ID   CO5_BOVIN               Reviewed;          74 AA.
AC   P12082;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Complement C5a anaphylatoxin;
GN   Name=C5;
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   PROTEIN SEQUENCE.
RX   PubMed=3081348; DOI=10.1111/j.1432-1033.1986.tb09460.x;
RA   Gennaro R., Simonic T., Negri A., Mottola C., Secchi C., Ronchi S.,
RA   Romeo D.;
RT   "C5a fragment of bovine complement. Purification, bioassays, amino-acid
RT   sequence and other structural studies.";
RL   Eur. J. Biochem. 155:77-86(1986).
RN   [2]
RP   STRUCTURE BY NMR.
RX   PubMed=3262536; DOI=10.1016/0014-5793(88)80499-x;
RA   Zarbock J., Gennaro R., Romeo D., Clore G.M., Gronenborn A.M.;
RT   "A proton nuclear magnetic resonance study of the conformation of bovine
RT   anaphylatoxin C5a in solution.";
RL   FEBS Lett. 238:289-294(1988).
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; A25408; A25408.
DR   AlphaFoldDB; P12082; -.
DR   SMR; P12082; -.
DR   STRING; 9913.ENSBTAP00000016204; -.
DR   MEROPS; I39.952; -.
DR   PRIDE; P12082; -.
DR   eggNOG; KOG1366; Eukaryota.
DR   InParanoid; P12082; -.
DR   OrthoDB; 20179at2759; -.
DR   Proteomes; UP000009136; 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   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_0000048520"
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   DISULFID        21..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT   DISULFID        22..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT   DISULFID        34..55
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
SQ   SEQUENCE   74 AA;  8517 MW;  C09DF742D12D70F6 CRC64;
     MLKKKIEEEA AKYRNAWVKK CCYDGAHRND DETCEERAAR IAIGPECIKA FKSCCAIASQ
     FRADEHHKNM QLGR