ID M7C5C8_CHEMY Unreviewed; 324 AA.
AC M7C5C8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=C-type lectin domain family 4 member E {ECO:0000313|EMBL:EMP39683.1};
GN ORFNames=UY3_03066 {ECO:0000313|EMBL:EMP39683.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP39683.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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DR EMBL; KB515918; EMP39683.1; -; Genomic_DNA.
DR AlphaFoldDB; M7C5C8; -.
DR eggNOG; KOG4297; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR033989; CD209-like_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR PANTHER; PTHR45710:SF23; C-TYPE LECTIN DOMAIN FAMILY 2 MEMBER D; 1.
DR PANTHER; PTHR45710; C-TYPE LECTIN DOMAIN-CONTAINING PROTEIN 180; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 4: Predicted;
KW Lectin {ECO:0000256|ARBA:ARBA00022734, ECO:0000313|EMBL:EMP39683.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 118..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 185..272
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 53..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 36614 MW; D7326808B44CD291 CRC64;
MPSSAVTPPP LPRPPWILQR DWRQWTAEIN PEDEVMDEEV TLVDDVENMA GLSGGMESQD
LFSTPERSTQ CQQSVSGVHD AGEERPDRQS FVQGPKQHTA PAEKSMPQSA PQKPTWRLLW
LISALLLLLC VSLLIALIVT LLKGTGGCEE HKALPQSSAE WRCVLGRAEE KGQVWTCCPM
DWEHFQSSCY YFSIDTMNWG DSETNCTGMG SHLVVINTGT EQDFIFNLTR RTVTSSPDKN
YYIGLTDQAQ EGQWRWVDQT PYNETAASGD PDYLPLSWLM KSYADVRTTG RRRFNYTQSS
FRMMVECAFG EIRQDGTAYK LFTG
//