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Q61282

- PGCA_MOUSE

UniProt

Q61282 - PGCA_MOUSE

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Protein

Aggrecan core protein

Gene

Acan

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1983 – 19831Calcium 1By similarity
Metal bindingi1987 – 19871Calcium 1By similarity
Metal bindingi1987 – 19871Calcium 3By similarity
Metal bindingi2007 – 20071Calcium 2By similarity
Metal bindingi2009 – 20091Calcium 2By similarity
Metal bindingi2010 – 20101Calcium 1By similarity
Metal bindingi2016 – 20161Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi2016 – 20161Calcium 2By similarity
Metal bindingi2017 – 20171Calcium 1By similarity
Metal bindingi2017 – 20171Calcium 3By similarity
Metal bindingi2030 – 20301Calcium 2By similarity
Metal bindingi2031 – 20311Calcium 2By similarity
Metal bindingi2031 – 20311Calcium 2; via carbonyl oxygenBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. hyaluronic acid binding Source: InterPro
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cartilage condensation Source: MGI
  2. chondrocyte development Source: MGI
  3. collagen fibril organization Source: MGI
  4. proteoglycan biosynthetic process Source: MGI
Complete GO annotation...

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Aggrecan core protein
Alternative name(s):
Cartilage-specific proteoglycan core protein
Short name:
CSPCP
Gene namesi
Name:Acan
Synonyms:Agc, Agc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:99602. Acan.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: MGI
  2. extracellular matrix Source: MGI
  3. proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

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).

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 21322113Aggrecan core proteinPRO_0000017507Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 133By similarity
Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi175 ↔ 246By similarity
Disulfide bondi199 ↔ 220By similarity
Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi273 ↔ 348By similarity
Disulfide bondi297 ↔ 318By similarity
Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi371 – 3711O-linked (Xyl...) (keratan sulfate)By similarity
Glycosylationi376 – 3761O-linked (Xyl...) (keratan sulfate)By similarity
Glycosylationi387 – 3871N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi509 ↔ 580By similarity
Disulfide bondi533 ↔ 554By similarity
Disulfide bondi607 ↔ 682By similarity
Glycosylationi611 – 6111N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi631 ↔ 652By similarity
Glycosylationi667 – 6671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1675 – 16751N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1922 ↔ 1933By similarity
Disulfide bondi1950 ↔ 2042By similarity
Disulfide bondi2018 ↔ 2034By similarity
Disulfide bondi2049 ↔ 2092By similarity
Disulfide bondi2078 ↔ 2105By similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan

Proteomic databases

PaxDbiQ61282.
PRIDEiQ61282.

PTM databases

PhosphoSiteiQ61282.

Expressioni

Tissue specificityi

Specifically expressed in cartilage tissues.1 Publication

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiQ61282.
CleanExiMM_ACAN.
GenevestigatoriQ61282.

Interactioni

Subunit structurei

Interacts with COMP (By similarity). Interacts with FBLN1.By similarity1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000032835.

Structurei

3D structure databases

ProteinModelPortaliQ61282.
SMRiQ61282. Positions 1920-2045.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 147114Ig-like V-typeAdd
BLAST
Domaini153 – 24896Link 1PROSITE-ProRule annotationAdd
BLAST
Domaini254 – 35097Link 2PROSITE-ProRule annotationAdd
BLAST
Domaini487 – 58296Link 3PROSITE-ProRule annotationAdd
BLAST
Domaini588 – 68497Link 4PROSITE-ProRule annotationAdd
BLAST
Domaini1918 – 2044127C-type lectinPROSITE-ProRule annotationAdd
BLAST
Domaini2047 – 210761SushiPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 14093G1-AAdd
BLAST
Regioni152 – 24796G1-BAdd
BLAST
Regioni253 – 34997G1-B'Add
BLAST
Regioni486 – 58095G2-BAdd
BLAST
Regioni587 – 68296G2-B'Add
BLAST
Regioni685 – 803119KSAdd
BLAST
Regioni805 – 1231427CS-1Add
BLAST
Regioni1232 – 1917686CS-2Add
BLAST
Regioni1917 – 2132216G3Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1171 – 11733Cell attachment siteSequence Analysis

Domaini

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.

