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Database: UniProt
Entry: A0A3B4ARN5_9GOBI
LinkDB: A0A3B4ARN5_9GOBI
Original site: A0A3B4ARN5_9GOBI 
ID   A0A3B4ARN5_9GOBI        Unreviewed;       266 AA.
AC   A0A3B4ARN5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPMGP00000019803.1};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000019803.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000019803.1}
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; A0A3B4ARN5; -.
DR   STRING; 409849.ENSPMGP00000019803; -.
DR   Ensembl; ENSPMGT00000021103.1; ENSPMGP00000019803.1; ENSPMGG00000016045.1.
DR   Proteomes; UP000261520; 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   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..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..266
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017314858"
FT   DOMAIN          42..135
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DOMAIN          141..253
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DISULFID        64..133
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT   DISULFID        88..109
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ   SEQUENCE   266 AA;  30494 MW;  893DDC097FC80C8F CRC64;
     MRVWTLLWTL LWTLGLLLKE VQTWSYQNGI FHNSIWLEQA AGVYHRESRK GRYQLTYKEA
     IAVCKYEGGA LATYDQLEAA RQIGFHVCSA GWFDKGRVGY PIVKAGANCG FGKIGIIDYG
     YRLNKSERWD VYCYNPDAKE CGGVLTEPER VIQSPGFPEE YQDEQICYWH IRVKLGQRIH
     VRFLEFDVED DTDCLADYLE IYDSYDDVTG FVGRFCGDYL PYDILSTGNV MTLKFLSDAS
     VTGGGFQLLY KAVNASMVSH NKDYFN
//
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