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Database: UniProt
Entry: G5BWM1_HETGA
LinkDB: G5BWM1_HETGA
Original site: G5BWM1_HETGA 
ID   G5BWM1_HETGA            Unreviewed;       225 AA.
AC   G5BWM1;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Pentraxin family member {ECO:0000256|RuleBase:RU362112};
GN   ORFNames=GW7_00542 {ECO:0000313|EMBL:EHB13682.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB13682.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHB13682.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
CC   -!- FUNCTION: Displays several functions associated with host defense: it
CC       promotes agglutination, bacterial capsular swelling, phagocytosis and
CC       complement fixation through its calcium-dependent binding to
CC       phosphorylcholine. Can interact with DNA and histones and may scavenge
CC       nuclear material released from damaged circulating cells.
CC       {ECO:0000256|ARBA:ARBA00037561}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|RuleBase:RU362112};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000256|RuleBase:RU362112};
CC   -!- SUBUNIT: Homopentamer. Pentaxin (or pentraxin) have a discoid
CC       arrangement of 5 non-covalently bound subunits.
CC       {ECO:0000256|RuleBase:RU362112}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362112}.
CC   -!- SIMILARITY: Belongs to the pentraxin family.
CC       {ECO:0000256|ARBA:ARBA00038102, ECO:0000256|RuleBase:RU362112}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01172}.
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DR   EMBL; JH172217; EHB13682.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5BWM1; -.
DR   STRING; 10181.G5BWM1; -.
DR   Ensembl; ENSHGLT00000021200; ENSHGLP00000020997; ENSHGLG00000015003.
DR   Ensembl; ENSHGLT00100008797; ENSHGLP00100008695; ENSHGLG00100006473.
DR   eggNOG; ENOG502S201; Eukaryota.
DR   InParanoid; G5BWM1; -.
DR   OMA; MEKLLWC; -.
DR   Proteomes; UP000006813; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR   GO; GO:0001849; F:complement component C1q complex binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0030169; F:low-density lipoprotein particle binding; IEA:Ensembl.
DR   GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IEA:Ensembl.
DR   GO; GO:0010888; P:negative regulation of lipid storage; IEA:Ensembl.
DR   GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
DR   GO; GO:0032945; P:negative regulation of mononuclear cell proliferation; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0032677; P:regulation of interleukin-8 production; IEA:Ensembl.
DR   GO; GO:0042310; P:vasoconstriction; IEA:Ensembl.
DR   CDD; cd00152; PTX; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001759; Pentraxin-related.
DR   PANTHER; PTHR45869:SF7; C-REACTIVE PROTEIN; 1.
DR   PANTHER; PTHR45869; C-REACTIVE PROTEIN-RELATED; 1.
DR   Pfam; PF00354; Pentaxin; 1.
DR   PRINTS; PR00895; PENTAXIN.
DR   SMART; SM00159; PTX; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51828; PTX_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU362112};
KW   Metal-binding {ECO:0000256|RuleBase:RU362112};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW   Signal {ECO:0000256|RuleBase:RU362112}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU362112"
FT   CHAIN           20..225
FT                   /note="Pentraxin family member"
FT                   /evidence="ECO:0000256|RuleBase:RU362112"
FT                   /id="PRO_5005132374"
SQ   SEQUENCE   225 AA;  25453 MW;  8E48DAB5AB97B9EF CRC64;
     MEKLLWCFLI LISLSDVFGQ KDMSKKTFVF PKESDNAYVS LKAQLKKPLN AFTVCLRFYT
     DLFTTRGYSI FSYATKKHDN EILVFWSKDR GYLLGVGGLE VPFKALEIPM APVHICANWE
     SISGIIELWV DGKPQVRKSL QKGYSVGTEA IIILGQDQDS FGGRFDANQS LVGDIGDVNM
     WDFVLSPEEI STVYASGTFS PNVLDWRALR FETHGEVFIK PQLWA
//
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