JELT_LEPLA
ID JELT_LEPLA Reviewed; 225 AA.
AC Q9PTT2;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Jeltraxin;
DE AltName: Full=Egg jelly pentraxin;
DE Flags: Precursor;
GN Name=PXN1 {ECO:0000312|EMBL:AAF21665.1};
OS Lepidobatrachus laevis (Budgett's frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Ceratophryidae; Ceratophryinae;
OC Lepidobatrachus.
OX NCBI_TaxID=8376;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF21665.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-33; 75-89; 101-109 AND
RP 120-129, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Egg jelly {ECO:0000269|PubMed:14596590}, and
RC Oviduct {ECO:0000312|EMBL:AAF21665.1};
RX PubMed=14596590; DOI=10.1021/bi035314o;
RA Peavy T.R., Hernandez C., Carroll E.J. Jr.;
RT "Jeltraxin, a frog egg jelly glycoprotein, has calcium-dependent lectin
RT properties and is related to human serum pentraxins CRP and SAP.";
RL Biochemistry 42:12761-12769(2003).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 20-39, SUBUNIT, AND GLYCOSYLATION.
RC TISSUE=Egg jelly {ECO:0000269|PubMed:1989518};
RX PubMed=1989518; DOI=10.1016/0003-9861(91)90306-4;
RA Carroll E.J. Jr., Wei S.H., Nagel G.M.;
RT "Purification, physicochemical characterization, and immunohistochemical
RT localization of a major 11.7 S glycoprotein from the jelly coats of the
RT anuran Lepidobatrachus laevis.";
RL Arch. Biochem. Biophys. 284:346-351(1991).
CC -!- FUNCTION: Calcium-dependent beta-galactose specific lectin.
CC {ECO:0000269|PubMed:14596590}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodecamer consisting of two homopentamer units. Pentraxin
CC (or pentaxin) have a discoid arrangement of 5 non-covalently bound
CC subunits. {ECO:0000269|PubMed:1989518}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14596590}.
CC -!- TISSUE SPECIFICITY: Oviduct. Highest expression levels were detected in
CC the pars convoluta with lower levels detected in the pars recta. No
CC expression was detected in the pars uterina.
CC {ECO:0000269|PubMed:14596590}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:1989518}.
CC -!- MASS SPECTROMETRY: Mass=27696; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:14596590};
CC -!- SIMILARITY: Belongs to the pentraxin family. {ECO:0000305}.
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DR EMBL; AF047712; AAF21665.1; -; mRNA.
DR AlphaFoldDB; Q9PTT2; -.
DR SMR; Q9PTT2; -.
DR PRIDE; Q9PTT2; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0016936; F:galactoside binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00152; PTX; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001759; Pentraxin-related.
DR Pfam; PF00354; Pentaxin; 1.
DR PRINTS; PR00895; PENTAXIN.
DR SMART; SM00159; PTX; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51828; PTX_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein; Lectin;
KW Metal-binding; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:14596590,
FT ECO:0000269|PubMed:1989518"
FT CHAIN 20..225
FT /note="Jeltraxin"
FT /evidence="ECO:0000269|PubMed:14596590"
FT /id="PRO_0000023555"
FT DOMAIN 21..223
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
SQ SEQUENCE 225 AA; 25618 MW; 68F3CB645AC503EC CRC64;
MKGLVIFFCL FYGCHVAGAT GKTIMLFPQK TDTDYVTLKP TERVLNQITV CLKSYTELIK
EHSLFSLAMQ GSGKDNTLLI YPYPPNNISI SIHNEDIYFK VDPEVLQWKR TCVTWDSKTG
LLQLWINGKL YPRRITKSRS PIGPQISVIL GQEQDSYGGS FDINQAFVGE MSDVNVWDYV
LPPENIKAYF SDDYTLDGNF YSWDGGNYTI NGLIVVLRNQ FIPKL
