ID A0A1U7R589_MESAU Unreviewed; 400 AA.
AC A0A1U7R589;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Hyaluronan and proteoglycan link protein 4 {ECO:0000313|RefSeq:XP_005086205.1};
GN Name=Hapln4 {ECO:0000313|RefSeq:XP_005086205.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005086205.1};
RN [1] {ECO:0000313|RefSeq:XP_005086205.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_005086205.1; XM_005086148.2.
DR AlphaFoldDB; A0A1U7R589; -.
DR STRING; 10036.ENSMAUP00000011366; -.
DR GeneID; 101837029; -.
DR KEGG; maua:101837029; -.
DR CTD; 404037; -.
DR eggNOG; ENOG502QRG1; Eukaryota.
DR OrthoDB; 5402504at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0072534; C:perineuronal net; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0150043; F:structural constituent of synapse-associated extracellular matrix; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:1904862; P:inhibitory synapse assembly; IEA:Ensembl.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IEA:Ensembl.
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; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR000538; Link_dom.
DR PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1.
DR PANTHER; PTHR22804:SF11; HYALURONAN AND PROTEOGLYCAN LINK PROTEIN 4; 1.
DR Pfam; PF07686; V-set; 1.
DR Pfam; PF00193; Xlink; 2.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 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 Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..400
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010559567"
FT DOMAIN 47..162
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 164..266
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 271..363
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DISULFID 210..231
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 316..337
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ SEQUENCE 400 AA; 42604 MW; 74104F8312F89F14 CRC64;
MACAPAALGP RALWAVAWGL LLLVPVPAGA QRGRKKVVHV LEGESGSVVV QTAPGQVVSH
RGGTIVLPCR YRYEAAAHGH DGVRLKWTKV VDPLAFADVF VALGPQHRAF GPYRGRAELQ
NDGPGDASLV LRNVTLQDYG RYECEVTNEL EDDAGMVKLD LEGVVFPYHP SGGRYKMTFV
EAQRACAEQD GILASAEQLH AAWRDGLDWC SAGWLRDGSV QYPVSQAREP CGGAGSPGAA
GGTNGGVRNY GYRHNAEERY DAFCFTSNLP GRVFFLKPLR PVALAGAARA CAARGATVAK
VGQLFAAWKL QLLDRCTAGW LADGSARYPI VNPRTRCGGP RPGVRSLGFP DASRRLFGVY
CYRAPGAPDP APGGWGWGWA GGGGWAGGSR DPAAWTPLRV
//
