; ENSMUSG00000030607.
GeneID11595.
KEGGmmu:11595.
UCSCuc009hxw.1. mouse.

Organism-specific databases

CTD176.
MGIMGI:99602. Acan.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00670000097775.
HOGENOMHOG000168421.
HOVERGENHBG007982.
InParanoidQ61282.
KOK06792.
OMAENFFGVG.
OrthoDBEOG43BMN5.

Gene expression databases

BgeeQ61282.
CleanExMM_ACAN.
GenevestigatorQ61282.
GermOnlineENSMUSG00000030607. Mus musculus.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.10.100.10. 5 hits.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR013106. Ig_V-set.
IPR003596. Ig_V-set_subgr.
IPR000538. Link.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF00059. Lectin_C. 1 hit.
PF00084. Sushi. 1 hit.
PF07686. V-set. 1 hit.
PF00193. Xlink. 4 hits.
[Graphical view]
PRINTSPR01265. LINKMODULE.
SMARTSM00032. CCP. 1 hit.
SM00034. CLECT. 1 hit.
SM00406. IGv. 1 hit.
SM00445. LINK. 4 hits.
[Graphical view]
SUPFAMSSF56436. C-type_lectin_fold. 5 hits.
SSF57535. Complement_control_module. 1 hit.
PROSITEPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
PS01241. LINK_1. 4 hits.
PS50963. LINK_2. 4 hits.
PS50923. SUSHI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio279108.
SOURCESearch...

Entry information

Entry namePGCA_MOUSE
AccessionPrimary (citable) accession number: Q61282
Secondary accession number(s): E9QLS9, Q64021
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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