ID A0A3Q1BDF7_AMPOC Unreviewed; 1290 AA.
AC A0A3Q1BDF7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Aggrecan core protein {ECO:0000256|ARBA:ARBA00039399};
DE AltName: Full=Cartilage-specific proteoglycan core protein {ECO:0000256|ARBA:ARBA00042947};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000007866.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000007866.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 80972.ENSAOCP00000007866; -.
DR Ensembl; ENSAOCT00000002067.1; ENSAOCP00000007866.1; ENSAOCG00000011821.1.
DR GeneTree; ENSGT00940000155971; -.
DR OMA; EDWIVTQ; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 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; IPR016187; CTDL_fold.
DR InterPro; IPR000742; EGF-like_dom.
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; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 1.
DR Pfam; PF00193; Xlink; 4.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00034; CLECT; 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; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
DR PROSITE; PS01241; LINK_1; 4.
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}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW 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 Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000257160};
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}; Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1290
FT /note="Aggrecan core protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018675210"
FT DOMAIN 36..151
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 155..250
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 255..352
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 436..531
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 536..633
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 1034..1069
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1082..1196
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1200..1260
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 383..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 201..222
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 299..320
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 482..503
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 580..601
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 1038..1048
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1059..1068
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1202..1245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1231..1258
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1290 AA; 139695 MW; 5B4094591CEBBCA8 CRC64;
MTPLLLLCLS LLPFISATIS FEDQDDVDGT LRVSIPMEMP LRPLLGSKVV VPCYFQDNTV
NDPGAPTIAP LSHRIKWTYV TKEKVSTILV ASEGKVQVET EYLDRVTMVN YPLVPTDATM
EMTELRSKDS GTYRCEVMHG IEDNYDSVDI QVQGIVFHYR AISTRYTLTF EKAKAACIQN
SATIATPAQL QAAYDDGYHQ CDAGWLSDQT VRYPIHEPRD RCYGDKETFP GVRTYGVRDV
NETYDVYCFA EKMSGRVFYS MSVEKFTFYE AGDQCAKLGA RLATTGELYL AWKGGMDVCN
AGWLGDRSVR YPINIARPQC GGGLLGVRTV YLFPNQTGYP YPDSRYDAIC FQAGEDGGVV
PERTTPFPDI INMTPAPGLF PSSTTSAGHK ESRSGGVDTF SPRPIPPSVT DTVTPVIREP
GLGLTDIYAA MAPTGVVFHY RPITGRYTLT FLEAQQACQN IGAVIASPPQ LQAAFEKGLH
QCDAGWLRDQ TVRYPIVSPR DNCAGNLPHL PGVRSYGLRP ATERYDVFCY VERLRGEVFF
TSDYDSFSYE EAVQHCQKLN TTLAAPGQLY AAWNQGLDKC RPGWLMDRSV RYPITTPRSH
CGGGQVGVHI IYAFPNQTGF PDEHSRYDAY CFKVETTVDY NETETHVIIT ETEFINKTTV
TTQQVAPAVR PVLPPPPVDV SGSGSADHSA SGEISGESGT SSTSGEASGS GQGVIFSGHT
DVFSGDQSGS GYPQEAEGGS SVIFTSGDAG SASGSGSVEG YDRQHSGSGI SGSGFASGSG
DISGESMIIM VDGKMVEVSK THQTSTEQEL GQGGIDTSGG FLESSVSGSG GMSGSGFSGF
SGVSFVDHSA IDLTVQPSGE QEVSGYHPFG SGFRGGFPSS FPSGVSGSGS ASGDSYQHRG
DVIYITDDEM IEMTVSPLER QPEQGRGVVE VSGEGSGSAI HHEFSGSFHL SGSGVPHERP
TAEGLSIALP PSSTMTHTEY IASLGQSGLG EIGQEEATPA VVTPDAAYTS PTTAPSVSFA
TPAVVEQPEV VEASVDLCDP NPCGSGTCSV QGDIAVCQCP TGFTGDDCST PLQGCAEGWL
EFMGNCYLHF AERDTWSEAE QRCQELNANL VSISSQEEQQ FVNSNGQDYQ WIGLNDKDVQ
NEFRWTDGSP LTFENWRPNQ PDNYFNSGED CVVMIWHEGG QWNDVPCNYH LPFTCKTGPV
MCGAPPEVEH GRPMGSSRQR YPVNSIVRYQ CDAGYTQRHL PVIRCLTNGQ WEEPQVECTE
AGANSNRLHK RSLRRRSRGV SSRQEQRKLH
//