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation
Contains 4 Link domains.PROSITE-ProRule annotation
Contains 1 Sushi (CCP/SCR) domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000119025.
HOGENOMiHOG000168421.
HOVERGENiHBG007982.
InParanoidiQ61282.
KOiK06792.
OMAiCESHNAT.
OrthoDBiEOG7ZWD1D.
TreeFamiTF332134.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.10.100.10. 5 hits.
InterProiIPR001304. 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]
PfamiPF00059. Lectin_C. 1 hit.
PF00084. Sushi. 1 hit.
PF07686. V-set. 1 hit.
PF00193. Xlink. 4 hits.
[Graphical view]
PRINTSiPR01265. LINKMODULE.
SMARTiSM00032. CCP. 1 hit.
SM00034. CLECT. 1 hit.
SM00406. IGv. 1 hit.
SM00445. LINK. 4 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 5 hits.
SSF57535. SSF57535. 1 hit.
PROSITEiPS00615. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61282-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTLLLVFVT LRVIAAVISE EVPDHDNSLS VSIPQPSPLK VLLGSSLTIP
60 70 80 90 100
CYFIDPMHPV TTAPSTAPLT PRIKWSRVSK EKEVVLLVAT EGQVRVNSIY
110 120 130 140 150
QDKVSLPNYP AIPSDATLEI QNLRSNDSGI YRCEVMHGIE DSEATLEVIV
160 170 180 190 200
KGIVFHYRAI STRYTLDFDR AQRACLQNSA IIATPEQLQA AYEDGFHQCD
210 220 230 240 250
AGWLADQTVR YPIHTPREGC YGDKDEFPGV RTYGIRDTNE TYDVYCFAEE
260 270 280 290 300
MEGEVFYATS PEKFTFQEAA NECRRLGARL ATTGQLYLAW QGGMDMCSAG
310 320 330 340 350
WLADRSVRYP ISKARPNCGG NLLGVRTVYL HANQTGYPDP SSRYDAICYT
360 370 380 390 400
GEDFVDIPEN FFGVGGEDDI TIQTVTWPDL ELPLPRNVTE GEALGSVILT
410 420 430 440 450
AKPIFDLSPT ISEPGEALTL APEVGSTAFP EAEERTGEAT RPWGFPAEVT
460 470 480 490 500
RGPDSATAFA SEDLVVRVTI SPGAAEVPGQ PRLPGGVVFH YRPGSTRYSL
510 520 530 540 550
TFEEAQQACM HTGAVIASPE QLQAAYEAGY EQCDAGWLQD QTVRYPIVSP
560 570 580 590 600
RTPCVGDKDS SPGVRTYGVR PSSETYDVYC YVDKLEGEVF FATRLEQFTF
610 620 630 640 650
QEARAFCAAQ NATLASTGQL YAAWSQGLDK CYAGWLADGT LRYPIITPRP
660 670 680 690 700
ACGGDKPGVR TVYLYPNQTG LPDPLSKHHA FCFRGVSVAP SPGEEGGSTP
710 720 730 740 750
TSPSDIEDWI VTQVGPGVDA VPLEPKTTEV PYFTTEPRKQ TEWEPAYTPV
760 770 780 790 800
GTSPQPGIPP TWLPTLPAAE EHTESPSASE EPSASAVPST SEEPYTSSFA
810 820 830 840 850
VPSMTELPGS GEASGAPDLS GDFTGSGDAS GRLDSSGQPS GGIESGLPSG
860 870 880 890 900
DLDSSGLSPT VSSGLPVESG SASGDGEVPW SHTPTVGRLP SGGESPEGSA
910 920 930 940 950
SASGTGDLSG LPSGGEITET STSGAEETSG LPSGGDGLET STSGVDDVSG
960 970 980 990 1000
IPTGREGLET SASGVEDLSG LPSGEEGSET STSGIEDISV LPTGGESLET
1010 1020 1030 1040 1050
SASGVGDLSG LPSGGESLET SASGAEDVTQ LPTERGGLET SASGVEDITV
1060 1070 1080 1090 1100
LPTGRESLET SASGVEDVSG LPSGREGLET SASGIEDISV FPTEAEGLDT
1110 1120 1130 1140 1150
SASGGYVSGI PSGGDGTETS ASGVEDVSGL PSGGEGLETS ASGVEDLGPS
1160 1170 1180 1190 1200
TRDSLETSAS GVDVTGFPSG RGDPETSVSG VGDDFSGLPS GKEGLETSAS
1210 1220 1230 1240 1250
GAEDLSGLPS GKEDLVGSAS GALDFGKLPP GTLGSGQTPE VNGFPSGFSG
1260 1270 1280 1290 1300
EYSGADIGSG PSSGLPDFSG LPSGFPTVSL VDSTLVEVIT ATTSSELEGR
1310 1320 1330 1340 1350
GTIGISGSGE VSGLPLGELD SSADISGLPS GTELSGQASG SPDSSGETSG
1360 1370 1380 1390 1400
FFDVSGQPFG SSGVSEETSG IPEISGQPSG TPDTTATSGV TELNELSSGQ
1410 1420 1430 1440 1450
PDVSGDGSGI LFGSGQSSGI TSVSGETSGI SDLSGQPSGF PVFSGTATRT
1460 1470 1480 1490 1500
PDLASGTISG SGESSGITFV DTSFVEVTPT TFREEEGLGS VELSGFPSGE
1510 1520 1530 1540 1550
TELSGTSGTV DVSEQSSGAI DSSGLTSPTP EFSGLPSGVA EVSGEFSGVE
1560 1570 1580 1590 1600
TGSSLPSGAF DGSGLVSGFP TVSLVDRTLV ESITQAPTAQ EAGEGPSGIL
1610 1620 1630 1640 1650
EFSGAHSGTP DISGELSGSL DLSTLQSGQM ETSTETPSSP YFSGDFSSTT
1660 1670 1680 1690 1700
DVSGESIAAT TGSGESSGLP EVTLNTSELV EGVTEPTVSQ ELGHGPSMTY
1710 1720 1730 1740 1750
TPRLFEASGD ASASGDLGGA VTNFPGSGIE ASVPEASSDL SAYPEAGVGV
1760 1770 1780 1790 1800
SAAPEASSKL SEFPDLHGIT SAFHETDLEM TTPSTEVNSN PWTFQEGTRE
1810 1820 1830 1840 1850
GSAAPEVSGE SSTTSDIDTG TSGVPSATPM ASGDRTEISG EWSDHTSEVN
1860 1870 1880 1890 1900
VAISSTITES EWAQPTRYPT ETLQEIESPN PSYSGEETQT AETTMSLTDA
1910 1920 1930 1940 1950
PTLSSSEGSG ETESTVADQE QCEEGWTKFQ GHCYRHFHDR ETWVDAERRC
1960 1970 1980 1990 2000
REQQSHLSSI VTPEEQEFVN KNAQDYQWIG LNDRTIEGDF RWSDGHSLQF
2010 2020 2030 2040 2050
EKWRPNQPDN FFATGEDCVV MIWHERGEWN DVPCNYQLPF TCKKGTVACG
2060 2070 2080 2090 2100
DPPVVEHART LGQKKDRYEI SSLVRYQCTE GFVQRHVPTI RCQPSGHWEE
2110 2120 2130
PRITCTDPNT YKHRLQKRSM RPTRRSRPSM AH
Length:2,132
Mass (Da):221,941
Last modified:July 27, 2011 - v2
Checksum:i17298662D95E1921
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti482 – 4821R → H in AAC37670. (PubMed:7806222)Curated
Sequence conflicti515 – 5151V → I in AAC37670. (PubMed:7806222)Curated
Sequence conflicti568 – 5681G → R in AAC37670. (PubMed:7806222)Curated
Sequence conflicti696 – 6961G → E in AAC37670. (PubMed:7806222)Curated
Sequence conflicti1701 – 17022TP → IS in AAC37670. (PubMed:7806222)Curated
Sequence conflicti1705 – 17051F → S in AAC37670. (PubMed:7806222)Curated
Sequence conflicti1729 – 17291I → V in AAC37670. (PubMed:7806222)Curated
Sequence conflicti1938 – 19381H → P in AAC37670. (PubMed:7806222)Curated
Sequence conflicti2119 – 21191S → T in AAC37670. (PubMed:7806222)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07049 mRNA. Translation: AAC37670.1.
AC110520 Genomic DNA. No translation available.
S73722, S73721 Genomic DNA. Translation: AAB32160.1.
CCDSiCCDS21377.1.
PIRiA55182.
RefSeqiNP_031450.2. NM_007424.2.
UniGeneiMm.358571.

