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Database: UniProt
Entry: A0A2U9BP18_SCOMX
LinkDB: A0A2U9BP18_SCOMX
Original site: A0A2U9BP18_SCOMX 
ID   A0A2U9BP18_SCOMX        Unreviewed;       489 AA.
AC   A0A2U9BP18;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Putative CD209 antigen-like {ECO:0000313|EMBL:AWP05888.1};
GN   ORFNames=SMAX5B_007596 {ECO:0000313|EMBL:AWP05888.1};
OS   Scophthalmus maximus (Turbot) (Psetta maxima).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC   Scophthalmus.
OX   NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP05888.1, ECO:0000313|Proteomes:UP000246464};
RN   [1] {ECO:0000313|EMBL:AWP05888.1, ECO:0000313|Proteomes:UP000246464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Martinez P.;
RT   "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT   evaluation of genetic and physical mapping variation across individuals.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP026250; AWP05888.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U9BP18; -.
DR   STRING; 52904.ENSSMAP00000029375; -.
DR   Proteomes; UP000246464; Chromosome 8.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 2.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR033989; CD209-like_CTLD.
DR   InterPro; IPR016187; CTDL_fold.
DR   PANTHER; PTHR45710; C-TYPE LECTIN DOMAIN-CONTAINING PROTEIN 180; 1.
DR   PANTHER; PTHR45710:SF8; EARLY ACTIVATION ANTIGEN CD69; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 2.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        28..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        286..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          148..266
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          90..131
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          315..349
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   489 AA;  56341 MW;  E58C32FAD41EA652 CRC64;
     MEMPDYINQQ PSHEQKCSSN TDRTETRILQ VLFLSFGVLC MVQAILNVSL RLTLHSNQVS
     TASLCNTTTL GVQNQKEEGN IDSERKNTLC NSLQKRVNDL TGVKNLLENK ISELNNKIKR
     LEEEKDRLSA LSGCGSSSKR CPANWIEMNR RCYFMSSERR TWDDSRTDCQ IKGADLVVIN
     SELEQNALYR LYGDPLLLFW IGLRNTDRTF RWVDGSALNK LFWQPGQPDS VGFLNREDCV
     EMNLRDPVEA SWNDAPCGQH RRWLCEKDPP NSANEPSGKK NVVRPAVMFL VLLCLLLLAV
     VIVLVVLWIQ EKSLSDNQTT ERDELQTRYD EMERLNDNLT RKTNRLEGDI DLLMVIQINL
     TKQRDELQKQ LDDSLSRHEL SKVFEVGDLG SSECSQNIRG YDNVMNNFSM TSKLFLEKGF
     LFNCSEIKRT SAYSYKKMSF CPDPWMRFDN SCYFSPTMEK NWFDSKAYCE IQNSTLVIIS
     SLNEHVLGE
//
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