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Protein

Aggrecan core protein

Gene

Acan

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi1975Calcium 11
Metal bindingi1979Calcium 11
Metal bindingi1979Calcium 31
Metal bindingi1999Calcium 21
Metal bindingi2001Calcium 21
Metal bindingi2002Calcium 11
Metal bindingi2008Calcium 1; via carbonyl oxygen1
Metal bindingi2008Calcium 21
Metal bindingi2009Calcium 11
Metal bindingi2009Calcium 31
Metal bindingi2022Calcium 21
Metal bindingi2023Calcium 21
Metal bindingi2023Calcium 2; via carbonyl oxygen1

GO - Molecular functioni

GO - Biological processi

  • cell adhesion Source: GO_Central
  • cellular response to growth factor stimulus Source: RGD
  • central nervous system development Source: RGD
  • chondroblast differentiation Source: RGD
  • multicellular organism aging Source: RGD
  • negative regulation of cell migration Source: RGD
  • ossification Source: RGD
  • response to acidic pH Source: RGD
  • response to drug Source: RGD
  • response to glucose Source: RGD
  • response to gravity Source: RGD
  • response to mechanical stimulus Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to radiation Source: RGD
  • spinal cord development Source: RGD
Complete GO annotation...

Keywords - Ligandi

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi68358. Acan.

Subcellular locationi

GO - Cellular componenti

  • perineuronal net Source: RGD
  • proteinaceous extracellular matrix Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000001750820 – 2124Aggrecan core proteinAdd BLAST2105

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi51 ↔ 133By similarity
Glycosylationi126N-linked (GlcNAc...)1 Publication1
Disulfide bondi175 ↔ 246By similarity
Disulfide bondi199 ↔ 220By similarity
Glycosylationi239N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi273 ↔ 348By similarity
Disulfide bondi297 ↔ 318By similarity
Glycosylationi333N-linked (GlcNAc...)1 Publication1
Glycosylationi371O-linked (Xyl...) (keratan sulfate)By similarity1
Glycosylationi376O-linked (Xyl...) (keratan sulfate)By similarity1
Glycosylationi387N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi509 ↔ 580By similarity
Disulfide bondi533 ↔ 554By similarity
Disulfide bondi607 ↔ 682By similarity
Glycosylationi611N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi631 ↔ 652By similarity
Glycosylationi667N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1842N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1914 ↔ 1925By similarity
Disulfide bondi1942 ↔ 20341 Publication
Disulfide bondi2010 ↔ 20261 Publication
Disulfide bondi2041 ↔ 2084By similarity
Disulfide bondi2070 ↔ 2097By similarity

Post-translational modificationi

Contains mostly chondroitin sulfate, but also keratan sulfate chains, N-linked and O-linked oligosaccharides.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan

Proteomic databases

PaxDbiP07897.
PRIDEiP07897.

Interactioni

Subunit structurei

Interacts with FBLN1 and COMP.By similarity

Protein-protein interaction databases

IntActiP07897. 1 interactor.
STRINGi10116.ENSRNOP00000042691.

Structurei

Secondary structure

12124
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1919 – 1921Combined sources3
Beta strandi1924 – 1933Combined sources10
Helixi1935 – 1944Combined sources10
Helixi1955 – 1965Combined sources11
Beta strandi1969 – 1974Combined sources6
Beta strandi1976 – 1978Combined sources3
Turni2005 – 2007Combined sources3
Beta strandi2008 – 2013Combined sources6
Turni2015 – 2019Combined sources5
Beta strandi2021 – 2025Combined sources5
Beta strandi2030 – 2036Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TDQX-ray2.60B1909-2037[»]
ProteinModelPortaliP07897.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07897.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 147Ig-like V-typeAdd BLAST114
Domaini153 – 248Link 1PROSITE-ProRule annotationAdd BLAST96
Domaini254 – 350Link 2PROSITE-ProRule annotationAdd BLAST97
Domaini487 – 582Link 3PROSITE-ProRule annotationAdd BLAST96
Domaini588 – 684Link 4PROSITE-ProRule annotationAdd BLAST97
Domaini1910 – 2036C-type lectinPROSITE-ProRule annotationAdd BLAST127
Domaini2039 – 2099SushiPROSITE-ProRule annotationAdd BLAST61

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni48 – 140G1-AAdd BLAST93
Regioni152 – 247G1-BAdd BLAST96
Regioni253 – 349G1-B'Add BLAST97
Regioni486 – 580G2-BAdd BLAST95
Regioni587 – 682G2-B'Add BLAST96
Regioni685 – 798KSAdd BLAST114
Regioni801 – 1226CS-1Add BLAST426
Regioni1227 – 1909CS-2Add BLAST683
Regioni1910 – 2124G3Add BLAST215

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

eggNOGiENOG410IJP2. Eukaryota.
ENOG410XRES. LUCA.
HOGENOMiHOG000168421.
HOVERGENiHBG007982.
InParanoidiP07897.
KOiK06792.

