MPTX_RAT
ID MPTX_RAT Reviewed; 219 AA.
AC Q6TA48;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Mucosal pentraxin;
DE Flags: Precursor;
GN Name=Mptx1; Synonyms=Mptx;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=Wistar; TISSUE=Colon;
RX PubMed=12832292; DOI=10.1096/fj.02-1036com;
RA Van Der Meer-Van Kraaij C., Van Lieshout E.M.M., Kramer E.,
RA Van Der Meer R., Keijer J.;
RT "Mucosal pentraxin (Mptx), a novel rat gene 10-fold down-regulated in colon
RT by dietary heme.";
RL FASEB J. 17:1277-1285(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC TISSUE=Colon;
RX PubMed=18850182; DOI=10.1007/s12263-007-0058-x;
RA van der Meer-van Kraaij C., Siezen R., Kramer E., Reinders M., Blokzijl H.,
RA van der Meer R., Keijer J.;
RT "Dietary modulation and structure prediction of rat mucosal pentraxin
RT (Mptx) protein and loss of function in humans.";
RL Genes Nutr. 2:275-285(2007).
RN [3]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15539406; DOI=10.1093/carcin/bgh288;
RA van der Meer-van Kraaij C., Kramer E., Jonker-Termont D., Katan M.B.,
RA van der Meer R., Keijer J.;
RT "Differential gene expression in rat colon by dietary heme and calcium.";
RL Carcinogenesis 26:73-79(2005).
RN [4]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16978845; DOI=10.1016/j.bbadis.2006.07.011;
RA Drew J.E., Farquharson A.J., Keijer J., Barrera L.N.;
RT "Complex regulation of mucosal pentraxin (Mptx) revealed by discrete micro-
RT anatomical locations in colon.";
RL Biochim. Biophys. Acta 1762:844-848(2006).
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: Homopentamer. Pentraxin (or pentaxin) have a discoid
CC arrangement of 5 non-covalently bound subunits (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expression is restricted to small intestine,
CC stomach and colon. Within colon, expressed in epithelial cells located
CC within the lower to mid region of transverse and distal crypts, but not
CC in proximal colon. {ECO:0000269|PubMed:15539406,
CC ECO:0000269|PubMed:16978845}.
CC -!- INDUCTION: Strongly down-regulated in colon by dietary heme, or by
CC dietary depletion of vitamin E. Up-regulated by calcium.
CC {ECO:0000269|PubMed:12832292, ECO:0000269|PubMed:15539406,
CC ECO:0000269|PubMed:16978845, ECO:0000269|PubMed:18850182}.
CC -!- SIMILARITY: Belongs to the pentraxin family. {ECO:0000305}.
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DR EMBL; AY426671; AAR04681.1; -; mRNA.
DR RefSeq; NP_001032731.1; NM_001037642.1.
DR RefSeq; XP_017454204.1; XM_017598715.1.
DR AlphaFoldDB; Q6TA48; -.
DR SMR; Q6TA48; -.
DR STRING; 10116.ENSRNOP00000067540; -.
DR PaxDb; Q6TA48; -.
DR Ensembl; ENSRNOT00000073147; ENSRNOP00000067540; ENSRNOG00000046165.
DR GeneID; 289243; -.
DR KEGG; rno:289243; -.
DR CTD; 649458; -.
DR RGD; 1590926; Mptx1.
DR eggNOG; ENOG502S201; Eukaryota.
DR GeneTree; ENSGT01050000244822; -.
DR HOGENOM; CLU_032051_2_0_1; -.
DR InParanoid; Q6TA48; -.
DR OMA; VCVSWES; -.
DR OrthoDB; 1088298at2759; -.
DR PhylomeDB; Q6TA48; -.
DR PRO; PR:Q6TA48; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000046165; Expressed in thymus and 12 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0001849; F:complement component C1q complex binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Metal-binding; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..219
FT /note="Mucosal pentraxin"
FT /id="PRO_0000342394"
FT DOMAIN 24..219
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
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 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT DISULFID 55..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT CONFLICT 150
FT /note="I -> V (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 219 AA; 24332 MW; 976F69731D9005E3 CRC64;
MEKLIVGTLL LTVLSGGISQ SDMDGKAFIF PQESSTAYVS LIPRVKKSLQ NFTLCLKAFT
DLTRPYSIFS YNTKTQDNEI LLFVQNSGEY MFYVGNSAAI FKAPTSLYDP VHICVNWESA
SGIAEFWLNG KPLGRKGLKK GYTVGGEAKI IIGQEQDSFG GNFDAKQSFV GEIWDVSLWD
HVIPLEEAHD SCDGGNLINF RALTYEENGY VVTKPKLWT
