ID A0A340YEZ0_LIPVE Unreviewed; 360 AA.
AC A0A340YEZ0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Hyaluronan and proteoglycan link protein 3 {ECO:0000313|RefSeq:XP_007470574.1};
GN Name=HAPLN3 {ECO:0000313|RefSeq:XP_007470574.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007470574.1};
RN [1] {ECO:0000313|RefSeq:XP_007470574.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00323}.
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DR RefSeq; XP_007470574.1; XM_007470512.1.
DR AlphaFoldDB; A0A340YEZ0; -.
DR STRING; 118797.A0A340YEZ0; -.
DR GeneID; 103088534; -.
DR KEGG; lve:103088534; -.
DR CTD; 145864; -.
DR InParanoid; A0A340YEZ0; -.
DR OrthoDB; 5402504at2759; -.
DR Proteomes; UP000265300; Unplaced.
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; 1.
DR PROSITE; PS50963; LINK_2; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00323};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Reference proteome {ECO:0000313|Proteomes:UP000265300};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..360
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016297600"
FT DOMAIN 63..164
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 166..261
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 266..358
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DISULFID 212..233
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 311..332
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ SEQUENCE 360 AA; 41045 MW; 983601729FCA50CA CRC64;
MGLPPLGLLL SLCCVSGLPF YNGFYYSNSP HGWNPGKGHG EGIFNGVKLV VETPEEILFS
YRGANVTLPC RYHYEPALVS PRPVRIKWWK LSENGAPEQD VLVAIGLRHR AFGDYRGRVH
LWQEREREVS LEIRDLRLED YGRYRCEVID GLEDESGLVE LELRGVVFPY QHPQGRYQFN
FHEAQWACEE QDAVVASFEQ LFRAWEEGLD WCNAGWLQDA SVQYPITQAR HPCGGLGLAP
GVRSYGPRHR RLHRYDVFCF AAALRGQVYY LEHPEKLTLA EAKEACQEDG AQIAKVGQLF
AAWKFHGLDR CDAGWLADGS ARYPVAHPRR NCGSLEPGVR SFGFPDPHSR KYGVYCYRPR
//
