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TSG6_RABIT
ID   TSG6_RABIT              Reviewed;         276 AA.
AC   P98065;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Tumor necrosis factor-inducible gene 6 protein;
DE            EC=3.1.1.- {ECO:0000250|UniProtKB:P98066};
DE   AltName: Full=Hyaluronate-binding protein PS4;
DE   AltName: Full=TNF-stimulated gene 6 protein;
DE            Short=TSG-6;
DE   AltName: Full=Tumor necrosis factor alpha-induced protein 6;
DE            Short=TNF alpha-induced protein 6;
DE   Flags: Precursor;
GN   Name=TNFAIP6; Synonyms=PS4, TSG6;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   INDUCTION BY GROWTH FACTORS.
RC   STRAIN=New Zealand white;
RX   PubMed=8098034; DOI=10.1016/s0021-9258(18)98362-6;
RA   Feng P., Liau G.;
RT   "Identification of a novel serum and growth factor-inducible gene in
RT   vascular smooth muscle cells.";
RL   J. Biol. Chem. 268:9387-9392(1993).
RN   [2]
RP   ERRATUM OF PUBMED:8098034.
RX   PubMed=8407990; DOI=10.1016/s0021-9258(19)36946-7;
RA   Feng P., Liau G.;
RL   J. Biol. Chem. 268:21453-21453(1993).
CC   -!- FUNCTION: Major regulator of extracellular matrix organization during
CC       tissue remodeling (By similarity). Catalyzes the transfer of a heavy
CC       chain (HC) from inter-alpha-inhibitor (I-alpha-I) complex to
CC       hyaluronan. Cleaves the ester bond between the C-terminus of the HC and
CC       GalNAc residue of the chondroitin sulfate chain in I-alpha-I complex
CC       followed by transesterification of the HC to hyaluronan. In the
CC       process, potentiates the antiprotease function of I-alpha-I complex
CC       through release of free bikunin (By similarity). Acts as a catalyst in
CC       the formation of hyaluronan-HC oligomers and hyaluronan-rich matrix
CC       surrounding the cumulus cell-oocyte complex, a necessary step for
CC       oocyte fertilization (By similarity). Assembles hyaluronan in
CC       pericellular matrices that serve as platforms for receptor clustering
CC       and signaling. Enables binding of hyaluronan deposited on the surface
CC       of macrophages to LYVE1 on lymphatic endothelium and facilitates
CC       macrophage extravasation. Alters hyaluronan binding to functionally
CC       latent CD44 on vascular endothelium, switching CD44 into an active
CC       state that supports leukocyte rolling (By similarity). Modulates the
CC       interaction of chemokines with extracellular matrix components and
CC       proteoglycans on endothelial cell surface, likely preventing chemokine
CC       gradient formation. In a negative feedback mechanism, may limit
CC       excessive neutrophil recruitment at inflammatory sites by antagonizing
CC       the association of CXCL8 with glycosaminoglycans on vascular
CC       endothelium (By similarity). Has a role in osteogenesis and bone
CC       remodeling. Inhibits BMP2-dependent differentiation of mesenchymal stem
CC       cell to osteoblasts. Protects against bone erosion during inflammation
CC       by inhibiting TNFSF11/RANKL-dependent osteoclast activation (By
CC       similarity). {ECO:0000250|UniProtKB:O08859,
CC       ECO:0000250|UniProtKB:P98066}.
CC   -!- SUBUNIT: Interacts (via Link domain) with inter-alpha-inhibitor (I-
CC       alpha-I) component bikunin. Interacts with ITIH2/HC2; this interaction
CC       is required for transesterification of the HC to hyaluronan. Interacts
CC       (via Link and CUB domains) with ITIH1. Chondroitin sulfate may be
CC       required for the stability of the complex. Interacts (via Link domain)
CC       with various C-X-C and C-C chemokines including PF4, CXCL8, CXCL11,
CC       CXCL12, CCL2, CCL7, CCL19, CCL21, and CCL27; this interaction
CC       interferes with chemokine binding to glycosaminoglycans. Interacts
CC       (primarily via Link domain) with BMP2; this interaction is inhibited by
CC       hyaluronan. Interacts (via both Link and CUB domains) with TNFSF11.
CC       Interacts (via CUB domain) with FN1 (via type III repeats 9-14); this
CC       interaction enhances fibronectin fibril assembly. TNFAIP6 may act as a
CC       bridging molecule between FN1 and THBS1.
CC       {ECO:0000250|UniProtKB:P98066}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P98066}.
CC   -!- TISSUE SPECIFICITY: Vascular smooth muscle cells.
