ID G3TU05_LOXAF Unreviewed; 717 AA.
AC G3TU05;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Collectin-12 {ECO:0000256|ARBA:ARBA00017460};
GN Name=COLEC12 {ECO:0000313|Ensembl:ENSLAFP00000019063.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000019063.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000019063.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000019063.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000019063.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000019063.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; G3TU05; -.
DR Ensembl; ENSLAFT00000027653.1; ENSLAFP00000019063.1; ENSLAFG00000009593.3.
DR GeneTree; ENSGT00950000183074; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033989; CD209-like_CTLD.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR016187; CTDL_fold.
DR PANTHER; PTHR22803:SF146; COLLECTIN-12; 1.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lectin {ECO:0000256|ARBA:ARBA00022734}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 596..713
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 420..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 201..235
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 500..520
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..562
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 717 AA; 78757 MW; 15572FC522F678D4 CRC64;
GIQEGTQCTK CKNNWALKFS IILLYVLCAL LTITVAILGY KVVEKMDNVT GGMETSRQTY
DDKLTAVESD LKKLGDQTGK KAISTNSELS TFRSDILDLR QQLREITEKT SKNKDTLEKL
QASGEALVDR QSQLKETLEN NSFLITTVNK TLQAYNGYVT NLQQDTSVLQ GNLQNQMYSH
NVVIMNLNNL NLTQVQQRNL ITNLQRSVDD TSQAIQRIKN DFQNLQQVFL QAKKDTDWLK
EKVQSLQTLA ANNSALAKAN NDTLEDMNSQ LSSFTGQMDN ITIVSQANEQ NLKDLQDLHK
DAENRTTIKF SQLEERFQLF ETDIVNIISN ISYTAHHLRT LTSNLNEVRT TCTDTLTKHT
DDLTSLNNTL ANIRLDSVSL RMQQDMMRSR LDTEVANLSV IMEEMKLVDS KHGQLIKNFT
ILQGPPGPRG PKGDRGSQGP PGPTGNKGQK GEKGEPGPPG PAGERGPVGP AGPPGERGGK
GSKGSQGPKG SRGSPGKPGP QGPSGDPGPP GPPGKDGLPG PQGPPGFQGL QGTVGEPGVP
GPRGLPGLPG VPGLPGPKDP PGENPGERGG TQTLDGFPRP AISEESHGCL PHWKNFTDKC
YYFSVEKEIF DDAKLFCEDK SSHLVYINTR EEQQWIKKQI VGKDSHWIGL TDSEHENDWK
WLDGTSPEYK NWKAGQPDNW GHGHGPGEDC AGLIYAGQWN DFQCEDINNF ICERVRE
//
