ID   PTX3_BOVIN              Reviewed;         382 AA.
AC   Q0VCG9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Pentraxin-related protein PTX3;
DE   AltName: Full=Pentaxin-related protein PTX3;
DE   Flags: Precursor;
GN   Name=PTX3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in the regulation of innate resistance to
CC       pathogens, inflammatory reactions, possibly clearance of self-
CC       components and female fertility. {ECO:0000250}.
CC   -!- SUBUNIT: Homooctamer; disulfide-linked. Binds to C1q (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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DR   EMBL; BC120175; AAI20176.1; -; mRNA.
DR   RefSeq; NP_001069727.1; NM_001076259.2.
DR   AlphaFoldDB; Q0VCG9; -.
DR   SMR; Q0VCG9; -.
DR   STRING; 9913.ENSBTAP00000011863; -.
DR   PaxDb; Q0VCG9; -.
DR   GeneID; 541148; -.
DR   KEGG; bta:541148; -.
DR   CTD; 5806; -.
DR   eggNOG; ENOG502QUBX; Eukaryota.
DR   InParanoid; Q0VCG9; -.
DR   OrthoDB; 770812at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0045087; P:innate immune response; IEA:InterPro.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR030476; Pentaxin_CS.
DR   InterPro; IPR001759; Pentraxin-related.
DR   InterPro; IPR042837; PTX3.
DR   PANTHER; PTHR46943; PTHR46943; 1.
DR   Pfam; PF00354; Pentaxin; 1.
DR   PRINTS; PR00895; PENTAXIN.
DR   SMART; SM00159; PTX; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00289; PTX_1; 1.
DR   PROSITE; PS51828; PTX_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..382
FT                   /note="Pentraxin-related protein PTX3"
FT                   /id="PRO_0000313023"
FT   DOMAIN          180..382
FT                   /note="Pentraxin (PTX)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   COILED          79..137
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        47
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        49
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        103
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        180..358
FT                   /evidence="ECO:0000250"
FT   DISULFID        211..272
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   DISULFID        318
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        319
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   382 AA;  42021 MW;  E67E249979D74AD6 CRC64;
     MHISVILFCA LWSAVSAENS DDYELMYVNL DNEIDNGLHP TEDPTPCDCS RENSEWDKLF
     TMLENSQMRE GMLLQATDVM LRGELQKLQA ELGRLEGSLQ KLCGPEAPSE TRLARALDDL
     LQASRDAGRR LARLEDAGAL RPQEEAGRAL GAVLEELRRT RADLRAVQGW AASRWLPAGC
     ETAILFPMRS KKIFASVHPV TPMKLETFSA CIWVKATEVL NKTVLFSYGT KRNPYEIQLY
     LSYRSIMLVV GGEENRLVAD AVISLGTWTH LCSTWDSKKG HMALWVNGDS VATAVDMATG
     HVVPEGGILQ IGQEKNGCCV GGGFDETLAF SGRLTGFNIW EGVLSNEEIR EAGGAESCHI
     RGNVVGWGVT EIQPHGGAQY VY