CC       {ECO:0000269|PubMed:8098034}.
CC   -!- DEVELOPMENTAL STAGE: Fetal skeletal muscle, esophagus, kidney, and
CC       lung. {ECO:0000269|PubMed:8098034}.
CC   -!- INDUCTION: By serum and growth factors. {ECO:0000269|PubMed:8098034}.
CC   -!- DOMAIN: The Link domain interacts with various extracellular matrix
CC       components, including heparin, heparan sulfates, hyaluronan and I-
CC       alpha-I complex. It is required for binding to various chemokines.
CC       {ECO:0000250|UniProtKB:P98066}.
CC   -!- DOMAIN: The CUB domain is necessary for calcium ion binding and
CC       transesterification reaction. It is required for binding to FN1.
CC       {ECO:0000250|UniProtKB:P98066}.
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DR   EMBL; M86381; AAA03342.1; -; mRNA.
DR   PIR; A48055; A47290.
DR   RefSeq; NP_001075780.1; NM_001082311.1.
DR   AlphaFoldDB; P98065; -.
DR   BMRB; P98065; -.
DR   SMR; P98065; -.
DR   STRING; 9986.ENSOCUP00000011779; -.
DR   PRIDE; P98065; -.
DR   Ensembl; ENSOCUT00000013688; ENSOCUP00000011779; ENSOCUG00000013688.
DR   GeneID; 100009149; -.
DR   KEGG; ocu:100009149; -.
DR   CTD; 7130; -.
DR   eggNOG; KOG1218; Eukaryota.
DR   eggNOG; KOG3714; Eukaryota.
DR   GeneTree; ENSGT00940000157201; -.
DR   HOGENOM; CLU_092089_0_0_1; -.
DR   InParanoid; P98065; -.
DR   OMA; DDTACMA; -.
DR   OrthoDB; 934805at2759; -.
DR   TreeFam; TF334173; -.
DR   Proteomes; UP000001811; Chromosome 7.
DR   Bgee; ENSOCUG00000013688; Expressed in ovary and 11 other tissues.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0001968; F:fibronectin binding; ISS:UniProtKB.
DR   GO; GO:0005540; F:hyaluronic acid binding; ISS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:1905590; P:fibronectin fibril organization; ISS:UniProtKB.
DR   GO; GO:0030212; P:hyaluronan metabolic process; ISS:UniProtKB.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0090024; P:negative regulation of neutrophil chemotaxis; ISS:UniProtKB.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB.
DR   GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISS:UniProtKB.
DR   GO; GO:0001550; P:ovarian cumulus expansion; ISS:UniProtKB.
DR   GO; GO:1903911; P:positive regulation of receptor clustering; ISS:UniProtKB.
DR   CDD; cd00041; CUB; 1.
DR   Gene3D; 2.60.120.290; -; 1.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR000538; Link_dom.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF00193; Xlink; 1.
DR   PRINTS; PR01265; LINKMODULE.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00445; LINK; 1.
DR   SUPFAM; SSF49854; SSF49854; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS01241; LINK_1; 1.
DR   PROSITE; PS50963; LINK_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Disulfide bond; Glycoprotein; Hydrolase;
KW   Metal-binding; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..276
FT                   /note="Tumor necrosis factor-inducible gene 6 protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026694"
FT   DOMAIN          36..129
FT                   /note="Link"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT   DOMAIN          135..247
FT                   /note="CUB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   BINDING         183
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P98066"
FT   BINDING         191
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P98066"
FT   BINDING         232
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P98066"
FT   BINDING         234
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P98066"
FT   BINDING         235
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P98066"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        58..127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT   DISULFID        82..103
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT   DISULFID        135..161
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   DISULFID        188..210
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
SQ   SEQUENCE   276 AA;  31081 MW;  3BDC5D9A24B2F75A CRC64;
     MIILIYLFVL VWEEAQGWGF KNGIFHNSIW LEQAAGVYHR EARSGKYKLT YAEAKAVCEF
     EGGRLATYKQ LEAARKIGFH VCAAGWMAKG RVGYPIVKPG SNCGFGKTGI IDYGIRLNRS
     ERWDAYCYNP HAKECGGVFT DPKRIFKSPG FPNEYDDNQI CYWHIRLKYG QRIHLSFLNF
     DLEYDPGCLA DYVEIYDSYD DVHGFVGRYC GDELPEDIIS TGNVMTLKFL SDASVTAGGF
     QIKYVTVDPA SKSSQGKNTS TVSGNKNFLA GRFSHL
 
 
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