ID I3K7U4_ORENI Unreviewed; 249 AA.
AC I3K7U4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Tumor necrosis factor, alpha-induced protein 6 {ECO:0000313|Ensembl:ENSONIP00000017189.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000017189.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Ensembl:ENSONIP00000017189.2}
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 AlphaFoldDB; I3K7U4; -.
DR Ensembl; ENSONIT00000017204.2; ENSONIP00000017189.2; ENSONIG00000013664.2.
DR eggNOG; KOG1218; Eukaryota.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000157201; -.
DR TreeFam; TF334173; -.
DR Proteomes; UP000005207; 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:UP000005207};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..249
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025646254"
FT DOMAIN 38..131
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 137..248
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 60..129
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 84..105
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ SEQUENCE 249 AA; 28594 MW; EC0620C15B28A5BB CRC64;
MRVLALLWIL GFVLKEVEAW SYSNGIFHNS IWLEQAAGVY HRESRKGRYQ LTYKEAKAVC
KYEGGTLATY EQLEAARQIG FHVCAAGWFD KGRVGYPIVK PGSNCGFGKV GIIDYGYRLN
KSERWDVYCY NPNSKECGGV LTEQQKIIQS PGFPEEYEDE QICYWHIRVR LGQKIRLHFM
EFDVEDDTEC LADYLEVYDS YDDVSGFAGR FCGDYLPDDI ISTGESPHIF TSKEHKETFG
FTAIQNICL
//
