CRP1_GADMO
ID CRP1_GADMO Reviewed; 27 AA.
AC P86688;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=C-reactive protein P1;
DE AltName: Full=C-reactive protein PI {ECO:0000303|PubMed:19081733};
DE AltName: Full=Phosphatidylcholine-binding protein {ECO:0000303|PubMed:9639088};
DE Short=Gm-PCBP {ECO:0000303|PubMed:9639088};
DE Flags: Fragment;
OS Gadus morhua (Atlantic cod).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX NCBI_TaxID=8049;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, COFACTOR, SUBUNIT, AND FUNCTION.
RC TISSUE=Serum {ECO:0000269|PubMed:9639088};
RX PubMed=9639088; DOI=10.1016/s0145-305x(97)00051-7;
RA Lund V., Olafsen J.A.;
RT "A comparative study of pentraxin-like proteins in different fish
RT species.";
RL Dev. Comp. Immunol. 22:185-194(1998).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-15, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
RP GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Serum {ECO:0000269|PubMed:19081733};
RX PubMed=19081733; DOI=10.1016/j.fsi.2008.03.015;
RA Gisladottir B., Gudmundsdottir S., Brown L., Jonsson Z.O., Magnadottir B.;
RT "Isolation of two C-reactive protein homologues from cod (Gadus morhua L.)
RT serum.";
RL Fish Shellfish Immunol. 26:210-219(2009).
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. {ECO:0000250|UniProtKB:P02741,
CC ECO:0000269|PubMed:19081733, ECO:0000269|PubMed:9639088}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P02741, ECO:0000269|PubMed:9639088};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:P02741,
CC ECO:0000269|PubMed:9639088};
CC -!- SUBUNIT: Homopentamer. Pentraxin (or pentaxin) have a discoid
CC arrangement of 5 non-covalently bound subunits. Exists as a dimer under
CC reducing conditions. {ECO:0000250|UniProtKB:P02741,
CC ECO:0000269|PubMed:19081733, ECO:0000269|PubMed:9639088}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19081733,
CC ECO:0000269|PubMed:9639088}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:19081733}.
CC -!- MISCELLANEOUS: Shows sequence similarity to serum amyloid P-component-
CC type pentraxins but binds to phosphatidylcholine.
CC {ECO:0000269|PubMed:19081733}.
CC -!- SIMILARITY: Belongs to the pentraxin family. {ECO:0000255}.
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DR AlphaFoldDB; P86688; -.
DR Proteomes; UP000694546; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR InterPro; IPR001759; Pentraxin-related.
DR PROSITE; PS51828; PTX_2; 1.
PE 1: Evidence at protein level;
KW Acute phase; Calcium; Direct protein sequencing; Reference proteome;
KW Secreted.
FT CHAIN 1..>27
FT /note="C-reactive protein P1"
FT /id="PRO_0000397241"
FT DOMAIN 6..>27
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT UNSURE 20
FT /evidence="ECO:0000269|PubMed:9639088"
FT NON_TER 27
FT /evidence="ECO:0000303|PubMed:9639088"
SQ SEQUENCE 27 AA; 3092 MW; 843AACE823CFE907 CRC64;
IPQDLSGKML TFPKEEDDDD VKLMTPK
