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Database: UniProt
Entry: A0A2Y9MTX6_DELLE
LinkDB: A0A2Y9MTX6_DELLE
Original site: A0A2Y9MTX6_DELLE 
ID   A0A2Y9MTX6_DELLE        Unreviewed;       277 AA.
AC   A0A2Y9MTX6;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Tumor necrosis factor-inducible gene 6 protein isoform X2 {ECO:0000313|RefSeq:XP_022425410.1};
GN   Name=TNFAIP6 {ECO:0000313|RefSeq:XP_022425410.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022425410.1};
RN   [1] {ECO:0000313|RefSeq:XP_022425410.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022425410.1};
RG   RefSeq;
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   RefSeq; XP_022425410.1; XM_022569702.1.
DR   AlphaFoldDB; A0A2Y9MTX6; -.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
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:UP000248483};
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_5016089174"
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"
SQ   SEQUENCE   277 AA;  31203 MW;  C4AA7F9AB1C48D2F CRC64;
     MIILIYLFVL LWEEAHGWGF RNGIFHNSIW LEQAAGVYHR EARSGKYKLT YAEAKAVCEY
     EGGHLATYKQ LEAARKIGFH ICAAGWMAKG RVGYPIVKPG PNCGFGKTGI IDYGVRLNRS
     ERWDAYCYNP HAKECGGVFT DPKQIFKTPG FPNEYDDNQI CYWHIRLKYG QRIHLSFLDF
     DLEDDPACLA DYVEIYDSYD DVHGFVGRYC GDELPEDIIS TGNVMTLKFL SDASVTAGGF
     QIKYVAVDPL SKSSQGKNTS TTSPGNKNFL AGRFSHL
//
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