ID D2HLK3_AILME Unreviewed; 277 AA.
AC D2HLK3;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=TNF alpha induced protein 6 {ECO:0000313|Ensembl:ENSAMEP00000013712.1};
DE Flags: Fragment;
GN Name=TNFAIP6 {ECO:0000313|Ensembl:ENSAMEP00000013712.1};
GN ORFNames=PANDA_012383 {ECO:0000313|EMBL:EFB21913.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB21913.1};
RN [1] {ECO:0000313|EMBL:EFB21913.1, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000013712.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR EMBL; GL193011; EFB21913.1; -; Genomic_DNA.
DR RefSeq; XP_002923271.1; XM_002923225.3.
DR STRING; 9646.ENSAMEP00000013712; -.
DR Ensembl; ENSAMET00000014283.2; ENSAMEP00000013712.1; ENSAMEG00000013023.2.
DR GeneID; 100480256; -.
DR KEGG; aml:100480256; -.
DR CTD; 7130; -.
DR eggNOG; KOG1218; Eukaryota.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000157201; -.
DR HOGENOM; CLU_092089_0_0_1; -.
DR OMA; WGFRNGI; -.
DR OrthoDB; 3019692at2759; -.
DR TreeFam; TF334173; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0106435; F:carboxylesterase activity; IEA:Ensembl.
DR GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:1905590; P:fibronectin fibril organization; IEA:Ensembl.
DR GO; GO:0030212; P:hyaluronan metabolic process; IEA:Ensembl.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0090024; P:negative regulation of neutrophil chemotaxis; IEA:Ensembl.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0001550; P:ovarian cumulus expansion; IEA:Ensembl.
DR GO; GO:1903911; P:positive regulation of receptor clustering; IEA:Ensembl.
DR CDD; cd00041; CUB; 1.
DR CDD; cd03515; Link_domain_TSG_6_like; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 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 PANTHER; PTHR46908; CUBILIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR46908:SF8; TUMOR NECROSIS FACTOR-INDUCIBLE GENE 6 PROTEIN; 1.
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; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01241; LINK_1; 1.
DR PROSITE; PS50963; LINK_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00323}; Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..277
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015088345"
FT DOMAIN 36..129
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 135..247
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 58..127
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 82..103
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT NON_TER 277
FT /evidence="ECO:0000313|EMBL:EFB21913.1"
SQ SEQUENCE 277 AA; 31142 MW; 0EFE892675E1C875 CRC64;
MIILTYLFVL LWEEAHGWGF KNGIFHNSIW LEQAAGVYHR EARSGKYKLT YAEAKAVCEY
EGGQLATYKQ LEAARKIGFH VCAAGWMAKG RVGYPIVKPG PNCGFGKTGI IDYGVRLNRS
ERWDAYCYNP HAKECGGVFT DPKRIFKSPG FPNEYDDNQI CYWHIRLKYG QRIHLSFLDF
DLEDDPACLA DYVEIYDSYD DVHGFVGRFC GDELPEDIVS TGNVMTLKFL SDASVTAGGF
QIKYVALDPL SKSSQGKNTS TTSTGNKNFL AGRFSHL
//
