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Q8SQ75 (CO2_PONPY) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Complement C2
EC=3.4.21.43
Alternative name(s):
C3/C5 convertase

Cleaved into the following 2 chains:

  1. Complement C2b fragment
  2. Complement C2a fragment
Gene names
Name:C2
OrganismPongo pygmaeus (Bornean orangutan)
Taxonomic identifier9600 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length752 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Component C2 which is part of the classical pathway of the complement system is cleaved by activated factor C1 into two fragments: C2b and C2a. C2a, a serine protease, then combines with complement factor 4b to generate the C3 or C5 convertase.

Catalytic activity

Selective cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to form C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to form C5a and C5b.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Contains 3 Sushi (CCP/SCR) domains.

Contains 1 VWFA domain.

Ontologies

Keywords
   Biological processComplement pathway
Immunity
Innate immunity
   Cellular componentSecreted
   DomainRepeat
Signal
Sushi
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processcomplement activation, classical pathway

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Chain21 – 752732Complement C2
PRO_0000027619
Chain21 – 243223Complement C2b fragment
PRO_0000027620
Chain244 – 752509Complement C2a fragment
PRO_0000027621

Regions

Domain22 – 8665Sushi 1
Domain87 – 14660Sushi 2
Domain149 – 20658Sushi 3
Domain254 – 452199VWFA
Domain464 – 744281Peptidase S1

Sites

Active site5071Charge relay system By similarity
Active site5611Charge relay system By similarity
Active site6791Charge relay system By similarity

Amino acid modifications

Glycosylation291N-linked (GlcNAc...) Potential
Glycosylation1121N-linked (GlcNAc...) Potential
Glycosylation2901N-linked (GlcNAc...) Potential
Glycosylation3331N-linked (GlcNAc...) Potential
Glycosylation4671N-linked (GlcNAc...) Potential
Glycosylation4711N-linked (GlcNAc...) Potential
Glycosylation6211N-linked (GlcNAc...) Potential
Disulfide bond24 ↔ 64 By similarity
Disulfide bond51 ↔ 84 By similarity
Disulfide bond89 ↔ 131 By similarity
Disulfide bond117 ↔ 144 By similarity
Disulfide bond151 ↔ 191 By similarity
Disulfide bond177 ↔ 204 By similarity
Disulfide bond492 ↔ 508 By similarity
Disulfide bond675 ↔ 705 By similarity

Experimental info

Sequence conflict201S → L in CAH91866. Ref.2
Sequence conflict1651F → S in CAH91866. Ref.2
Sequence conflict1871S → E in CAH91866. Ref.2
Sequence conflict316 – 3183MTD → ITE in CAH91866. Ref.2
Sequence conflict3951I → L in CAH91866. Ref.2
Sequence conflict6211N → S in CAH91866. Ref.2
Sequence conflict7211K → E in CAH91866. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8SQ75 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: DD35111E68FF264E

FASTA75283,326
        10         20         30         40         50         60 
MGPLMVLFCL LFLYPGLADS APSCPQNVNI SGGTFTLSHG WAPGSLLTYS CPQGLYPSPA 

        70         80         90        100        110        120 
SRLCKSSGQW QTPRATRSLS KAVCKPVRCP APVSFENGIY TPRLGSYPVG GNVSFECEDG 

       130        140        150        160        170        180 
FILRGSPVRQ CRPNGMWDGE TAVCDNGAGH CPNPGISLGA VRTGFRFGHG DKVRYRCSSN 

       190        200        210        220        230        240 
LVLTGSSERE CQGNGVWSGT EPICRQPYSY DFPEDVAPAL GTSFSHMLGA TNPTQKTKES 

       250        260        270        280        290        300 
LGRKIQIQRS GHLNLYLLLD CSQSVSENDF LIFKESASLM VDRIFSFEIN VSVAIITFAS 

       310        320        330        340        350        360 
EPKVLMSVLN DNSRDMTDVI SSLENANYKD HENGTGTNTY AALNSVYLMM NNQMRLLGME 

       370        380        390        400        410        420 
TMAWQEIRHA IILLTDGKSN MGGSPKTAVD HIREILNINQ KRNDYLDIYA IGVGKLDVDW 

       430        440        450        460        470        480 
RELNELGSKK DGERHAFILQ DTKALHQVFE HMLDVSKLTD TICGVGNMSA NASDQERTPW 

       490        500        510        520        530        540 
HVTIKPKSQE TCRGALISDQ WVLTAAHCFR DGNDHSLWRV NVGDPKSQWG KEFLIEKAVI 

       550        560        570        580        590        600 
SPGFDVFAKK NQGILEFYGD DIALLKLAQK VKMSTHARPI CLPCTMEANL ALRRPQGSTC 

       610        620        630        640        650        660 
RDHENELLNK QSVPAHFVAL NGSKLNINLK MGVEWTSCAE VVSQEKTMFP SLTDVREVVT 

       670        680        690        700        710        720 
DQFLCSGTQE DESPCKGESG GAVFLERRFR FFQVGLVSWG LYNPCLGSAD KNSRKRAPRS 

       730        740        750 
KVPPPRDFHI NLFRMQPWLR QHLGDVLNFL PL

« Hide

References

« Hide 'large scale' references
[1]"Comparative analysis of human and primate complement C2 and factor B genes."
Schneider P.M., Tantalaki E., Stradmann-Bellinghausen B., Rittner C.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY074690 expand/collapse EMBL AC list , AY074678, AY074679, AY074680, AY074681, AY074682, AY074683, AY074684, AY074685, AY074686, AY074687, AY074688, AY074689 Genomic DNA. Translation: AAL82820.1.
CR859707 mRNA. Translation: CAH91866.1.
UniGenePab.18930.

3D structure databases

ProteinModelPortalQ8SQ75.
SMRQ8SQ75. Positions 244-752.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8SQ75.

Protein family/group databases

MEROPSS01.194.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG002567.

Family and domain databases

InterProIPR011360. Compl_C2_B.
IPR016060. Complement_control_module.
IPR009003. Pept_cys/ser_Trypsin-like.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP.
IPR002035. VWF_A.
[Graphical view]
Gene3DG3DSA:2.10.70.10. Complement_control_module. 3 hits.
PfamPF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
PIRSFPIRSF001154. Compl_C2_B. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00032. CCP. 3 hits.
SM00020. Tryp_SPc. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF57535. Complement_control_module. 3 hits.
SSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS50923. SUSHI. 3 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCO2_PONPY
AccessionPrimary (citable) accession number: Q8SQ75
Secondary accession number(s): Q5R8P4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2002
Last modified: November 16, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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