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Complement C5 [Cleaved into: C5a anaphylatoxin] (Fragment)

 CO5_RAT                 Reviewed;          77 AA.
P08650; Q63078;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 2.
23-MAY-2018, entry version 123.
RecName: Full=Complement C5;
Contains:
RecName: Full=C5a anaphylatoxin;
Flags: Fragment;
Name=C5;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
PROTEIN SEQUENCE.
Cui L.-X., Ferreri K., Hugli T.E.;
"Characterization of rat C5a, a uniquely active spasmogen.";
Complement 2:18-19(1985).
[2]
PROTEIN SEQUENCE, AND CHARACTERIZATION.
TISSUE=Serum;
PubMed=7987212; DOI=10.1002/pro.5560030803;
Cui L.-X., Carney D.F., Hugli T.E.;
"Primary structure and functional characterization of rat C5a: an
anaphylatoxin with unusually high potency.";
Protein Sci. 3:1169-1177(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Brown Norway, Lewis, and Wistar; TISSUE=Liver;
PubMed=9116048; DOI=10.1016/S0167-4781(97)00006-7;
Rothermel E., Rolf O., Goetze O., Zwirner J.;
"Nucleotide and corrected amino acid sequence of the functional
recombinant rat anaphylatoxin C5a.";
Biochim. Biophys. Acta 1351:9-12(1997).
-!- FUNCTION: Derived from proteolytic degradation of complement C5,
C5 anaphylatoxin is a mediator of local inflammatory process.
Binding to the receptor C5AR1 induces a variety of responses
including intracellular calcium release, contraction of smooth
muscle, increased vascular permeability, and histamine release
from mast cells and basophilic leukocytes. C5a is also a potent
chemokine which stimulates the locomotion of polymorphonuclear
leukocytes and directs their migration toward sites of
inflammation. {ECO:0000250|UniProtKB:P01031}.
-!- SUBUNIT: The C5a anaphylatoxin interacts with C5AR1.
{ECO:0000250|UniProtKB:P01031}.
-!- SUBCELLULAR LOCATION: Secreted.
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EMBL; X91892; CAA62994.1; -; mRNA.
PIR; A57689; A57689.
UniGene; Rn.21259; -.
ProteinModelPortal; P08650; -.
SMR; P08650; -.
STRING; 10116.ENSRNOP00000025534; -.
PaxDb; P08650; -.
PRIDE; P08650; -.
UCSC; RGD:2237; rat.
RGD; 2237; C5.
eggNOG; ENOG410IMYH; Eukaryota.
eggNOG; ENOG410ZFKB; LUCA.
InParanoid; P08650; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0031714; F:C5a anaphylatoxin chemotactic receptor binding; IDA:RGD.
GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:RGD.
GO; GO:0006935; P:chemotaxis; IDA:RGD.
GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0042593; P:glucose homeostasis; IDA:RGD.
GO; GO:0006954; P:inflammatory response; IDA:RGD.
GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IMP:RGD.
GO; GO:0033602; P:negative regulation of dopamine secretion; IDA:RGD.
GO; GO:0010700; P:negative regulation of norepinephrine secretion; IDA:RGD.
GO; GO:0050921; P:positive regulation of chemotaxis; IDA:RGD.
InterPro; IPR000020; Anaphylatoxin/fibulin.
InterPro; IPR018081; Anaphylatoxin_comp_syst.
InterPro; IPR001840; Anaphylatoxn_comp_syst_dom.
InterPro; IPR037562; Complement_C5.
PANTHER; PTHR11412:SF83; PTHR11412:SF83; 1.
Pfam; PF01821; ANATO; 1.
PRINTS; PR00004; ANAPHYLATOXN.
SMART; SM00104; ANATO; 1.
SUPFAM; SSF47686; SSF47686; 1.
PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
1: Evidence at protein level;
Complement alternate pathway; Complement pathway; Complete proteome;
Direct protein sequencing; Disulfide bond; Immunity;
Inflammatory response; Innate immunity; Reference proteome; Secreted.
CHAIN 1 77 C5a anaphylatoxin.
/FTId=PRO_0000005996.
DOMAIN 24 58 Anaphylatoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00022}.
REGION 18 47 Involved in C5AR1 binding.
{ECO:0000250|UniProtKB:P01031}.
DISULFID 24 50 {ECO:0000255|PROSITE-ProRule:PRU00022}.
DISULFID 25 57 {ECO:0000255|PROSITE-ProRule:PRU00022}.
DISULFID 37 58 {ECO:0000255|PROSITE-ProRule:PRU00022}.
CONFLICT 55 55 N -> K (in Ref. 1; AA sequence and 2; AA
sequence). {ECO:0000305}.
CONFLICT 61 63 ADK -> DP (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 63 63 K -> H (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 67 69 ESH -> NES (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 67 69 ESH -> NQS (in Ref. 1; AA sequence).
{ECO:0000305}.
NON_TER 1 1
NON_TER 77 77
SEQUENCE 77 AA; 8981 MW; 14141F41CC38BD28 CRC64;
DLQLLHQKVE EQAAKYKHRV PKKCCYDGAR ENKYETCEQR VARVTIGPHC IRAFNECCTI
ADKIRKESHH KGMLLGR


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