ID A0A2K5UIA3_MACFA Unreviewed; 2247 AA.
AC A0A2K5UIA3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Aggrecan core protein {ECO:0000256|ARBA:ARBA00039399};
DE AltName: Full=Cartilage-specific proteoglycan core protein {ECO:0000256|ARBA:ARBA00042947};
GN Name=ACAN {ECO:0000313|Ensembl:ENSMFAP00000012113.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000012113.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000012113.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000012113.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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DR STRING; 9541.ENSMFAP00000012113; -.
DR Ensembl; ENSMFAT00000055435.2; ENSMFAP00000012113.2; ENSMFAG00000019208.2.
DR VEuPathDB; HostDB:ENSMFAG00000019208; -.
DR GeneTree; ENSGT00940000155971; -.
DR OrthoDB; 5402504at2759; -.
DR Proteomes; UP000233100; Chromosome 7.
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; cd05900; Ig_Aggrecan; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000233100};
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..2247
FT /note="Aggrecan core protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030050959"
FT DOMAIN 34..147
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 153..248
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 254..350
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 478..573
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 579..675
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 1995..2031
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2044..2158
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 2162..2222
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 738..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1665..1691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1726..1745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1763..1926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1963..1990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..830
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1726..1742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1763..1787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1810..1824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1836..1850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1863..1926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1963..1989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 199..220
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 297..318
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 524..545
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 622..643
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 2021..2030
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2164..2207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 2193..2220
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 2247 AA; 233228 MW; A24D037813CFA7DF CRC64;
MTTLLWVFVT LRVIAAAVTV ETSDHDNSLS VSIPQPSPLR VLLGTSLTIP CYFIDPMHPV
TTAPSTAPLA PRIKWSRVSK EKEVVLLVAT EGRVRVNSAY QDKVSLPNYP AIPSDATLEI
QSLRSNDSGV YRCEVMHGIE DSEATLEVVV KGIVFHYRAI STRYTLDFDR AQRACLQNSA
IIATPEQLQA AYEDGFHQCD AGWLADQTVR YPIHTPREGC YGDKDEFPGV RTYGIRDTNE
TYDVYCFAEE MEGEVFYATS PEKFTFQEAA SECRRLGARL ATTGQLYLAW QAGMDMCSAG
WLADRSVRYP ISKARPNCGG NLLGVRTIYL HANQTGYPDP SSRYDAICYT GEDFVDIPEN
FFGVGGEEDI TVQTVTWPDM ELPLPRNITE GEARGSVILT VKPIFDVSPS PLEPEEPFTF
APEIGATAFP EVENETGEAT RPWGFPTPGL GPATAFTSED LVVQVTAVPG QPHLPGGVVF
HYRPGSTRYS LTFEEAQQAC LRTGAVIASP EQLQAAYEAG YEQCDAGWLR DQTVRYPIVS
PRTPCVGDKD SSPGVRTYGV RPSTETYDVY CYVDRLEGEV FFATRLEQFT FQEALEFCES
HNATLATTGQ LYAAWSRGLD KCYAGWLADG SLRYPIVTPR PACGGDKPGV RTVYLYPNQT
GLPDPLSRHH AFCFRGVSAV PSPGEEEGGT PTSPSGVEDW IATQVVPGVA AVPVEEETTA
VPLGETTAIL EFTTEPENQT EWEPAYTPMG TSPLPGILPT WPPTGTATEE STEGPSATEV
LTASKEPSPP EVPFPSEEPS PSEEPFPSVR PFPSVEPSPS EEPFPSVEPS PSEEPSASEE
PYTPSPPVPS WTELPGSGEE SGAPDVSGDF IGSGDVSGHL DFSGQLSGDR ISGLPSGDLD
SSGLTSTVGS GLPVDSGLAS GDEERIEWSS TPTVGELPSG AEILEGSASE VGDLSGLPSG
DILETSASGV GDLSGLPSGE VLETSASGVG DLSGLPSGEV LETSTSGVGD LSGLPSGEVL
ETSTSGVGDL SGLPSAGEVL ETTASGVEDI SGLPSGEVLE TTASGVEDIS GLPSGEVLET
TASGVEDISG LPSGEVLETT ASGVGDLGGL PSGEVLETST SGVGDLSGLP SGEVVETSTS
GVEDLSGLPS GGEVLETSTS GVEDISGLPS GEVLETTASG IEDVSELPSG EGLETSASGV
EDLSRLPSGE VLETSASGVG DISGLPSGGE VLEISASGVG DLSGLPSGGE GLETSASGVG
TDLSGLPSGR EGLETSASGA EDLSGLPSGK EDLVGPASGD LDLGKLPSGT LGSGQAPETS
GLPSGFSGEY SGVDLGSGPP SGLPDFSGLP SGFPTVSLVD STLVEVVTAS TASELEGRGT
IGISGAGEIS GLPSSELDIS GEASGLPSGT ELSGQASGSP DVSRETPGLF DVSGQPSGFP
DISGGTSGIS EVSGQPSGFP DTSGETSGVT ELSGLPSGQP GVSGEASGVP YGSSQPFGIT
DLSGETSGVP DLSGQPSGLP GFSGATSGVP DLVSGATSGS GESSGITFVD TSLVEVTPTT
FKEEEGLGSV ELSGLPSGEA DLSGRSGMVD VSGQFSGTVD SSGFTSQTTE FSGLPIGIAE
VSGESSGAET GSSLPSGAYY GSELPSGFPT VSLVDRTLVE SVTQAPTAQE AGEGPPGILE
LSGTHSGAPD MSGDHSGFLD VSGLQFGLVE PSGEPPSTPY FSGDFASTTD VSGESSAAMG
TSGEASGLPE VTLITSEFME GVTEPTVSQE LGQRPPVTHT PQLFESSGEA SVAGDISGAT
PVLPGSGVEV SSVPESSSET SAYPEAGVGA SAAPETSGED SGSPDLSETT SAFHEADLER
SSGLGVSGST LTFQEGEPSA SPEVSGESTT TGDVGTEAPG LPSATPTASG DRTEISGDLS
GHTSGLGVVI STSIPESEWT QQTQRPAEAH LETESSSLLY SGEETHTAET ATSPTDASIP
ASPEWTGESE STVADIDECL SSPCLNGATC VDAIDSFTCL CLPSYGGDLC EIDQEVCEEG
WTKYQGHCYR HFPDRETWVD AERRCREQQS HLSSIVTPEE QEFVNNNAQD YQWIGLNDRT
IEGDFRWSDG HPMQFENWRP NQPDNFFAAG EDCVVMIWHE KGEWNDVPCN YHLPFTCKKG
TVACGEPPMV QHARTFGQKK DRYEINSLVR YQCTEGFVQR HVPTIRCQPS GHWEEPRITC
TDATAYKRRL QKRSSRHPRR SRPSTAH
//
