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Database: UniProt
Entry: A0A452FU44_CAPHI
LinkDB: A0A452FU44_CAPHI
Original site: A0A452FU44_CAPHI 
ID   A0A452FU44_CAPHI        Unreviewed;       354 AA.
AC   A0A452FU44;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=HAPLN1 {ECO:0000313|Ensembl:ENSCHIP00000027903.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000027903.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000027903.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000027903.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   EMBL; LWLT01000008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005683456.1; XM_005683399.3.
DR   STRING; 9925.ENSCHIP00000027901; -.
DR   Ensembl; ENSCHIT00000035770.1; ENSCHIP00000027901.1; ENSCHIG00000023635.1.
DR   Ensembl; ENSCHIT00000035773.1; ENSCHIP00000027903.1; ENSCHIG00000023635.1.
DR   GeneID; 102169475; -.
DR   KEGG; chx:102169475; -.
DR   CTD; 1404; -.
DR   GeneTree; ENSGT00940000159267; -.
DR   OMA; ERACHDQ; -.
DR   OrthoDB; 5402504at2759; -.
DR   Proteomes; UP000291000; Chromosome 7.
DR   Bgee; ENSCHIG00000023635; Expressed in ovary and 13 other cell types or tissues.
DR   GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR   GO; GO:0045202; C:synapse; IEA:Ensembl.
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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hyaluronic acid {ECO:0000256|ARBA:ARBA00023290};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291000};
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_5040596426"
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;  40253 MW;  0F41984546B68D7D CRC64;
     MKSLLLLVLI SICWADHHSN NYTVDHDRVI HIQAENGPRL LVEAEQAKVF SRRGGNVTLP
     CKFYRDPTAF GSGTHKIRIK WTKLTSDYLK EVDVFVSMGY HKKTYGGYHG RVFLKGGSDN
     DASLVITDLT LEDYGRYKCE VIEGLEDDTA VVALDLQGVV FPYFPRLGRY NLNFHEAQQA
     CLDQDAVIAS FDQLYDAWRS GLDWCNAGWL SDGSVQYPIT KPREPCGGQN TVPGVRNYGF
     WDKDKSRYDV FCFTSNFNGR FYYLIHPTKL TYDEAVQACL NDGAQIAKVG QIFAAWKLLG
     YDRCDAGWLA DGSVRYPISR PRRRCSPSEA AVRFVGFPDK KHKLYGVYCF RAYN
//
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