Genome annotation databases

EnsembliENSMUST00000032835; ENSMUSP00000032835; ENSMUSG00000030607.
GeneIDi11595.
KEGGimmu:11595.
UCSCiuc009hxw.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Aggrecan

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07049 mRNA. Translation: AAC37670.1 .
AC110520 Genomic DNA. No translation available.
S73722 , S73721 Genomic DNA. Translation: AAB32160.1 .
CCDSi CCDS21377.1.
PIRi A55182.
RefSeqi NP_031450.2. NM_007424.2.
UniGenei Mm.358571.

3D structure databases

ProteinModelPortali Q61282.
SMRi Q61282. Positions 1920-2045.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000032835.

PTM databases

PhosphoSitei Q61282.

Proteomic databases

PaxDbi Q61282.
PRIDEi Q61282.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000032835 ; ENSMUSP00000032835 ; ENSMUSG00000030607 .
GeneIDi 11595.
KEGGi mmu:11595.
UCSCi uc009hxw.1. mouse.

Organism-specific databases

CTDi 176.
MGIi MGI:99602. Acan.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000119025.
HOGENOMi HOG000168421.
HOVERGENi HBG007982.
InParanoidi Q61282.
KOi K06792.
OMAi CESHNAT.
OrthoDBi EOG7ZWD1D.
TreeFami TF332134.

Miscellaneous databases

NextBioi 279108.
PROi Q61282.
SOURCEi Search...

Gene expression databases

Bgeei Q61282.
CleanExi MM_ACAN.
Genevestigatori Q61282.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
3.10.100.10. 5 hits.
InterProi IPR001304. 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 ]
Pfami PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 1 hit.
PF07686. V-set. 1 hit.
PF00193. Xlink. 4 hits.
[Graphical view ]
PRINTSi PR01265. LINKMODULE.
SMARTi SM00032. CCP. 1 hit.
SM00034. CLECT. 1 hit.
SM00406. IGv. 1 hit.
SM00445. LINK. 4 hits.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 5 hits.
SSF57535. SSF57535. 1 hit.
PROSITEi PS00615. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiPGCA_MOUSE
AccessioniPrimary (citable) accession number: Q61282
Secondary accession number(s): E9QLS9, Q64021
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3