ID   HPLN1_PIG               Reviewed;         354 AA.
AC   P10859;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Hyaluronan and proteoglycan link protein 1;
DE   AltName: Full=Cartilage-linking protein 1;
DE            Short=Cartilage-link protein;
DE   AltName: Full=Proteoglycan link protein;
DE   Flags: Precursor;
GN   Name=HAPLN1; Synonyms=CRTL1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Laryngeal cartilage chondrocyte;
RX   PubMed=2738916; DOI=10.1016/0022-2836(89)90580-9;
RA   Perkins S.J., Nealis A.S., Dudhia J., Hardingham T.E.;
RT   "Immunoglobulin fold and tandem repeat structures in proteoglycan N-
RT   terminal domains and link protein.";
RL   J. Mol. Biol. 206:737-753(1989).
CC   -!- FUNCTION: Stabilizes the aggregates of proteoglycan monomers with
CC       hyaluronic acid in the extracellular cartilage matrix.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- SIMILARITY: Belongs to the HAPLN family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Y00165; CAA68358.1; -; mRNA.
DR   PIR; S04243; S04243.
DR   RefSeq; NP_001004028.1; NM_001004028.1.
DR   AlphaFoldDB; P10859; -.
DR   SMR; P10859; -.
DR   STRING; 9823.ENSSSCP00000015032; -.
DR   PaxDb; P10859; -.
DR   PeptideAtlas; P10859; -.
DR   PRIDE; P10859; -.
DR   GeneID; 445513; -.
DR   KEGG; ssc:445513; -.
DR   CTD; 1404; -.
DR   eggNOG; ENOG502QRAR; Eukaryota.
DR   InParanoid; P10859; -.
DR   OrthoDB; 743812at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.10.100.10; -; 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   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; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF56436; SSF56436; 2.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS01241; LINK_1; 2.
DR   PROSITE; PS50963; LINK_2; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Hyaluronic acid;
KW   Immunoglobulin domain; Reference proteome; Repeat; Secreted.
FT   PROPEP          1..9
FT                   /id="PRO_0000013181"
FT   CHAIN           10..354
FT                   /note="Hyaluronan and proteoglycan link protein 1"
FT                   /id="PRO_0000013182"
FT   DOMAIN          38..152
FT                   /note="Ig-like V-type"
FT   DOMAIN          159..254
FT                   /note="Link 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT   DOMAIN          259..351
FT                   /note="Link 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        61..139
FT                   /evidence="ECO:0000250"
FT   DISULFID        181..252
FT                   /evidence="ECO:0000250"
FT   DISULFID        205..226
FT                   /evidence="ECO:0000250"
FT   DISULFID        279..349
FT                   /evidence="ECO:0000250"
FT   DISULFID        304..325
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  40261 MW;  68FFFB9DE51ABCC1 CRC64;
     MKSLLLLVLI SVCWADHLSN NYTLDHDRVI HIQAENGPRL LVEAEQAKVF SHRGGNVTLP
     CKFFRDPTAF GSGTHKIRIK WTKLTSDYLK EVDVFVSMGY HKKTYGGYHG RVFLKGGSDN
     DASLVITDLT LEDYGRYKCE VIEGLEDDTA VVALDLEGVV FPYFPRLGRY NLNFHEAQQA
     CLDQDAVIAS FDQLYDAWRG GLDWCNAGWL SDGSVQYPIT KPREPCGGQN TVPGVRNYGF
     WDKDKSRYDV FCFTSNFNGR FYYLIHPTKL TYDEAVQACL NDGAQIAKVG QIFAAWKLLG
     YDRCDAGWLA DGSVRYPISR PRRRCRPNEA AVRFVGFPDK KHKLYGVYCF RAYN