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HPLN1_BOVIN
ID   HPLN1_BOVIN             Reviewed;         354 AA.
AC   P55252;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 141.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cartilage;
RX   PubMed=7584851; DOI=10.1016/0305-0491(95)00073-9;
RA   Hering T.M., Kollar J., Huynh T.D., Sandell L.J.;
RT   "Bovine chondrocyte link protein cDNA sequence: interspecies conservation
RT   of primary structure and mRNA untranslated regions.";
RL   Comp. Biochem. Physiol. 112B:197-203(1995).
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; U02292; AAC04311.1; -; mRNA.
DR   PIR; A60141; A29165.
DR   RefSeq; NP_776713.1; NM_174288.1.
DR   RefSeq; XP_005209775.1; XM_005209718.2.
DR   RefSeq; XP_015327843.1; XM_015472357.1.
DR   AlphaFoldDB; P55252; -.
DR   SMR; P55252; -.
DR   STRING; 9913.ENSBTAP00000016468; -.
DR   PaxDb; P55252; -.
DR   PRIDE; P55252; -.
DR   Ensembl; ENSBTAT00000016468; ENSBTAP00000016468; ENSBTAG00000012411.
DR   Ensembl; ENSBTAT00000080855; ENSBTAP00000072384; ENSBTAG00000012411.
DR   Ensembl; ENSBTAT00000086745; ENSBTAP00000064592; ENSBTAG00000012411.
DR   GeneID; 281717; -.
DR   KEGG; bta:281717; -.
DR   CTD; 1404; -.
DR   VEuPathDB; HostDB:ENSBTAG00000012411; -.
DR   VGNC; VGNC:29749; HAPLN1.
DR   eggNOG; ENOG502QRAR; Eukaryota.
DR   GeneTree; ENSGT00940000159267; -.
DR   HOGENOM; CLU_052285_1_0_1; -.
DR   InParanoid; P55252; -.
DR   OMA; NYQGRVF; -.
DR   OrthoDB; 743812at2759; -.
DR   TreeFam; TF332134; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000012411; Expressed in Ammon's horn and 60 other tissues.
DR   ExpressionAtlas; P55252; baseline.
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   2: Evidence at transcript level;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Hyaluronic acid;
KW   Immunoglobulin domain; Reference proteome; Repeat; Secreted.
FT   PROPEP          1..15
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000013173"
FT   CHAIN           16..354
FT                   /note="Hyaluronan and proteoglycan link protein 1"
FT                   /id="PRO_0000013174"
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;  40288 MW;  065D155378A1283C CRC64;
     MKSLLLLVLI SFCWADHHSD 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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