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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//