Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Complement C5a anaphylatoxin

Gene

C5

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Complement alternate pathway, Complement pathway, Immunity, Inflammatory response, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Complement C5a anaphylatoxin
Gene namesi
Name:C5
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7474Complement C5a anaphylatoxinPRO_0000048521Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 ↔ 47
Disulfide bondi22 ↔ 54
Disulfide bondi34 ↔ 55

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP01032.

Interactioni

Subunit structurei

The C5a anaphylatoxin interacts with C5AR1.By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000005908.

Structurei

Secondary structure

1
74
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1110Combined sources
Helixi16 – 2611Combined sources
Helixi34 – 407Combined sources
Helixi45 – 6218Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C5ANMR-A1-73[»]
ProteinModelPortaliP01032.
SMRiP01032. Positions 1-65.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01032.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 5535Anaphylatoxin-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni15 – 4430Involved in C5AR1 bindingBy similarityAdd
BLAST
Regioni72 – 743Required for 90% of C5a activity; although Arg-74 is not essential

Sequence similaritiesi

Contains 1 anaphylatoxin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
HOVERGENiHBG051050.
InParanoidiP01032.

Family and domain databases

Gene3Di1.20.91.20. 1 hit.
InterProiIPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_comp_syst.
IPR001840. Anaphylatoxn_comp_syst_dom.
[Graphical view]
PfamiPF01821. ANATO. 1 hit.
[Graphical view]
PRINTSiPR00004. ANAPHYLATOXN.
SMARTiSM00104. ANATO. 1 hit.
[Graphical view]
SUPFAMiSSF47686. SSF47686. 1 hit.
PROSITEiPS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P01032-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQKKIEEEA AKYKYAMLKK CCYDGAYRND DETCEERAAR IKIGPKCVKA
60 70
FKDCCYIANQ VRAEQSHKNI QLGR
Length:74
Mass (Da):8,609
Last modified:July 21, 1986 - v1
Checksum:i11AAF2E94A026EB3
GO

Sequence databases

PIRiA01268.

Cross-referencesi

Sequence databases

PIRiA01268.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C5ANMR-A1-73[»]
ProteinModelPortaliP01032.
SMRiP01032. Positions 1-65.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000005908.

Proteomic databases

PaxDbiP01032.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
HOVERGENiHBG051050.
InParanoidiP01032.

Miscellaneous databases

EvolutionaryTraceiP01032.

Family and domain databases

Gene3Di1.20.91.20. 1 hit.
InterProiIPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_comp_syst.
IPR001840. Anaphylatoxn_comp_syst_dom.
[Graphical view]
PfamiPF01821. ANATO. 1 hit.
[Graphical view]
PRINTSiPR00004. ANAPHYLATOXN.
SMARTiSM00104. ANATO. 1 hit.
[Graphical view]
SUPFAMiSSF47686. SSF47686. 1 hit.
PROSITEiPS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Amino acid sequence of the anaphylatoxin from the fifth component of porcine complement."
    Gerard C., Hugli T.E.
    J. Biol. Chem. 255:4710-4715(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Identification of classical anaphylatoxin as the des-Arg form of the C5a molecule: evidence of a modulator role for the oligosaccharide unit in human des-Arg74-C5a."
    Gerard C., Hugli T.E.
    Proc. Natl. Acad. Sci. U.S.A. 78:1833-1837(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE REGION.
  3. "Three-dimensional structure of porcine C5adesArg from 1H nuclear magnetic resonance data."
    Williamson M.P., Madison V.S.
    Biochemistry 29:2895-2905(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiCO5_PIG
AccessioniPrimary (citable) accession number: P01032
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 11, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.