ID   CO5_PIG                 Reviewed;          74 AA.
AC   P01032;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Complement C5a anaphylatoxin;
GN   Name=C5;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=7372604; DOI=10.1016/s0021-9258(19)85553-9;
RA   Gerard C., Hugli T.E.;
RT   "Amino acid sequence of the anaphylatoxin from the fifth component of
RT   porcine complement.";
RL   J. Biol. Chem. 255:4710-4715(1980).
RN   [2]
RP   ACTIVE REGION.
RX   PubMed=6940191; DOI=10.1073/pnas.78.3.1833;
RA   Gerard C., Hugli T.E.;
RT   "Identification of classical anaphylatoxin as the des-Arg form of the C5a
RT   molecule: evidence of a modulator role for the oligosaccharide unit in
RT   human des-Arg74-C5a.";
RL   Proc. Natl. Acad. Sci. U.S.A. 78:1833-1837(1981).
RN   [3]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   PubMed=2337573; DOI=10.1021/bi00464a002;
RA   Williamson M.P., Madison V.S.;
RT   "Three-dimensional structure of porcine C5adesArg from 1H nuclear magnetic
RT   resonance data.";
RL   Biochemistry 29:2895-2905(1990).
CC   -!- FUNCTION: Derived from proteolytic degradation of complement C5, C5a
CC       anaphylatoxin is a mediator of local inflammatory process. Binding to
CC       the receptor C5AR1 induces a variety of responses including
CC       intracellular calcium release, contraction of smooth muscle, increased
CC       vascular permeability, and histamine release from mast cells and
CC       basophilic leukocytes. C5a is also a potent chemokine which stimulates
CC       the locomotion of polymorphonuclear leukocytes and directs their
CC       migration toward sites of inflammation. {ECO:0000250|UniProtKB:P01031}.
CC   -!- SUBUNIT: Interacts with C5AR1. {ECO:0000250|UniProtKB:P01031}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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DR   PIR; A01268; A01268.
DR   PDB; 1C5A; NMR; -; A=1-73.
DR   PDBsum; 1C5A; -.
DR   AlphaFoldDB; P01032; -.
DR   BMRB; P01032; -.
DR   SMR; P01032; -.
DR   STRING; 9823.ENSSSCP00000005908; -.
DR   MEROPS; I39.952; -.
DR   PaxDb; P01032; -.
DR   PeptideAtlas; P01032; -.
DR   PRIDE; P01032; -.
DR   eggNOG; KOG1366; Eukaryota.
DR   InParanoid; P01032; -.
DR   EvolutionaryTrace; P01032; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   CDD; cd00017; ANATO; 1.
DR   InterPro; IPR000020; Anaphylatoxin/fibulin.
DR   InterPro; IPR018081; Anaphylatoxin_comp_syst.
DR   InterPro; IPR001840; Anaphylatoxn_comp_syst_dom.
DR   Pfam; PF01821; ANATO; 1.
DR   PRINTS; PR00004; ANAPHYLATOXN.
DR   SMART; SM00104; ANATO; 1.
DR   SUPFAM; SSF47686; SSF47686; 1.
DR   PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR   PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complement alternate pathway; Complement pathway;
KW   Direct protein sequencing; Disulfide bond; Immunity; Inflammatory response;
KW   Innate immunity; Reference proteome; Secreted.
FT   CHAIN           1..74
FT                   /note="Complement C5a anaphylatoxin"
FT                   /id="PRO_0000048521"
FT   DOMAIN          21..55
FT                   /note="Anaphylatoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT   REGION          15..44
FT                   /note="Involved in C5AR1 binding"
FT                   /evidence="ECO:0000250|UniProtKB:P01031"
FT   REGION          72..74
FT                   /note="Required for 90% of C5a activity; although Arg-74 is
FT                   not essential"
FT   DISULFID        21..47
FT                   /evidence="ECO:0000269|PubMed:2337573,
FT                   ECO:0007744|PDB:1C5A"
FT   DISULFID        22..54
FT                   /evidence="ECO:0000269|PubMed:2337573,
FT                   ECO:0007744|PDB:1C5A"
FT   DISULFID        34..55
FT                   /evidence="ECO:0000269|PubMed:2337573,
FT                   ECO:0007744|PDB:1C5A"
FT   HELIX           2..11
FT                   /evidence="ECO:0007829|PDB:1C5A"
FT   HELIX           16..26
FT                   /evidence="ECO:0007829|PDB:1C5A"
FT   HELIX           34..40
FT                   /evidence="ECO:0007829|PDB:1C5A"
FT   HELIX           45..62
FT                   /evidence="ECO:0007829|PDB:1C5A"
SQ   SEQUENCE   74 AA;  8609 MW;  11AAF2E94A026EB3 CRC64;
     MLQKKIEEEA AKYKYAMLKK CCYDGAYRND DETCEERAAR IKIGPKCVKA FKDCCYIANQ
     VRAEQSHKNI QLGR