ID A0A3Q0SS09_AMPCI Unreviewed; 256 AA.
AC A0A3Q0SS09;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Tumor necrosis factor, alpha-induced protein 6 {ECO:0000313|Ensembl:ENSACIP00000022975.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000022975.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000022975.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3Q0SS09; -.
DR STRING; 61819.ENSACIP00000022975; -.
DR Ensembl; ENSACIT00000023584.1; ENSACIP00000022975.1; ENSACIG00000017872.1.
DR GeneTree; ENSGT00940000157201; -.
DR OMA; WGFRNGI; -.
DR Proteomes; UP000261340; 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}; Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..256
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018702413"
FT DOMAIN 38..131
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 137..249
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 256 AA; 29129 MW; 7717E3763E7C8E46 CRC64;
MRVLALLWIL GFLLEEVQAW GFKNGIFHNS IWLEQAAGVY HRESRKGRYQ LTYKEAKAVC
KYEGGTLATY EQLEAARQIG FHVCAAGWFD KGRVGYPIVK PGSNCGFGKV GIIDYGYRLN
KSEKWDVYCY NPYSKECGGV LTDQQRIIQS PGFPEEYQDE QICYWHIRVR LGQKIRLHFL
EFDVEDDTAC LADYLEVYDS YDDVSGFAGR FCGDYLPDNI ISTGNVMTLK FLSDASVTAG
GFQLQYIAFN ASLPQN
//
