ID A0A2R9C002_PANPA Unreviewed; 2007 AA.
AC A0A2R9C002;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:ENSPPAP00000032073.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000032073.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000032073.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000032073.1}
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:PRU00323}.
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DR EMBL; AJFE02069887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02069888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008972114.1; XM_008973866.1.
DR Ensembl; ENSPPAT00000054939.1; ENSPPAP00000032073.1; ENSPPAG00000038878.1.
DR GeneTree; ENSGT00940000155971; -.
DR OMA; EDWIVTQ; -.
DR OrthoDB; 5402504at2759; -.
DR Proteomes; UP000240080; Chromosome 15.
DR Bgee; ENSPPAG00000038878; Expressed in prefrontal cortex.
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; cd03588; CLECT_CSPGs; 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; 2.60.40.10; 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; IPR033987; CSPG_CTLD.
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 PANTHER; PTHR22804:SF42; AGGRECAN CORE PROTEIN; 1.
DR PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF07686; V-set; 1.
DR Pfam; PF00193; Xlink; 4.
DR PRINTS; PR01265; LINKMODULE.
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; 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; 3.
DR PROSITE; PS50963; LINK_2; 4.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00323}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022974};
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:UP000240080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|ARBA:ARBA00022659}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..2007
FT /note="Aggrecan core protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015359599"
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 1865..1979
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 734..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1360..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1459..1478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1524..1608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1622..1782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1824..1851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1987..2007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1581..1601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1622..1653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1742..1782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1824..1838
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"
SQ SEQUENCE 2007 AA; 209526 MW; 45E856B4450448EB CRC64;
MTTLLWVFVT LRVITAAVTV ETSDHDNSLS VSIPQPSPLR VLLGTSLTIP CYFIDPMHPV
TTAPSTAPLA PRIKWSRVSK EKEVVLLVAT EGRVRVNSAY QDKVSLPNYP AIPSDATLEV
QSLRSNDSGV YRCEVMHGIE DSEATLEVVV KGIVFHYRAI STRYTLDFDR AQRACLQNSA
IIATPEQLQA AYEDGFHQCD AGWLADQTVR YPIHTPREGC YGDKDEFPGV RTYGIRDTNE
TYDVYCFAEE MEGEVFYATS PEKFTFQEAA NECRRLGARL ATTGQLYLAW QAGMDMCSAG
WLADRSVRYP ISKARPNCGG NLLGVRTVYV HANQTGYPDP SSRYDAICYT GEDFVDIPEN
FFGVGGEEDI TVQTVTWPDM ELPLPRNITE GEARGSVILT VKPIFEVSPS PLEPEEPFTF
APEIGATAFP EVENETGEAT RPWGFPTPGL GPATAFTSED LVVQVTAVPG QPHLPGGVVF
HYRPGPTRYS LTFEEAQQAC LRTGAVIASP EQLQAAYEAG YEQCDAGWLR DQTVRYPIVS
PRTPCVGDKD SSPGVRTYGV RPSTETYDVY CFVDRLEGEV FFATRLEQFT FQEALEFCES
HNATLATTGQ LYAAWSRGLD ECYAGWLADG SLRYPIVTPR PACGGDKPGV RTVYLYPNQT
GLPDPLSRHH AFCFRGISAV PSPGEEEGGT PTSPSGVEEW IATQVVPGVA AVPVEEETTA
VPSRETTAIL EFTTEPENQT EWEPAYTPVG TSPLPGILPT WPPTGAATEE STEGPSATEV
PSASEEPSPS EVPFPSEEPS PSEEPFPSVE LFPSEEPFPS KEPSPSEEPS ALEEPYTPSP
PVPSWTELPS SGEESGAPDV SGDFTGSGDV SGHLDFSGQL SGDRASGLPS GDLDSSGLIS
TVGSGLPVES GLPSGDEERI EWPSTPTVGE LPSGAEILEG SASGVGDLSG LPSGEVLETS
ASGVGDLSGL PSGEVLETTA PGVEDISGLP SGEVLETTAP GVEEISGLPS GEVLETTAPG
VEEISGLPSG EVLETSTSAA GDLSGLPSGG EVLEISASGV EDISGLPSGE VVETSASGIE
DVSELPSGEG LETSASGVED LSRLPSGEEV LEISASGFGD LSGLPSGGEG LETSASEVGT
DLSGLPSGRE GLETSASGAE DLSVLPSGKE DLVGSASGDL DLGKLPSGTL GSGQAPETSG
LPSGFSGEYS GVDLGSGPPS GLPDFSGLPS GFPTVSLVDS TLVEVVTAST ASELEGRGTI
GISGAGEISG LPSSELDISG RASGLPSGTE LSGQASGSPD VSGEIPGLFG VSGQPSGFPD
TSGETSGVTE LSGLSSGQPG VSGEASGVLY GTSQPFGITD LSGETSGVPD LSGQPSGLPG
FSGATSGVPD LVSGTTSGSG ESSGITFVDT SLVEVAPTTF KEEEGLGSVE LSGLPSGEAD
LSGKSGMVDV SGQFSGTVDS SGFTSQTPEF SGLPSGIAEV SGESSRAEIG SSLPSGAYYG
SGTPSSFPTV SLVDRTLVES VTQAPTAQEA GEGPSGILEL SGAHSGAPDM SGEHSGFLDL
SGLQSGLVEP SGEPPGTPYF SGDFASTTNV SGESSVAMGT SGEASGLPEV TLITSEFVEG
VTEPTVSQEL GQRPPVTHTP QLFESSGEVS TAGDVSGATP VLPGSGVEVS SVPESSSETS
AYPEAGFGAS AAPEASREDS GSPDLSETTS AFHEADLERS SGLGVSGSTL TFQEGEASAA
PEVSGESTTT NDVGTEAPGL PSATPTASGD RTEISGDLSG HTSRLGVVIS TSIPESEWTQ
QTQRPAETHL EIESSSLLYS GEETHTVETA TSPTDASIPA SPEWKRESES TAADQEVCEE
GWNKYQGHCY RHFPDRETWV DAERRCREQQ SHLSSIVTPE EQEFVNNNAQ DYQWIGLNDR
TIEGDFRWSD GHPMQFENWR PNQPDNFFAA GEDCVVMIWH EKGEWNDVPC NYHLPFTCKK
GTATTYKRRL QKRSSRHPRR SRPSTAH
//
