ID A0A3B3T3G3_9TELE Unreviewed; 355 AA.
AC A0A3B3T3G3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Hyaluronan and proteoglycan link protein 3 {ECO:0000313|Ensembl:ENSPKIP00000037008.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000037008.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000037008.1}
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; A0A3B3T3G3; -.
DR Ensembl; ENSPKIT00000017962.1; ENSPKIP00000037008.1; ENSPKIG00000015365.1.
DR GeneTree; ENSGT00940000159628; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; SM00406; IGv; 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|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00323}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 29..155
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 162..257
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 262..353
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DISULFID 208..229
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 282..351
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 307..328
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ SEQUENCE 355 AA; 39671 MW; B9E74B750C4577B0 CRC64;
MKCIFEIPPS MHVCIITVSK ACRVTSLIPF YVCTVLTVHF NGVKLIVETT ESSIFAAQGG
NVTLPCRYHY QPELQSPRRT RVKWSWVPAL GGRELDVLAA IGHRHRTFGA FQGRVRLLQD
PPGEASLVMG ELRTSDAGRY RCEVIDGLED ESAVVDLELR GVVFPYQPSR GRYRMNFSSA
QKACEEQGAM LATFDQLFSA WEEGLDWCNA GWLADGTVQY PITASRTPCG GQDLAPGVRS
YGARHRRLHL YDAFCFSPSL HGEVYFLQHP QKLNFTEAVQ ACEEDGSEIA RVGQLYVAWR
FLGLDHCDAG WLADGSLRYP VSTPRPNCGL QRPGVRSLGF PTQHQKYGVY CFRAP
//