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Database: UniProt
Entry: A0A3Q0S1X7_AMPCI
LinkDB: A0A3Q0S1X7_AMPCI
Original site: A0A3Q0S1X7_AMPCI 
ID   A0A3Q0S1X7_AMPCI        Unreviewed;       345 AA.
AC   A0A3Q0S1X7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Aggrecan a {ECO:0000313|Ensembl:ENSACIP00000016822.1};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000016822.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000016822.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00323}.
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DR   AlphaFoldDB; A0A3Q0S1X7; -.
DR   Ensembl; ENSACIT00000017277.1; ENSACIP00000016822.1; ENSACIG00000013081.1.
DR   GeneTree; ENSGT00940000155971; -.
DR   OMA; PEFDAYC; -.
DR   Proteomes; UP000261340; Unplaced.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   CDD; cd03517; Link_domain_CSPGs_modules_1_3; 1.
DR   CDD; cd03520; Link_domain_CSPGs_modules_2_4; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 2.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
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; PF07686; V-set; 1.
DR   Pfam; PF00193; Xlink; 2.
DR   PRINTS; PR01265; LINKMODULE.
DR   SMART; SM00445; LINK; 2.
DR   SUPFAM; SSF56436; C-type lectin-like; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS01241; LINK_1; 2.
DR   PROSITE; PS50963; LINK_2; 2.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00323};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..345
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018644181"
FT   DOMAIN          134..229
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DOMAIN          234..331
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DISULFID        180..201
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT   DISULFID        278..299
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ   SEQUENCE   345 AA;  38725 MW;  F7D4C290421C031F CRC64;
     CVLLSFFVLC VFLSFTDPDD VLRNKLIVKM FPLMQDHTVE DPGAPTIAPL SHRIKWSFVT
     KENVTTILVA LEGGVRITEN YKDRVQLLSY PGSPTDASIR ISELRSSDTG VYRCEVQRDI
     EDSYDIVHVQ VQGIVFHYRA IMGRYSLTFE KANAACTQNS AVMASPEQLQ AAYDDGFHQC
     DAGWLADRTV RYPIHSPRLN CYGDKEELPG VRTYGVRDLN ETYDVYCFAE KMTGRVFYTA
     TAEKFTFSEA VVACSNKGAQ LATTGQLYLA WQGGMDVCNA GWLGDRSVRY PINIRRPQCG
     GGLLGVRTVY LHTNQTGYPF PESRYDAFCY TGRSECALPH QQPTC
//
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