ID G3ICD5_CRIGR Unreviewed; 2120 AA.
AC G3ICD5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Aggrecan core protein {ECO:0000256|ARBA:ARBA00039399};
DE AltName: Full=Cartilage-specific proteoglycan core protein {ECO:0000256|ARBA:ARBA00042947};
GN ORFNames=I79_021328 {ECO:0000313|EMBL:EGW13739.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW13739.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC {ECO:0000256|ARBA:ARBA00006838}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; JH001911; EGW13739.1; -; Genomic_DNA.
DR STRING; 10029.G3ICD5; -.
DR PaxDb; 10029-XP_007628531-1; -.
DR eggNOG; ENOG502QUX8; Eukaryota.
DR InParanoid; G3ICD5; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR GO; GO:0031012; C:extracellular matrix; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 1.
DR CDD; cd03588; CLECT_CSPGs; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd03517; Link_domain_CSPGs_modules_1_3; 2.
DR CDD; cd03520; Link_domain_CSPGs_modules_2_4; 2.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 5.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033987; CSPG_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR000538; Link_dom.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR22804:SF42; AGGRECAN CORE PROTEIN; 1.
DR PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 1.
DR Pfam; PF07686; V-set; 1.
DR Pfam; PF00193; Xlink; 4.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SMART; SM00445; LINK; 4.
DR SUPFAM; SSF56436; C-type lectin-like; 5.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
DR PROSITE; PS01241; LINK_1; 3.
DR PROSITE; PS50963; LINK_2; 4.
DR PROSITE; PS50923; SUSHI; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hyaluronic acid {ECO:0000256|ARBA:ARBA00023290};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}.
FT DOMAIN 1..91
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 97..192
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 198..294
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 429..524
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 530..626
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 1868..1904
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1917..2031
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 2035..2095
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 665..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1275..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1537..1619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1680..1713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1744..1866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1049
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1553..1619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1755..1861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 143..164
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 241..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 475..496
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 573..594
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 1894..1903
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2037..2080
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 2066..2093
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 2120 AA; 220279 MW; 8763C6BA5AB5C554 CRC64;
MHPVTTAPST APLAPRIKWS RVSKEREVVL LVATEGQVRV NSIYQDKVSL PNYPAIPSDA
TLEIQNLRSN DSGIYRCEVM HGIEDSEATL EVIVKGIVFH YRAISTRYTL DFDRAQRACL
QNSAIIATPE QLQAAYEDGF HQCDAGWLAD QTVRYPIHTP REGCYGDKDE FPGVRTYGIR
DTNETYDVYC FAEEMEGEVF YATSPEKFTF QEAANECRRL GARLATTGQL YLAWQGGMDM
CSAGWLADRS VRYPISKARP NCGGNLLGVR TVYLHANQTG YPDPSSRYDA ICYTGEDFVD
IPENFFGVGV EDDITIQTVT WPDLELPLPR NTTEGEVRGN EILTAKPFFD LSPTISEPEE
ALTVFSGVRV TAFPEEETEE TTRPWAFPEE HTPGLDSATA FTSEDLVVQV TLAPGAAEVP
GQSRLPGGVV FHYRPGSTRY SLTFEEAQQA CMQTGAVMAS PEQLQAAYEA GYEQCDAGWL
QDQTVRYPIV SPRTPCVGDK NSSPGVRTYG VRPSSETYDV YCYVDKLEGE VFFVTRLEQF
TFQEAQVFCE AQNATLASTG QLYAAWSHGL DKCYAGWLAD GSLRYPIVTP RPACGGDKPG
VRTVYLYPNQ TGLPDPLSRH HAFCFRGVSV VPSLGREEGG MPTSPSDIED WIVTQVVPGV
DAIPLESETT ARPDFTTEPE KQTEWEPAYT PVGTSPLPGI PPTWLPTIPA AEDHTETPSA
TEEPSASEVP STSEEPHTTS LTSPSETELP GSGEASGPHD LSGDFTGSGE ASGGLGSSGQ
PSGVSESGLP SGDLDSSGLS PTVSSGLPVE SGQASGDGEG VGWSPTPTVS RLPSGGEGLE
GSASGTGELS GLPSGRETIE TSASGAEDIS GLPSGGDGLE TSTSGVEDVS GIPTETGGLE
ISASGVEDLS GLPSGQEGPE TSTSGIEDIS VLPTGGENLE TSASGVGDLS GLPSGGESLE
TSASGTEDVT QLPTEREGLE TSASGVEDIS VLPTGRETLE TSASGVEDVS GLPSGTGGLE
TSATGVEDVS GLSSGTGGLE TSSSGVEDIS VLPTEAGGLE TSASGGYVSG IPSGGDATET
SASGVEGVSG LPSGGDDLET SASGVEDLGL STREDLESSA SGVGATGPPA EREDLETSVS
GVGDDLSGLP SGKEGLETST SGAEDLGGLP SGKEDLIGSA SGAPDVDRLP TGTLGSGQTP
EASGLPSGFS GEYSGVDVGS GPSSGLPDFS GLPSGFPTVS LVDSTLVEVV TATTASEQEG
RGTIGISGAG EVSGLPLGEL DNSGDISGVP SGTELSGQAS GLPDVSGETS GFFDVSGQPF
ESSGVSQGTF GIPDTNGTSE VTELSGLSSG QPDVSGEGSG VLFGSGQSSG ITFVSGETSG
LPDLSGQPSG LPVFSGTTPR TPDLVSGSMS GSGDSSGITF VDSGFVEVTP TTFKEEEGLG
SVELSGLLSG EMDLSGTSGT VDISGQSSGA IDSSGFTSPA PELSGLSSGV AEVSGEFSGV
ETGSSLPSGA YDGSGLTSGF PTVSLVDRTL VESITQAPTA QEAGEGPSGI LELSGTHSGT
PDMSGDLSGS LDLSTLQSGL EPSTEPPSSP YFSGDFSSST DVSGESIAAT TGSGETSGLP
EVTLITSELV EAVTEPTVSQ ELGQGPSVTY TPGLFEVSGE ASASEDLGGA VTNFPGSGVE
ASVPEASSES SAYPEAGLGA SAAPEASSKQ SGFPDLHEIT SAFHEADLET TTSGMEVGST
SWTFQEGTRE GSAALEVSGE STTTSSVDTD TSGMPSATSV TSGDRTEVSG EWSDHTSKLN
VVISTNLPES EGAQPTQNPA GTHGEIKSPI SSYSGEETQT PETTISLTDA PSPSSPEGSG
EAESTAADID ECLSSPCLNG ATCVDAIDTF TCLCLPSYGG NLCEIDQEQC EEGWTKFQGH
CYRHFPDRET WVDAERRCRE QQSHLSSIVT PEEQEFVNKN AQDYQWIGLN DRTIEGDFRW
SDGHSLQFEK WRPNQPDNFF ATGEDCVVMI WHEKGEWNDV PCNYQLPFTC KKGTVACGDP
PVVEHARTLG QKKDRYEISS LVRYQCTEGF VQRHVPTIRC QPNGHWEEPR ITCTDSTMYK
RRLQKRSLRP TRRSRPSMAH
//
