ID A0A091G3R6_9AVES Unreviewed; 357 AA.
AC A0A091G3R6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Hyaluronan and proteoglycan link protein 3 {ECO:0000313|EMBL:KFO76518.1};
DE Flags: Fragment;
GN ORFNames=N303_10975 {ECO:0000313|EMBL:KFO76518.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO76518.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO76518.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO76518.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KL447713; KFO76518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091G3R6; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd05877; Ig_LP_like; 1.
DR CDD; cd03518; Link_domain_HAPLN_module_1; 1.
DR CDD; cd03519; Link_domain_HAPLN_module_2; 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; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR000538; Link_dom.
DR PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1.
DR PANTHER; PTHR22804:SF40; HYALURONAN AND PROTEOGLYCAN LINK PROTEIN 3; 1.
DR Pfam; PF07686; V-set; 1.
DR Pfam; PF00193; Xlink; 2.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00409; IG; 1.
DR SMART; SM00445; LINK; 2.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS50835; IG_LIKE; 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 Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..357
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011955102"
FT DOMAIN 47..158
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 165..260
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 266..355
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DISULFID 211..232
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 310..331
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO76518.1"
FT NON_TER 357
FT /evidence="ECO:0000313|EMBL:KFO76518.1"
SQ SEQUENCE 357 AA; 40416 MW; B251B8CD56DAAFFB CRC64;
LPLLLEATLL QLVSGFHRPF YNGFYYNHIM NDKGNGQETV DYFNGAKLVV ETPKDPVYSS
NGANVTLPCR YYYEPDLEAK PKIRIKWSKL RDDYTKDQDV LVAIGKTYVA FGDFQGRAHL
HQASRREASL VVSDVRLQDD GKYRCEVIDG LEDESNVVEL RLQGIVFPYQ PPLGQYKLNF
HEAERVCQEQ GAILATFNQL FQAWSEGLDW CNAGWLADGT VQYPIRLPRK KCGGLHLAPG
IRSYGPRHRH LHRFDAFCFS SGLRGEVFFL DHPAGMTLEE AKQSCQNAEA EIARVGQLYS
AWKFLGLDRC DAGWLADGSV RYPIVKPRAN CGPAEPGIRS FGFPSKGRFG VFCYKER
//
