位置:首页 > 蛋白库 > HPLN1_RAT
HPLN1_RAT
ID   HPLN1_RAT               Reviewed;         354 AA.
AC   P03994;
DT   23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 163.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2452158; DOI=10.1016/s0021-9258(18)68749-6;
RA   Rhodes C., Doege K., Sasaki M., Yamada Y.;
RT   "Alternative splicing generates two different mRNA species for rat link
RT   protein.";
RL   J. Biol. Chem. 263:6063-6067(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 126-354.
RX   PubMed=3459153; DOI=10.1073/pnas.83.11.3761;
RA   Doege K., Hassell J.R., Caterson B., Yamada Y.;
RT   "Link protein cDNA sequence reveals a tandemly repeated protein
RT   structure.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:3761-3765(1986).
RN   [3]
RP   PROTEIN SEQUENCE OF 16-354.
RX   PubMed=2419334; DOI=10.1016/s0021-9258(17)35678-8;
RA   Neame P.J., Christner J.E., Baker J.R.;
RT   "The primary structure of link protein from rat chondrosarcoma proteoglycan
RT   aggregate.";
RL   J. Biol. Chem. 261:3519-3535(1986).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P03994-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P03994-2; Sequence=VSP_005301, VSP_005302;
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; M22340; AAA41535.1; -; Genomic_DNA.
DR   EMBL; M22336; AAA41535.1; JOINED; Genomic_DNA.
DR   EMBL; M22337; AAA41535.1; JOINED; Genomic_DNA.
DR   EMBL; M22339; AAA41535.1; JOINED; Genomic_DNA.
DR   EMBL; M22340; AAA41536.1; -; Genomic_DNA.
DR   EMBL; M22336; AAA41536.1; JOINED; Genomic_DNA.
DR   EMBL; M22338; AAA41536.1; JOINED; Genomic_DNA.
DR   EMBL; M22339; AAA41536.1; JOINED; Genomic_DNA.
DR   PIR; A28654; LKRT2.
DR   RefSeq; XP_006231810.1; XM_006231748.3. [P03994-1]
DR   AlphaFoldDB; P03994; -.
DR   SMR; P03994; -.
DR   BioGRID; 247990; 2.
DR   IntAct; P03994; 2.
DR   MINT; P03994; -.
DR   STRING; 10116.ENSRNOP00000045959; -.
DR   GlyGen; P03994; 1 site.
DR   PaxDb; P03994; -.
DR   PRIDE; P03994; -.
DR   Ensembl; ENSRNOT00000042958; ENSRNOP00000045959; ENSRNOG00000032002. [P03994-1]
DR   Ensembl; ENSRNOT00000108518; ENSRNOP00000094436; ENSRNOG00000032002. [P03994-2]
DR   GeneID; 29331; -.
DR   UCSC; RGD:2412; rat. [P03994-1]
DR   CTD; 1404; -.
DR   RGD; 2412; Hapln1.
DR   eggNOG; ENOG502QRAR; Eukaryota.
DR   GeneTree; ENSGT00940000159267; -.
DR   HOGENOM; CLU_052285_1_0_1; -.
DR   InParanoid; P03994; -.
DR   OMA; NYQGRVF; -.
DR   PhylomeDB; P03994; -.
DR   TreeFam; TF332134; -.
DR   Reactome; R-RNO-3000178; ECM proteoglycans.
DR   PRO; PR:P03994; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000032002; Expressed in frontal cortex and 4 other tissues.
DR   Genevisible; P03994; RN.
DR   GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; ISO:RGD.
DR   GO; GO:0005540; F:hyaluronic acid binding; TAS:RGD.
DR   GO; GO:0005198; F:structural molecule activity; TAS:RGD.
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   Alternative splicing; Direct protein sequencing; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Hyaluronic acid; Immunoglobulin domain;
KW   Reference proteome; Repeat; Secreted.
FT   PROPEP          1..9
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000013183"
FT   CHAIN           10..354
FT                   /note="Hyaluronan and proteoglycan link protein 1"
FT                   /id="PRO_0000013184"
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        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        61..139
FT                   /evidence="ECO:0000269|PubMed:2419334"
FT   DISULFID        181..252
FT                   /evidence="ECO:0000269|PubMed:2419334"
FT   DISULFID        205..226
FT                   /evidence="ECO:0000269|PubMed:2419334"
FT   DISULFID        279..349
FT                   /evidence="ECO:0000269|PubMed:2419334"
FT   DISULFID        304..325
FT                   /evidence="ECO:0000269|PubMed:2419334"
FT   VAR_SEQ         34..88
FT                   /note="AENGPRLLVEAEQAKVFSHRGGNVTLPCKFYRDPTAFGSGIHKIRIKWTKLT
FT                   SDY -> DCTAFWKLIRGRQRSSASPVGILTMPCCFPWRKHYTWKGIKSLKLPSLAISD
FT                   RTS (in isoform Short)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005301"
FT   VAR_SEQ         89..158
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_005302"
FT   CONFLICT        322
FT                   /note="R -> W (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   354 AA;  40262 MW;  23278AEA56273D6C CRC64;
     MRSLLFLVLI SVCRADHLSD SYTPDQDRVI HIQAENGPRL LVEAEQAKVF SHRGGNVTLP
     CKFYRDPTAF GSGIHKIRIK WTKLTSDYLR EVDVFVSMGY HKKTYGGYQG RVFLKGGSDN
     DASLIITDLT LEDYGRYKCE VIEGLEDDTA VVALELQGVV FPYFPRLGRY NLNFHEARQA
     CLDQDAVIAS FDQLYDAWRG GLDWCNAGWL SDGSVQYPIT KPREPCGGQN TVPGVRNYGF
     WDKDKSRYDV FCFTSNFNGR FYYLIHPTKL TYDEAVQACL NDGAQIAKVG QIFAAWKLLG
     YDRCDAGWLA DGSVRYPISR PRRRCSPTEA AVRFVGFPDK KHKLYGVYCF RAYN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024