ITLN1_XENLA
ID ITLN1_XENLA Reviewed; 339 AA.
AC Q5PPM0; Q800K0;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Intelectin-1;
DE AltName: Full=Embryonic epidermal lectin {ECO:0000303|PubMed:26755729};
DE Short=Xeel {ECO:0000303|PubMed:12802587, ECO:0000303|PubMed:26755729};
DE Flags: Precursor;
GN Name=itln1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|EMBL:AAH87616.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=12802587; DOI=10.1007/s00427-003-0341-9;
RA Nagata S., Nakanishi M., Nanba R., Fujita N.;
RT "Developmental expression of XEEL, a novel molecule of the Xenopus oocyte
RT cortical granule lectin family.";
RL Dev. Genes Evol. 213:368-370(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH87616.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION AT ASN-189, AND
RP MUTAGENESIS OF ASN-180 AND ASN-189.
RX PubMed=15537792; DOI=10.1093/glycob/cwi010;
RA Nagata S.;
RT "Isolation, characterization, and extra-embryonic secretion of the Xenopus
RT laevis embryonic epidermal lectin, XEEL.";
RL Glycobiology 15:281-290(2005).
RN [4] {ECO:0007744|PDB:4WMO, ECO:0007744|PDB:4WN0}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 51-339 IN COMPLEX WITH CALCIUM
RP IONS AND GLYCEROL 1-PHOSPHATE, FUNCTION, DISULFIDE BONDS, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=26755729; DOI=10.1074/jbc.m115.709212;
RA Wangkanont K., Wesener D.A., Vidani J.A., Kiessling L.L., Forest K.T.;
RT "Structures of Xenopus embryonic epidermal lectin reveal a conserved
RT mechanism of microbial glycan recognition.";
RL J. Biol. Chem. 291:5596-5610(2016).
CC -!- FUNCTION: Lectin that specifically recognizes microbial carbohydrate
CC chains in a calcium-dependent manner (PubMed:26755729). Binds to
CC microbial glycans that contain a terminal acyclic 1,2-diol moiety,
CC including beta-linked D-galactofuranose (beta-Galf) and D-
CC phosphoglycerol-modified glycans (PubMed:26755729). Binds to
CC S.pneumoniae serotypes with glycans that contain beta-linked D-
CC galactofuranose (beta-Galf) and with D-phosphoglycerol-modified glycans
CC (PubMed:26755729). Can bind a variety of monosaccharides (in vitro)
CC (PubMed:15537792). Probably plays a role in the defense system against
CC microorganisms (Probable). {ECO:0000269|PubMed:15537792,
CC ECO:0000269|PubMed:26755729, ECO:0000305}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked (PubMed:26755729). Homohexamer;
CC disulfide-linked (PubMed:15537792, PubMed:26755729). Forms primarily
CC homotrimers in solution, but can also form homohexamers
CC (PubMed:26755729). {ECO:0000269|PubMed:15537792,
CC ECO:0000269|PubMed:26755729}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15537792,
CC ECO:0000305|PubMed:26755729}. Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000269|PubMed:15537792}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryonic epidermal cells; expression
CC increases during neurula and tailbud stage and decreases again after 1
CC week dpf (at protein level) (PubMed:15537792). First detected in
CC gastrula-stage embryos; expression increases during later stages of
CC embryogenesis. Detected in epidermis and throughout the embryo.
CC {ECO:0000269|PubMed:12802587, ECO:0000269|PubMed:15537792}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15537792}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65329.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AB105372; BAC65329.1; ALT_INIT; mRNA.
DR EMBL; BC087616; AAH87616.1; -; mRNA.
DR RefSeq; NP_001082570.1; NM_001089101.1.
DR PDB; 4WMO; X-ray; 2.30 A; A/B/C/D/E/F=51-339.
DR PDB; 4WN0; X-ray; 2.20 A; A=51-339.
DR PDB; 5ZC0; X-ray; 2.75 A; A/B/C/D/E/F=51-339.
DR PDBsum; 4WMO; -.
DR PDBsum; 4WN0; -.
DR PDBsum; 5ZC0; -.
DR AlphaFoldDB; Q5PPM0; -.
DR SMR; Q5PPM0; -.
DR UniLectin; Q5PPM0; -.
DR iPTMnet; Q5PPM0; -.
DR DNASU; 398574; -.
DR GeneID; 398574; -.
DR KEGG; xla:398574; -.
DR CTD; 398574; -.
DR Xenbase; XB-GENE-6256033; itln1.L.
DR OrthoDB; 754383at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 398574; Expressed in neurula embryo and 16 other tissues.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0034214; P:protein hexamerization; IDA:UniProtKB.
