ITLN_ONCMY
ID ITLN_ONCMY Reviewed; 325 AA.
AC P0DMV4;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2015, sequence version 1.
DT 03-AUG-2022, entry version 10.
DE RecName: Full=Intelectin {ECO:0000303|PubMed:18502147};
DE Short=RTInt {ECO:0000303|PubMed:18502147};
DE Flags: Precursor;
GN Name=itln {ECO:0000305};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 116-124; 145-152; 272-287
RP AND 318-325, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18502147; DOI=10.1016/j.fsi.2008.02.018;
RA Russell S., Young K.M., Smith M., Hayes M.A., Lumsden J.S.;
RT "Identification, cloning and tissue localization of a rainbow trout
RT (Oncorhynchus mykiss) intelectin-like protein that binds bacteria and
RT chitin.";
RL Fish Shellfish Immunol. 25:91-105(2008).
CC -!- FUNCTION: May be involved in innate immune surveillance. May
CC specifically recognize carbohydrate chains of pathogens and bacterial
CC components in a calcium-dependent manner. In vitro binds N-
CC acetylglucosamine residues. {ECO:0000305|PubMed:18502147}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in caudal kidney, liver,
CC and swim bladder. Also expressed in gill, spleen, intestine and head
CC kidney. Not detected in heart. {ECO:0000269|PubMed:18502147}.
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DR AlphaFoldDB; P0DMV4; -.
DR SMR; P0DMV4; -.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0008061; F:chitin binding; IDA:AgBase.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:AgBase.
DR GO; GO:0005537; F:mannose binding; IDA:AgBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Lectin; Metal-binding;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..325
FT /note="Intelectin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433020"
FT DOMAIN 44..266
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 101
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q5PPM0"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 274..275
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 286
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 294
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT DISULFID 53..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 106..292
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT DISULFID 262..277
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
SQ SEQUENCE 325 AA; 36087 MW; D6CC5948083C75E3 CRC64;
MKYCVLLIMI HLLLVELPQF PEALQGNVYA AAPVVAATDL RLRIRSSYIG RSCKEIRDRY
NQHEDGLYYL STASGTVYQT FCDMTTAGGG WTLVASVHEN NVYGKCTMGD RWSSQQGSNP
NWPDGDGNWA NRATFGTAEG ATSDDFKNPG YYDIVAEDIS VWHVPNNSPM EHWNLGAILR
YHTERSFLSI QGGNLHQLFK LYPVRYNAEA SGNTGPVIPI VYDFGDKETT RELYGPNTRN
QFEPGFITFR PINNELAAMA ICSGVKPTTG GDTEHYCIGG GGHFPEGAPR QCGDFPAFDW
NGYGTNTEWS ASKQLTEAAV LLFYR
