ID A0A091SBY3_9GRUI Unreviewed; 2099 AA.
AC A0A091SBY3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Aggrecan core protein {ECO:0000256|ARBA:ARBA00039399};
DE AltName: Full=Cartilage-specific proteoglycan core protein {ECO:0000256|ARBA:ARBA00042947};
GN ORFNames=N332_08763 {ECO:0000313|EMBL:KFQ37905.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ37905.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ37905.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ37905.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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; KK814983; KFQ37905.1; -; Genomic_DNA.
DR Proteomes; UP000053369; Unassembled WGS sequence.
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:InterPro.
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; 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; PS01241; LINK_1; 3.
DR PROSITE; PS50963; LINK_2; 4.
DR PROSITE; PS50923; SUSHI; 1.
PE 4: Predicted;
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 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:UP000053369};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..2099
FT /note="Aggrecan core protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001879798"
FT DOMAIN 34..143
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 149..244
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 250..346
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 519..614
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 620..716
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 1843..1879
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1892..2006
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 2010..2070
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 790..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1221..1269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1371..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1416..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1774..1802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2079..2099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 195..216
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 293..314
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 565..586
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 663..684
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 1869..1878
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2012..2055
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 2041..2068
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 2099 AA; 223512 MW; 69634D829C5D72B3 CRC64;
MTTLLLVFVC LRVITAAVSV ELSDSSDGLE VKIPEKSPLR VVLGSSLNIP CYFNIPEEED
TSALLTPRIK WSKLSNGTEV VLLVATGGKI RLNTEYREVI SLSNYPAIPT DASLEIKALR
SNHTGIYRCE VMYGIEDRQD TIEVLVKGIV FHYRAISTRY TLNFEKAKQA CIQNSAVIAT
PEQLQAAYED GYEQCDAGWL ADQTVRYPIH WPRERCYGDK DEFPGVRTYG VREPDETYDV
YCYAEQMQGE VFYATAPEKF TFQEAFDKCH SLGARLATTG ELYLAWKDGM DMCSAGWLAD
RSVRYPISRA RPNCGGNLVG VRTVYLYVNQ TGYPHPDSRY DAICYRGDDV ELLVPGQFID
EIGSELGSAF TVQTVTQTEV ELPLPRNATE EEARGSIATL EPIEVTPTVT ELYEGFTVLP
DLFATSVTVE TAAPEEENVT REDATRAWTV PEEVTTIALD TAISTEMAEV SSVEEVVGVT
ATPGLESTSA FTVEDQLVRV TAAPGVGLLP RQPISPTGVV FHYRAATSRY AFSFVQAQQA
CLENNAVIAT PEQLQAAYEA GFDQCDAGWL RDQTVRYPIV NPRSNCLGDK ENSPGVRSYG
MRPASETYDV YCYIDRLKGE VFFATQPEQF TFPEAQQYCE SQNATLASVG QLHAAWKQGL
DRCYAGWLAD GSLRYPIVSP RPACGGDAPG VRTVYQHYNQ TGFPDPLSRH HTFCFRALPP
AEEEGVTSFF EEDVLATQVI PGVEGVPSGE EATMETEFAT QPENQTAWGT EVFPTDVSLL
SVSPSAFPPA TVIPEETSTN ASISEVSGEV TDSGDHQVSG ESSASGWVSG VPDASGEPTS
GVFEHSGEHS GIGESGLPSV DLHASGFLPG ESGLPSGDLS GVPSGTVDIS GLPSAEEEVL
VSTSRITEIS GMPSGVESSG LPSGFSGDIS GTELVSGMSS GEESGVASGF PTVSLVDTTL
VEVVTTAPER REEGKGSIGV SGEGDLSGFP STEWGASGGA QELPSGAELS GEPSGEPKLS
REHSGVPELS GEPSGGPELS ELPSGLDVSG EPSGTHEVSG MVDLSGLTSG TDGSGEASGI
TFVDASLEEV TTTPSITGAE AKETLEISGL PSGGEDTSGM ASGSLDISGE PSGHVDFGGS
ASGVFEVSGH PSGVIDSSGD LSGVDVTSGH LSGEESGFTS GFPTVSLVDA TLVEVVTQPS
VAQEVGEGPS GVIEISGFPS GDRGLSGEGS GAVETSGFPS GTEEFSGETS GIPYASGDIS
GATDLSGQSS AVTDISGEVS GLPEVTLVTS DLIEVVTRPT VSQELGGETA VTFPYGFGPS
GEASASGELS GETSALPESS IETSTAYEIS GETAVFPESS TETSTFQEIS GETSAFPETS
VETSTIPETS GETSAFPEIN IETSTIQEII QEVSGETSAF PEGSTETSTT QEISGETSAF
PEIRIETSTI QEISGESSAF PEIRIETFTS QEARGETSGY PEISIETSTV HETSGETSAF
PEISIETSTV HEISGETSAF PEISIETSTV HEISGESSAF PEIRIETSTN QEARGETSAF
PEISIETSTV HETSGETSAF PEISIETSTV HEISGETSAF PEIRIETSTN QEARGEISAF
PEISIETSTV HEISGETSAF PEISIETPTS QEARGETSAY PEIIIETSTV QEVSGETSAF
PEIRTEMSTT QEAWVETSAF PETSIETSTV HETSGETSAL PAANIETAVT SLASGEPSGA
PKQKEIADAT SGAVTHSVTG VSGETSVPDI VISTSAPDVE PTQGPRSPEE GQLNIEPSPP
VVSGQETETA VVLDNPHLLA TATAALPQAS QEAIDTLGPT TEDTDECHSS PCLNGATCVD
GIDSFKCLCL PSYGGDLCEI DLENCEEGWT KFQGHCYKHF EDRETWMDAE ARCRQHQAHL
SSIITPEEQE FVNSHAQDYQ WIGLSDRAVE NDFRWSDGHP LQLENWRPNQ PDNFFSAGED
CVVMIWHEKG EWNDVPCNYH LPFTCKKGTV ACGDPPAVEN ARTFGRKKDR YEINSLVRYQ
CSQGYIQRHV PTIRCQPNGQ WEEPRISCIN PSNYQRRLYK RSPRSRSRPS GRAVHRPTH
//