Family and domain databases

CDDicd00033. CCP. 1 hit.
Gene3Di2.60.40.10. 1 hit.
3.10.100.10. 5 hits.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR016187. CTDL_fold.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR000538. Link_dom.
IPR000436. Sushi_SCR_CCP_dom.
[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.
SM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
SM00445. LINK. 4 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF56436. 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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P07897-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTTLLLVFVT LRVIAAVISE EVPDHDNSLS VSIPQPSPLK ALLGTSLTIP
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 NECRTVGARL ATTGQLYLAW QGGMDMCSAG
310 320 330 340 350
WLADRSVRYP ISKARPNCGG NLLGVRTVYL HANQTGYPDP SSRYDAICYT
360 370 380 390 400
GEDFVDIPEN FFGVGGEEDI TIQTVTWPDL ELPLPRNITE GEARGNVILT
410 420 430 440 450
AKPIFDMSPT VSEPGEALTL APEVGTTVFP EAGERTEKTT RPWGFPEEAT
460 470 480 490 500
RGPDSATAFA SEDLVVRVTI SPGAVEVPGQ PRLPGGVVFH YRPGSTRYSL
510 520 530 540 550
TFEEAQQACI RTGAAIASPE QLQAAYEAGY EQCDAGWLQD QTVRYPIVSP
560 570 580 590 600
RTPCVGDKDS SPGVRTYGVR PSSETYDVYC YVDKLEGEVF FATQMEQFTF
610 620 630 640 650
QEAQAFCAAQ NATLASTGQL YAAWSQGLDK CYAGWLADGT LRYPIVNPRP
660 670 680 690 700
ACGGDKPGVR TVYLYPNQTG LPDPLSKHHA FCFRGVSVVP SPGGTPTSPS
710 720 730 740 750
DIEDWIVTRV EPGVDAVPLE PETTEVPYFT TEPEKQTEWE PAYTPVGTSP
760 770 780 790 800
LPGIPPTWLP TVPAAEEHTE SPSASQEPSA SQVPSTSEEP YTPSLAVPSG
810 820 830 840 850
TELPSSGDTS GAPDLSGDFT GSTDTSGRLD SSGEPSGGSE SGLPSGDLDS
860 870 880 890 900
SGLGPTVSSG LPVESGSASG DGEIPWSSTP TVDRLPSGGE SLEGSASASG
910 920 930 940 950
TGDLSGLPSG GEITETSASG TEEISGLPSG GDDLETSTSG IDGASVLPTG
960 970 980 990 1000
RGGLETSASG VEDLSGLPSG EEGSETSTSG IEDISVLPTG ESPETSASGV
1010 1020 1030 1040 1050
GDLSGLPSGG ESLETSASGV EDVTQLPTER GGLETSASGI EDITVLPTGR
1060 1070 1080 1090 1100
ENLETSASGV EDVSGLPSGK EGLETSASGI EDISVFPTEA EGLETSASGG
1110 1120 1130 1140 1150
YVSGIPSGED GTETSTSGVE GVSGLPSGGE GLETSASGVE DLGLPTRDSL
1160 1170 1180 1190 1200
ETSASGVDVT GYPSGREDTE TSVPGVGDDL SGLPSGQEGL ETSASGAEDL
1210 1220 1230 1240 1250
GGLPSGKEDL VGSASGALDF GKLPSGTLGS GQTPEASGLP SGFSGEYSGV
1260 1270 1280 1290 1300
DIGSGPSSGL PDFSGLPSGF PTVSLVDSTL VEVITATTAS ELEGRGTISV
1310 1320 1330 1340 1350
SGSGEESGPP LSELDSSADI SGLPSGTELS GQTSGSLDVS GETSGFFDVS
1360 1370 1380 1390 1400
GQPFGSSGTG EGTSGIPEVS GQAVRSPDTT EISELSGLSS GQPDVSGEGS
1410 1420 1430 1440 1450
GILFGSGQSS GITSVSGETS GISDLSGQPS GFPVLSGTTP GTPDLASGAM
1460 1470 1480 1490 1500
SGSGDSSGIT FVDTSLIEVT PTTFREEEGL GSVELSGLPS GETDLSGTSG
1510 1520 1530 1540 1550
MVDVSGQSSG AIDSSGLISP TPEFSGLPSG VAEVSGEVSG VETGSSLSSG
1560 1570 1580 1590 1600
AFDGSGLVSG FPTVSLVDRT LVESITLAPT AQEAGEGPSS ILEFSGAHSG
1610 1620 1630 1640 1650
TPDISGDLSG SLDQSTWQPG WTEASTEPPS SPYFSGDFSS TTDASGESIT
1660 1670 1680 1690 1700
APTGSGETSG LPEVTLITSE LVEGVTEPTV SQELGHGPSM TYTPRLFEAS
1710 1720 1730 1740 1750
GEASASGDLG GPVTIFPGSG VEASVPEGSS DPSAYPEAGV GVSAAPEASS
1760 1770 1780 1790 1800
QLSEFPDLHG ITSASRETDL EMTTPGTEVS SNPWTFQEGT REGSAAPEVS
1810 1820 1830 1840 1850
GESSTTSDID AGTSGVPFAT PMTSGDRTEI SGEWSDHTSE VNVTVSTTVP
1860 1870 1880 1890 1900
ESRWAQSTQH PTETLQEIGS PNPSYSGEET QTAETAKSLT DTPTLASPEG
1910 1920 1930 1940 1950
SGETESTAAD QEQCEEGWTK FQGHCYRHFP DRETWVDAER RCREQQSHLS
1960 1970 1980 1990 2000
SIVTPEEQEF VNKNAQDYQW IGLNDRTIEG DFRWSDGHSL QFEKWRPNQP
2010 2020 2030 2040 2050
DNFFATGEDC VVMIWHERGE WNDVPCNYQL PFTCKKGTVA CGEPPAVEHA
2060 2070 2080 2090 2100
RTLGQKKDRY EISSLVRYQC TEGFVQRHVP TIRCQPSADW EEPRITCTDP
2110 2120
NTYKHRLQKR TMRPTRRSRP SMAH
Length:2,124
Mass (Da):221,118
Last modified:July 1, 1989 - v2
Checksum:iE30BBE61593A34B1
GO
Isoform 2 (identifier: P07897-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1909-1909: A → ADIDECLSSPCLNGATCVDALDTFTCLCLPSYRGDLCEI

