ID A0A3Q3EGG2_9LABR Unreviewed; 478 AA.
AC A0A3Q3EGG2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Hyaluronan binding protein 2 {ECO:0000313|Ensembl:ENSLBEP00000006601.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000006601.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000006601.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A3Q3EGG2; -.
DR STRING; 56723.ENSLBEP00000006601; -.
DR Ensembl; ENSLBET00000006938.1; ENSLBEP00000006601.1; ENSLBEG00000005064.1.
DR GeneTree; ENSGT00940000167141; -.
DR InParanoid; A0A3Q3EGG2; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00108; KR; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR24264:SF40; HYALURONAN-BINDING PROTEIN 2; 1.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00130; KR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 4: Predicted;
KW Digestion {ECO:0000256|ARBA:ARBA00022757};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 44..82
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 85..121
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 126..208
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 239..476
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 48..58
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 53..70
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 72..81
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 111..120
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 478 AA; 53247 MW; 1FE4B0618AA5261E CRC64;
MKSIQLQPSQ RSLLPSSPSV GGRSQAAPPG SLEERSLFLE LIPVKDVCEN VRCGRGDCVV
NLKRPPFYEC KCTPPYYGPN CRSFPTSPCV RNPCKNGGSC VARDKRLSCA CPNEFTGRFC
QTGKEDCYIG NGESYRGAVS VTEGGMECLD WNSYFILSQG EDPFTMYSDF PGLGYNNDCR
NPDNDDKPWC YYKKQGRLEW DFCKINKCSE GNLKLPVSTL FSQCGKVDLG TQPVRTGRIY
GGTKSYPGAH PWQVSLQAKL RGSSFQFTHF CGGILLSSCW VLTAAHCINN ENEYQVVLGG
VHLEKQEQMD QTIPVIQTIV HENYRETPVA LYNDIALLKL KITEAPYCAK ETRFVRAACL
PDQAFPAGKE CVISGWGATE NQRYSPQLLN ARVFMISDRK CRSPEVYGSV LNNSMICAGT
LRGGIDSCQV DLWCVSRTVH IISGVVSWGD DCGKKNKPGV YANIHAFTDW INRKMNWK
//