ID A0A2Y9DEX0_TRIMA Unreviewed; 274 AA.
AC A0A2Y9DEX0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Collectin-11 {ECO:0000256|ARBA:ARBA00040130};
GN Name=LOC101354743 {ECO:0000313|RefSeq:XP_004373140.2};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004373140.2};
RN [1] {ECO:0000313|RefSeq:XP_004373140.2}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the COLEC10/COLEC11 family.
CC {ECO:0000256|ARBA:ARBA00038195}.
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DR RefSeq; XP_004373140.2; XM_004373083.2.
DR AlphaFoldDB; A0A2Y9DEX0; -.
DR STRING; 127582.A0A2Y9DEX0; -.
DR KEGG; tmu:101354743; -.
DR InParanoid; A0A2Y9DEX0; -.
DR OrthoDB; 4835894at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IEA:UniProt.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0050778; P:positive regulation of immune response; IEA:UniProt.
DR CDD; cd03591; CLECT_collectin_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; IPR008160; Collagen.
DR InterPro; IPR033990; Collectin_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR PANTHER; PTHR22801:SF60; COLLECTIN SUBFAMILY MEMBER 11; 1.
DR PANTHER; PTHR22801; LITHOSTATHINE; 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 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..274
FT /note="Collectin-11"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015846573"
FT DOMAIN 152..268
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 47..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 274 AA; 29611 MW; 6ECFF72DAFD2F7CA CRC64;
MLIMKRDLAF LGTLISLTFL SLLRSGYPQQ TAEETCSMQI LVPGLKGDAG EKGEKGAPGR
PGRVGPTGEK GDMGDKGQKG GVGRHGKIGP IGSKGQKGDS GDIGPPGLNG EPGIPCECSQ
LRKAIGEMDN QVTQLTTELK FIKNAVAGVR ETDNKIYLLV KEEKRYVDAQ LSCQGRGGML
SMPKDETSNG LIASYITQAG LTRVFIGIND LEKEGTFVYS DRSPMQTFSK WRNGEPNNAY
DEEDCVEMVA SGGWNDVACH ITMYFICEFD KENV
//
