ID A0A2U9BUR7_SCOMX Unreviewed; 1200 AA.
AC A0A2U9BUR7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Aggrecan core protein {ECO:0000256|ARBA:ARBA00039399};
DE AltName: Full=Cartilage-specific proteoglycan core protein {ECO:0000256|ARBA:ARBA00042947};
GN ORFNames=SMAX5B_005101 {ECO:0000313|EMBL:AWP08008.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP08008.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP08008.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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:PRU00323}.
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DR EMBL; CP026252; AWP08008.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9BUR7; -.
DR STRING; 52904.ENSSMAP00000007545; -.
DR Proteomes; UP000246464; Chromosome 10.
DR GO; GO:0016020; C:membrane; 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; 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; 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; 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; 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:PRU00302}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; 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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1200
FT /note="Aggrecan core protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016064455"
FT DOMAIN 35..150
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 154..249
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 254..351
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 438..533
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 538..635
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 986..1106
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1110..1170
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 670..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 200..221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 298..319
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 484..505
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 582..603
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 1112..1155
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1141..1168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1200 AA; 130391 MW; 2611B97E0CB9A67A CRC64;
MTPLLLLCVS LPLISATISF EDHENLDGTL RVSIPMEMPL QPLLGGKVVV PCYFQDNTVS
DPGAPTIPPL SHRIKWSYVT KEKVTTILVA SEGKVQVDTE YLDRVTLINY PLVPTDATLE
ITELRSKDSG TYRCEVMHGI EDNYDSVDIQ VQGIVFHYRA ISTRYTLTFE KAKAACTQNS
ATIATPAQLQ AAYDDGYHQC DAGWLSDQTV RYPIQEPRER CYGDKENFPG VRTYGVRDVN
ETYDVYCFAE KMSGRVFYSM SVEKFTFYEA GDQCTKLGAR LATTGELYLA WKAGMDVCNA
GWLGDRSVRY PINIARTQCG GGLLGVRTVY LFPNQTGYPY PDSRYDAICF RDGEDEDVVP
MRTTPFPDII RITPAPGVYP GLSPAPGGEE IRGGEVDILS PLPVPPRVTD TYTKVTTVVR
EPGLDLTGFD AAMAPTGVVF HYRPITGRYT LTFLEAQQAC QSIGAVIASP LQLQAAFEKG
LHQCDAGWLR DQTVRYPIVS PRDNCAGNLP HLPGVRSYGL RPASELYDVF CYVERLQGEV
FFTSDYDSFS YDEAVQHCQK LNTTLATTGQ LFAAWKQGLD KCRPGWLMDR SVRYPITTPR
SHCGGGQVGV HIIYAFPNQT GFPDEHSRYD AYCFKVETTV VYNETESSVN ITEIEEVISK
TIITTHQVAP PVDVSGSGSA DHSASGETSG ASGVSSASGD ASGLGQDITY SGHTDIVSGD
QSASGGPQEA EGSTVLFSSG ELGSASGSGE GIDGGSGDIS GSGDISASGD ISGSGGDLII
IMVDGKMVEV SKTQSQPDEQ LLGKEGIEII ESSASGSASA SGSGSGGFSG ISFIDHSAVD
LTVEPSGEQE VSGYRPFGSG FHSGFPSGFP SGASGSGSAS GDSVQHRGDV IYVTDDEMIE
VTVPPLERQP QQGRGVVEVS GAGSGSGIHH EEFSGALEQS SHLSGSGAAH EKPTTEKLSV
ILPPGSTMTY SEYIAVQGCA DGWLEFGGSC YLHFAERYTW TDAEQRCQEL NAHLVSINSQ
EEQEFVNSTQ QTNTHGQDYQ WIGLNDKDVQ NEFRWTDRSP LTFVNWRPNQ PDNYFNSEED
CVVMIWHEGG QWNDVPCNYH LPFTCKTGPV VCGAPPEVEH GRPMGSGRDR YPVDSIVRYQ
CDAGYTQRHL PVIRCMPDGQ WAEPQVECTE AGANSNRLHK RSVRRRSKAV SSQQEQRKLL
//