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 3D-structure; Calcium; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW Lectin; Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..339
FT /note="Intelectin-1"
FT /id="PRO_5004261008"
FT DOMAIN 58..108
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT BINDING 112
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26755729,
FT ECO:0007744|PDB:4WMO, ECO:0007744|PDB:4WN0"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26755729,
FT ECO:0007744|PDB:4WMO, ECO:0007744|PDB:4WN0"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26755729,
FT ECO:0007744|PDB:4WMO, ECO:0007744|PDB:4WN0"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26755729,
FT ECO:0007744|PDB:4WMO, ECO:0007744|PDB:4WN0"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26755729,
FT ECO:0007744|PDB:4WMO, ECO:0007744|PDB:4WN0"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26755729,
FT ECO:0007744|PDB:4WMO, ECO:0007744|PDB:4WN0"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26755729,
FT ECO:0007744|PDB:4WMO, ECO:0007744|PDB:4WN0"
FT BINDING 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:26755729,
FT ECO:0007744|PDB:4WMO, ECO:0007744|PDB:4WN0"
FT BINDING 288..289
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000305|PubMed:26755729"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:26755729,
FT ECO:0007744|PDB:4WMO, ECO:0007744|PDB:4WN0"
FT BINDING 300
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000305|PubMed:26755729"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:26755729,
FT ECO:0007744|PDB:4WMO, ECO:0007744|PDB:4WN0"
FT BINDING 308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26755729,
FT ECO:0007744|PDB:4WMO, ECO:0007744|PDB:4WN0"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:15537792"
FT DISULFID 21
FT /note="Interchain (with C-39)"
FT /evidence="ECO:0000305|PubMed:26755729"
FT DISULFID 39
FT /note="Interchain (with C-21)"
FT /evidence="ECO:0000305|PubMed:26755729"
FT DISULFID 67..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739,
FT ECO:0007744|PDB:4WMO, ECO:0007744|PDB:4WN0"
FT DISULFID 120..306
FT /evidence="ECO:0007744|PDB:4WMO, ECO:0007744|PDB:4WN0"
FT DISULFID 225..285
FT /evidence="ECO:0007744|PDB:4WMO, ECO:0007744|PDB:4WN0"
FT DISULFID 277..291
FT /evidence="ECO:0007744|PDB:4WMO, ECO:0007744|PDB:4WN0"
FT MUTAGEN 180
FT /note="N->Q: No effect on N-glycosylation."
FT /evidence="ECO:0000269|PubMed:15537792"
FT MUTAGEN 189
FT /note="N->Q: Abolishes N-glycosylation."
FT /evidence="ECO:0000269|PubMed:15537792"
FT CONFLICT 9
FT /note="L -> F (in Ref. 1; BAC65329)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="S -> T (in Ref. 1; BAC65329)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="G -> A (in Ref. 1; BAC65329)"
FT /evidence="ECO:0000305"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:5ZC0"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:4WN0"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:4WN0"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:4WN0"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4WN0"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:4WN0"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5ZC0"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:4WN0"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:4WN0"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:4WN0"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:4WN0"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:4WN0"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:4WN0"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:4WN0"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:4WN0"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:4WN0"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:4WN0"
FT HELIX 209..215
FT /evidence="ECO:0007829|PDB:4WN0"
FT TURN 225..228
FT /evidence="ECO:0007829|PDB:4WN0"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:4WN0"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:4WN0"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:4WN0"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:4WN0"
FT STRAND 257..267
FT /evidence="ECO:0007829|PDB:4WN0"
FT STRAND 273..282
FT /evidence="ECO:0007829|PDB:4WN0"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:4WN0"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:4WN0"
FT TURN 300..305
FT /evidence="ECO:0007829|PDB:4WN0"
FT TURN 308..315
FT /evidence="ECO:0007829|PDB:4WN0"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:4WN0"
FT STRAND 332..339
FT /evidence="ECO:0007829|PDB:4WN0"
SQ SEQUENCE 339 AA; 36916 MW; 6310E126AD4AE6C8 CRC64;
MLSYSLLLLA LAFPAGHAGS CEQASISEKK EKILNLLACW TEGNADNSLS RSGGSPTGDM
NYGYRSCNEI KSSDSRAPDG IYTLATEDGE SYQTFCDMTT NGGGWTLVAS VHENNMFGKC
TVGDRWSTQQ GNMLQNPEGD GNWANYATFG LPEGATSDDY KNPGYYDIEA KNLALWHVPN
KTPMVMWRNS SILRYRTQNG FLTEEGGNLF ELYKKYPVKY DIGKCLADNG PAVPVVYDLG
SAEKTASLYS PNGRSEFTPG FVQFRAVNSE RATLALCAGV KVKGCNVEHH CIGGGGYIPE
GSPRQCGDFA ALDWDGYGTN LGWSASKQII EAAVMLFYR
