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Database: UniProt
Entry: A0A2Y9JLZ8_ENHLU
LinkDB: A0A2Y9JLZ8_ENHLU
Original site: A0A2Y9JLZ8_ENHLU 
ID   A0A2Y9JLZ8_ENHLU        Unreviewed;       354 AA.
AC   A0A2Y9JLZ8;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Hyaluronan and proteoglycan link protein 1 {ECO:0000256|ARBA:ARBA00040183};
DE   AltName: Full=Cartilage-linking protein 1 {ECO:0000256|ARBA:ARBA00042100};
DE   AltName: Full=Proteoglycan link protein {ECO:0000256|ARBA:ARBA00042980};
GN   Name=LOC111148410 {ECO:0000313|RefSeq:XP_022360639.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022360639.1};
RN   [1] {ECO:0000313|RefSeq:XP_022360639.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022360639.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Stabilizes the aggregates of proteoglycan monomers with
CC       hyaluronic acid in the extracellular cartilage matrix.
CC       {ECO:0000256|ARBA:ARBA00037563}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000256|ARBA:ARBA00004498}.
CC   -!- SIMILARITY: Belongs to the HAPLN family.
CC       {ECO:0000256|ARBA:ARBA00038272}.
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_022360639.1; XM_022504931.1.
DR   AlphaFoldDB; A0A2Y9JLZ8; -.
DR   STRING; 391180.A0A2Y9JLZ8; -.
DR   KEGG; elk:111148410; -.
DR   OrthoDB; 5402504at2759; -.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
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:SF10; HYALURONAN AND PROTEOGLYCAN LINK PROTEIN 1; 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   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00323};
KW   Hyaluronic acid {ECO:0000256|ARBA:ARBA00023290};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..354
FT                   /note="Hyaluronan and proteoglycan link protein 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015846616"
FT   DOMAIN          38..152
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          159..254
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DOMAIN          259..351
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DISULFID        205..226
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT   DISULFID        304..325
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ   SEQUENCE   354 AA;  40240 MW;  73BBE7CC915CB281 CRC64;
     MKRLLLLVLI SICWADHHSD NYTLDHDRVI HIQAENGPHL LVEAEQARVF SHRGGNVTLP
     CKFYRDPTAF GSGTHKIRIK WTKLTSDYLK EVDVFVSMGY HKKAYGGYQG RVFLKGGSDN
     DASLVIADLT LEDYGKYKCE VIEGLEDDTA VVALDLQGVV FPYFPRLGRY NLNFHEAQQA
     CLDQDAVIAS FDQLYDAWRG GLDWCNAGWL SDGSVQYPIT KPREPCGGQN TVPGVRNYGF
     WDKDKSRYDV FCFTSNFNGR FYYLIHPTKL TYDEAVQACL NDGAQIAKVG QIFAAWKLLG
     YDRCDAGWLA DGSVRYPISR PRRRCSPTEA AVRFVGFPDK KHKLYGVYCF RPYN
//
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