Show »
Length:2,162
Mass (Da):225,171
Checksum:iAE948F63BAC16612
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti38P → W AA sequence (PubMed:3693371).Curated1
Sequence conflicti61T → E AA sequence (PubMed:3693371).Curated1
Sequence conflicti149I → L AA sequence (PubMed:3693371).Curated1
Sequence conflicti239N → S AA sequence (PubMed:3693371).Curated1
Sequence conflicti241T → A AA sequence (PubMed:3693371).Curated1
Sequence conflicti275 – 276TV → RL in AAA21000 (PubMed:3693370).Curated2
Sequence conflicti374T → H AA sequence (PubMed:3693371).Curated1
Sequence conflicti377W → E AA sequence (PubMed:3693371).Curated1
Sequence conflicti380L → V AA sequence (PubMed:3693371).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0391961909A → ADIDECLSSPCLNGATCVDA LDTFTCLCLPSYRGDLCEI in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03485 mRNA. Translation: AAA21000.1.
M13518 mRNA. Translation: AAA41836.1.
PIRiA92623. A28452.
RefSeqiNP_071526.1. NM_022190.1.
UniGeneiRn.54503.

Genome annotation databases

GeneIDi58968.
KEGGirno:58968.
UCSCiRGD:68358. rat. [P07897-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03485 mRNA. Translation: AAA21000.1.
M13518 mRNA. Translation: AAA41836.1.
PIRiA92623. A28452.
RefSeqiNP_071526.1. NM_022190.1.
UniGeneiRn.54503.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TDQX-ray2.60B1909-2037[»]
ProteinModelPortaliP07897.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP07897. 1 interactor.
STRINGi10116.ENSRNOP00000042691.

Proteomic databases

PaxDbiP07897.
PRIDEiP07897.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi58968.
KEGGirno:58968.
UCSCiRGD:68358. rat. [P07897-1]

Organism-specific databases

CTDi176.
RGDi68358. Acan.

Phylogenomic databases

eggNOGiENOG410IJP2. Eukaryota.
ENOG410XRES. LUCA.
HOGENOMiHOG000168421.
HOVERGENiHBG007982.
InParanoidiP07897.
KOiK06792.

Miscellaneous databases

EvolutionaryTraceiP07897.
PROiP07897.

Family and domain databases

CDDicd00033. CCP. 1 hit.
Gene3Di2.60.40.10. 1 hit.
3.10.100.10. 5 hits.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR016187. CTDL_fold.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR000538. Link_dom.
IPR000436. Sushi_SCR_CCP_dom.
[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.
SM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
SM00445. LINK. 4 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF56436. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiPGCA_RAT
AccessioniPrimary (citable) accession number: P07897
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 1, 1989
Last modified: November 30, 2016
This is version 149 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.