HPLN1_CHICK
ID HPLN1_CHICK Reviewed; 355 AA.
AC P07354;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 143.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryonic sternal cartilage;
RX PubMed=3459154; DOI=10.1073/pnas.83.11.3766;
RA Deak F., Kiss I., Sparks K.J., Argraves W.S., Hampikian G., Goetinck P.F.;
RT "Complete amino acid sequence of chicken cartilage link protein deduced
RT from cDNA clones.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3766-3770(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3476955; DOI=10.1073/pnas.84.18.6399;
RA Kiss I., Deak F., Mestric S., Delius H., Soos J., Dekany K., Argraves W.S.,
RA Sparks K.J., Goetinck P.F.;
RT "Structure of the chicken link protein gene: exons correlate with the
RT protein domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6399-6403(1987).
RN [3]
RP GLYCOSYLATION AT ASN-56.
RX PubMed=1985942; DOI=10.1016/s0021-9258(17)35300-0;
RA Wu L.N., Genge B.R., Wuthier R.E.;
RT "Association between proteoglycans and matrix vesicles in the extracellular
RT matrix of growth plate cartilage.";
RL J. Biol. Chem. 266:1187-1194(1991).
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}.
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DR EMBL; M13212; AAA48940.1; -; mRNA.
DR EMBL; M35038; AAA48941.1; -; Genomic_DNA.
DR EMBL; M35035; AAA48941.1; JOINED; Genomic_DNA.
DR EMBL; M35036; AAA48941.1; JOINED; Genomic_DNA.
DR EMBL; M35037; AAA48941.1; JOINED; Genomic_DNA.
DR PIR; A28305; LKCH.
DR RefSeq; NP_990813.1; NM_205482.1.
DR RefSeq; XP_015136080.1; XM_015280594.1.
DR RefSeq; XP_015136082.1; XM_015280596.1.
DR RefSeq; XP_015136083.1; XM_015280597.1.
DR RefSeq; XP_015136084.1; XM_015280598.1.
DR AlphaFoldDB; P07354; -.
DR SMR; P07354; -.
DR STRING; 9031.ENSGALP00000041828; -.
DR iPTMnet; P07354; -.
DR PaxDb; P07354; -.
DR Ensembl; ENSGALT00000025196; ENSGALP00000025150; ENSGALG00000015627.
DR Ensembl; ENSGALT00000047210; ENSGALP00000053484; ENSGALG00000015627.
DR Ensembl; ENSGALT00000087055; ENSGALP00000062830; ENSGALG00000015627.
DR Ensembl; ENSGALT00000098803; ENSGALP00000072418; ENSGALG00000015627.
DR GeneID; 396475; -.
DR KEGG; gga:396475; -.
DR CTD; 1404; -.
DR VEuPathDB; HostDB:geneid_396475; -.
DR eggNOG; ENOG502QRAR; Eukaryota.
DR GeneTree; ENSGT00940000159267; -.
DR HOGENOM; CLU_052285_1_0_1; -.
DR InParanoid; P07354; -.
DR OMA; NYQGRVF; -.
DR OrthoDB; 743812at2759; -.
DR PhylomeDB; P07354; -.
DR TreeFam; TF332134; -.
DR Reactome; R-GGA-3000178; ECM proteoglycans.
DR PRO; PR:P07354; -.
DR Proteomes; UP000000539; Chromosome Z.
DR Bgee; ENSGALG00000015627; Expressed in testis and 6 other tissues.
DR ExpressionAtlas; P07354; baseline and differential.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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 GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
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 1: Evidence at protein level;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Hyaluronic acid;
KW Immunoglobulin domain; Reference proteome; Repeat; Secreted.
FT PROPEP 1..9
FT /id="PRO_0000013185"
FT CHAIN 10..355
FT /note="Hyaluronan and proteoglycan link protein 1"
FT /id="PRO_0000013186"
FT DOMAIN 38..156
FT /note="Ig-like V-type"
FT DOMAIN 160..255
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 260..352
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:0000269|PubMed:1985942"
FT DISULFID 61..140
FT /evidence="ECO:0000250"
FT DISULFID 182..253
FT /evidence="ECO:0000250"
FT DISULFID 206..227
FT /evidence="ECO:0000250"
FT DISULFID 280..350
FT /evidence="ECO:0000250"
FT DISULFID 305..326
FT /evidence="ECO:0000250"
SQ SEQUENCE 355 AA; 40533 MW; 2581CAE22158B60F CRC64;
MTSLLFLVLI SVCWAEPHPD NSSLEHERII HIQEENGPRL LVVAEQAKIF SQRGGNVTLP
CKFYHEHTST AGSGTHKIRV KWTKLTSDYL KEVDVFVAMG HHRKSYGKYQ GRVFLRESSE
NDASLIITNI MLEDYGRYKC EVIEGLEDDT AVVALNLEGV VFPYSPRLGR YNLNFHEAQQ
ACLDQDSIIA SFDQLYEAWR SGLDWCNAGW LSDGSVQYPI TKPREPCGGK NTVPGVRNYG
FWDKERSRYD VFCFTSNFNG RFYYLIHPTK LTYDEAVQAC LKDGAQIAKV GQIFAAWKLL
GYDRCDAGWL ADGSVRYPIS RPRKRCSPNE AAVRFVGFPD KKHKLYGVYC FRAYN
