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Tumor necrosis factor-inducible gene 6 protein (Hyaluronate-binding protein) (TNF-stimulated gene 6 protein) (TSG-6) (Tumor necrosis factor alpha-induced protein 6) (TNF alpha-induced protein 6)

 TSG6_HUMAN              Reviewed;         277 AA.
P98066; Q53TI7; Q8WWI9;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 2.
12-SEP-2018, entry version 169.
RecName: Full=Tumor necrosis factor-inducible gene 6 protein;
AltName: Full=Hyaluronate-binding protein;
AltName: Full=TNF-stimulated gene 6 protein;
Short=TSG-6;
AltName: Full=Tumor necrosis factor alpha-induced protein 6;
Short=TNF alpha-induced protein 6;
Flags: Precursor;
Name=TNFAIP6; Synonyms=TSG6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-144.
TISSUE=Fibroblast;
PubMed=1730767; DOI=10.1083/jcb.116.2.545;
Lee T.H., Wisniewski H.-G., Vilcek J.;
"A novel secretory tumor necrosis factor-inducible protein (TSG-6) is
a member of the family of hyaluronate binding proteins, closely
related to the adhesion receptor CD44.";
J. Cell Biol. 116:545-557(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11854277; DOI=10.1074/jbc.M110765200;
Nentwich H.A., Mustafa Z., Rugg M.S., Marsden B.D., Cordell M.R.,
Mahoney D.J., Jenkins S.C., Dowling B., Fries E., Milner C.M.,
Loughlin J., Day A.J.;
"A novel allelic variant of the human TSG-6 gene encoding an amino
acid difference in the CUB module. Chromosomal localization, frequency
analysis, modeling, and expression.";
J. Biol. Chem. 277:15354-15362(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-144.
TISSUE=Lung, and Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 18-27, TISSUE SPECIFICITY, AND INTERACTION WITH
INTER-ALPHA-INHIBITOR.
PubMed=7516184; DOI=10.1021/bi00189a049;
Wisniewski H.-G., Burgess W.H., Oppenheim J.D., Vilcek J.;
"TSG-6, an arthritis-associated hyaluronan binding protein, forms a
stable complex with the serum protein inter-alpha-inhibitor.";
Biochemistry 33:7423-7429(1994).
[7]
STRUCTURE BY NMR OF 36-133.
PubMed=8797823; DOI=10.1016/S0092-8674(00)80151-8;
Kohda D., Morton C.J., Parkar A.A., Hatanaka H., Inagaki F.M.,
Campbell I.D., Day A.J.;
"Solution structure of the link module: a hyaluronan-binding domain
involved in extracellular matrix stability and cell migration.";
Cell 86:767-775(1996).
-!- FUNCTION: Possibly involved in cell-cell and cell-matrix
interactions during inflammation and tumorigenesis.
-!- SUBUNIT: Interacts with inter-alpha-inhibitor (I-alpha-I).
Chondroitin sulfate may be required for the stability of the
complex. {ECO:0000269|PubMed:7516184}.
-!- INTERACTION:
P12643:BMP2; NbExp=3; IntAct=EBI-11700693, EBI-9697918;
Q99731:CCL19; NbExp=2; IntAct=EBI-11700693, EBI-11711510;
P13500:CCL2; NbExp=2; IntAct=EBI-11700693, EBI-11711396;
P80098:CCL7; NbExp=2; IntAct=EBI-11700693, EBI-11711410;
O14625:CXCL11; NbExp=2; IntAct=EBI-11700693, EBI-11711364;
P10145:CXCL8; NbExp=15; IntAct=EBI-11700693, EBI-3917999;
P02751:FN1; NbExp=8; IntAct=EBI-11700693, EBI-1220319;
P43026:GDF5; NbExp=3; IntAct=EBI-11700693, EBI-11710512;
P26022:PTX3; NbExp=8; IntAct=EBI-11700693, EBI-11574553;
O14788:TNFSF11; NbExp=4; IntAct=EBI-11700693, EBI-7404021;
-!- TISSUE SPECIFICITY: Found in the synovial fluid of patients with
rheumatoid arthritis. {ECO:0000269|PubMed:7516184}.
-!- INDUCTION: By TNF.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M31165; AAB00792.1; -; mRNA.
EMBL; AJ421518; CAD13434.1; -; mRNA.
EMBL; AJ419936; CAD12353.1; -; mRNA.
EMBL; AC009311; AAY15067.1; -; Genomic_DNA.
EMBL; CH471058; EAX11511.1; -; Genomic_DNA.
EMBL; BC030205; AAH30205.1; -; mRNA.
CCDS; CCDS2193.1; -.
PIR; A41735; A41735.
RefSeq; NP_009046.2; NM_007115.3.
UniGene; Hs.437322; -.
PDB; 1O7B; NMR; -; T=36-133.
PDB; 1O7C; NMR; -; T=36-133.
PDB; 2N40; NMR; -; A=36-133.
PDB; 2PF5; X-ray; 1.90 A; A/B/C/D/E=36-133.
PDB; 2WNO; X-ray; 2.30 A; A=129-277.
PDBsum; 1O7B; -.
PDBsum; 1O7C; -.
PDBsum; 2N40; -.
PDBsum; 2PF5; -.
PDBsum; 2WNO; -.
ProteinModelPortal; P98066; -.
SMR; P98066; -.
BioGrid; 112984; 22.
IntAct; P98066; 25.
STRING; 9606.ENSP00000243347; -.
DrugBank; DB08818; Hyaluronic acid.
iPTMnet; P98066; -.
PhosphoSitePlus; P98066; -.
BioMuta; TNFAIP6; -.
DMDM; 68067717; -.
PaxDb; P98066; -.
PeptideAtlas; P98066; -.
PRIDE; P98066; -.
ProteomicsDB; 57783; -.
DNASU; 7130; -.
Ensembl; ENST00000243347; ENSP00000243347; ENSG00000123610.
GeneID; 7130; -.
KEGG; hsa:7130; -.
UCSC; uc002txk.3; human.
CTD; 7130; -.
DisGeNET; 7130; -.
EuPathDB; HostDB:ENSG00000123610.4; -.
GeneCards; TNFAIP6; -.
HGNC; HGNC:11898; TNFAIP6.
HPA; CAB032719; -.
HPA; HPA050884; -.
MIM; 600410; gene.
neXtProt; NX_P98066; -.
OpenTargets; ENSG00000123610; -.
PharmGKB; PA36595; -.
eggNOG; KOG1218; Eukaryota.
eggNOG; KOG3714; Eukaryota.
eggNOG; ENOG410ZI1H; LUCA.
GeneTree; ENSGT00760000119025; -.
HOGENOM; HOG000043074; -.
HOVERGEN; HBG006669; -.
InParanoid; P98066; -.
KO; K19018; -.
OMA; GHLATYK; -.
OrthoDB; EOG091G09EL; -.
PhylomeDB; P98066; -.
TreeFam; TF334173; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SIGNOR; P98066; -.
ChiTaRS; TNFAIP6; human.
EvolutionaryTrace; P98066; -.
GeneWiki; TSG-6; -.
GenomeRNAi; 7130; -.
PRO; PR:P98066; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000123610; Expressed in 178 organ(s), highest expression level in layer of synovial tissue.
CleanEx; HS_TNFAIP6; -.
Genevisible; P98066; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0005540; F:hyaluronic acid binding; TAS:ProtInc.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0050728; P:negative regulation of inflammatory response; IDA:CACAO.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0030728; P:ovulation; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00041; CUB; 1.
Gene3D; 2.60.120.290; -; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR000859; CUB_dom.
InterPro; IPR000538; Link_dom.
InterPro; IPR035914; Sperma_CUB_dom_sf.
Pfam; PF00431; CUB; 1.
Pfam; PF00193; Xlink; 1.
PRINTS; PR01265; LINKMODULE.
SMART; SM00042; CUB; 1.
SMART; SM00445; LINK; 1.
SUPFAM; SSF49854; SSF49854; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS01180; CUB; 1.
PROSITE; PS01241; LINK_1; 1.
PROSITE; PS50963; LINK_2; 1.
1: Evidence at protein level;
3D-structure; Cell adhesion; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Polymorphism;
Reference proteome; Signal.
SIGNAL 1 17 {ECO:0000269|PubMed:7516184}.
CHAIN 18 277 Tumor necrosis factor-inducible gene 6
protein.
/FTId=PRO_0000026692.
DOMAIN 36 129 Link. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
DOMAIN 135 247 CUB. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
CARBOHYD 118 118 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 58 127
DISULFID 82 103
DISULFID 135 161 {ECO:0000250}.
DISULFID 188 210 {ECO:0000250}.
VARIANT 144 144 Q -> R (in dbSNP:rs1046668).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1730767}.
/FTId=VAR_013005.
STRAND 37 40 {ECO:0000244|PDB:2PF5}.
STRAND 42 44 {ECO:0000244|PDB:1O7B}.
STRAND 45 47 {ECO:0000244|PDB:2PF5}.
HELIX 51 60 {ECO:0000244|PDB:2PF5}.
HELIX 68 76 {ECO:0000244|PDB:2PF5}.
STRAND 85 87 {ECO:0000244|PDB:1O7B}.
HELIX 88 90 {ECO:0000244|PDB:2PF5}.
STRAND 91 97 {ECO:0000244|PDB:2PF5}.
TURN 101 103 {ECO:0000244|PDB:1O7B}.
STRAND 109 115 {ECO:0000244|PDB:2PF5}.
STRAND 123 128 {ECO:0000244|PDB:2PF5}.
STRAND 137 139 {ECO:0000244|PDB:2WNO}.
STRAND 141 147 {ECO:0000244|PDB:2WNO}.
TURN 149 152 {ECO:0000244|PDB:2WNO}.
STRAND 160 166 {ECO:0000244|PDB:2WNO}.
STRAND 172 181 {ECO:0000244|PDB:2WNO}.
STRAND 190 209 {ECO:0000244|PDB:2WNO}.
STRAND 211 213 {ECO:0000244|PDB:2WNO}.
STRAND 221 230 {ECO:0000244|PDB:2WNO}.
STRAND 239 247 {ECO:0000244|PDB:2WNO}.
SEQUENCE 277 AA; 31203 MW; E2B3AEB76353A782 CRC64;
MIILIYLFLL LWEDTQGWGF KDGIFHNSIW LERAAGVYHR EARSGKYKLT YAEAKAVCEF
EGGHLATYKQ LEAARKIGFH VCAAGWMAKG RVGYPIVKPG PNCGFGKTGI IDYGIRLNRS
ERWDAYCYNP HAKECGGVFT DPKQIFKSPG FPNEYEDNQI CYWHIRLKYG QRIHLSFLDF
DLEDDPGCLA DYVEIYDSYD DVHGFVGRYC GDELPDDIIS TGNVMTLKFL SDASVTAGGF
QIKYVAMDPV SKSSQGKNTS TTSTGNKNFL AGRFSHL


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