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Complement C2 (EC 3.4.21.43) (C3/C5 convertase) [Cleaved into: Complement C2b fragment; Complement C2a fragment]

 CO2_HUMAN               Reviewed;         752 AA.
P06681; B4DPF3; B4DV20; E9PFN7; O19694; Q13904;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
25-OCT-2017, entry version 199.
RecName: Full=Complement C2;
EC=3.4.21.43;
AltName: Full=C3/C5 convertase;
Contains:
RecName: Full=Complement C2b fragment;
Contains:
RecName: Full=Complement C2a fragment;
Flags: Precursor;
Name=C2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=2949737; DOI=10.1042/bj2390339;
Bentley D.R.;
"Primary structure of human complement component C2. Homology to two
unrelated protein families.";
Biochem. J. 239:339-345(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=2493504;
Horiuchi T., Macon K.J., Kidd V.J., Volanakis J.E.;
"cDNA cloning and expression of human complement component C2.";
J. Immunol. 142:2105-2111(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8326124;
Ishii Y., Zhu Z.B., Macon K.J., Volanakis J.E.;
"Structure of the human C2 gene.";
J. Immunol. 151:170-174(1993).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Rowen L., Dankers C., Baskin D., Faust J., Loretz C., Ahearn M.E.,
Banta A., Swartzell S., Smith T.M., Spies T., Hood L.;
"Sequence determination of 300 kilobases of the human class III MHC
locus.";
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-318 AND CYS-734.
SeattleSNPs variation discovery resource;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Kidney, and Small intestine;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 21-46 AND 244-256.
PubMed=6922702; DOI=10.1042/bj2050059;
Kerr M.A., Gagnon J.;
"The purification and properties of the second component of guinea-pig
complement.";
Biochem. J. 205:59-67(1982).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-46.
PubMed=2997031; DOI=10.1007/BF00430921;
Bentley D.R., Campbell R.D., Cross S.J.;
"DNA polymorphism of the C2 locus.";
Immunogenetics 22:377-390(1985).
[11]
PROTEIN SEQUENCE OF 21-28, AND INTERACTION WITH SCHISTOSOMA
HAEMATOBIUM TOR.
PubMed=10734221; DOI=10.1016/S0014-5793(00)01304-1;
Inal J.M., Sim R.B.;
"A Schistosoma protein, Sh-TOR, is a novel inhibitor of complement
which binds human C2.";
FEBS Lett. 470:131-134(2000).
[12]
PROTEIN SEQUENCE OF 137-171; 454-466 AND 574-717.
PubMed=6149575; DOI=10.1098/rstb.1984.0091;
Gagnon J.;
"Structure and activation of complement components C2 and factor B.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 306:301-309(1984).
[13]
PROTEIN SEQUENCE OF 244-269.
PubMed=6555044; DOI=10.1042/bj2130201;
Parkes C., Gagnon J., Kerr M.A.;
"The reaction of iodine and thiol-blocking reagents with human
complement components C2 and factor B. Purification and N-terminal
amino acid sequence of a peptide from C2a containing a free thiol
group.";
Biochem. J. 213:201-209(1983).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 588-717 (ISOFORM 1).
PubMed=6199794; DOI=10.1073/pnas.81.4.1212;
Bentley D.R., Porter R.R.;
"Isolation of cDNA clones for human complement component C2.";
Proc. Natl. Acad. Sci. U.S.A. 81:1212-1215(1984).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 694-752.
PubMed=3643061; DOI=10.1016/0092-8674(87)90436-3;
Wu L.C., Morley B.J., Campbell R.D.;
"Cell-specific expression of the human complement protein factor B
gene: evidence for the role of two distinct 5'-flanking elements.";
Cell 48:331-342(1987).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112; ASN-333; ASN-467;
ASN-471; ASN-621 AND ASN-651.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112 AND ASN-333.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 244-752, GLYCOSYLATION AT
ASN-333; ASN-467 AND ASN-621, MIDAS-LIKE MOTIF, METAL-BINDING SITES,
ACTIVE SITE, AND DISULFIDE BONDS.
PubMed=17027507; DOI=10.1016/j.str.2006.08.008;
Milder F.J., Raaijmakers H.C., Vandeputte M.D., Schouten A.,
Huizinga E.G., Romijn R.A., Hemrika W., Roos A., Daha M.R., Gros P.;
"Structure of complement component C2A: implications for convertase
formation and substrate binding.";
Structure 14:1587-1597(2006).
[20]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-243, AND DISULFIDE BONDS.
PubMed=19237749; DOI=10.1107/S0907444909000389;
Krishnan V., Xu Y., Macon K., Volanakis J.E., Narayana S.V.;
"The structure of C2b, a fragment of complement component C2 produced
during C3 convertase formation.";
Acta Crystallogr. D 65:266-274(2009).
[21]
VARIANTS C2D PHE-209 AND ARG-464.
PubMed=8621452; DOI=10.1074/jbc.271.10.5824;
Wetsel R.A., Kulics J., Lokki M.L., Kiepiela P., Akama H.,
Johnson C.A., Densen P., Colten H.R.;
"Type II human complement C2 deficiency. Allele-specific amino acid
substitutions (Ser189 --> Phe; Gly444 --> Arg) cause impaired C2
secretion.";
J. Biol. Chem. 271:5824-5831(1996).
[22]
VARIANT C2D TYR-131.
PubMed=9670930;
Zhu Z.B., Atkinson T.P., Volanakis J.E.;
"A novel type II complement C2 deficiency allele in an African-
American family.";
J. Immunol. 161:578-584(1998).
[23]
VARIANT ASP-318, AND INVOLVEMENT IN REDUCED RISK OF ARMD.
PubMed=16518403; DOI=10.1038/ng1750;
Gold B., Merriam J.E., Zernant J., Hancox L.S., Taiber A.J., Gehrs K.,
Cramer K., Neel J., Bergeron J., Barile G.R., Smith R.T.,
Hageman G.S., Dean M., Allikmets R.;
"Variation in factor B (BF) and complement component 2 (C2) genes is
associated with age-related macular degeneration.";
Nat. Genet. 38:458-462(2006).
-!- 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 C4b 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.
-!- SUBUNIT: C2a interacts with Schistosoma haematobium TOR (via N-
terminal extracellular domain). This results in inhibition of the
classical and lectin pathway of complement activation, probably
due to interference with binding of C2a to C4b such that C3
convertase cannot be formed. This infers resistance to complement-
mediated cell lysis, allowing parasite survival and infection.
{ECO:0000269|PubMed:10734221}.
-!- INTERACTION:
O43889-2:CREB3; NbExp=3; IntAct=EBI-2835920, EBI-625022;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P06681-1; Sequence=Displayed;
Name=2;
IsoId=P06681-2; Sequence=VSP_043038, VSP_043039;
Note=No experimental confirmation available.;
Name=3;
IsoId=P06681-3; Sequence=VSP_046103;
Note=No experimental confirmation available.;
-!- DOMAIN: The MIDAS-like motif in the VWFA domain binds divalent
metal cations.
-!- POLYMORPHISM: The variant Asp-318 is associated with a reduced
risk of age-related macular degeneration (ARMD) [MIM:603075]. ARMD
is a multifactorial eye disease and the most common cause of
irreversible vision loss in the developed world.
{ECO:0000269|PubMed:16518403}.
-!- DISEASE: Complement component 2 deficiency (C2D) [MIM:217000]: A
rare defect of the complement classical pathway associated with
the development of autoimmune disorders, mainly systemic lupus
erythematosus. Skin and joint manifestations are common and renal
disease is relatively rare. Patients with complement component 2
deficiency are also reported to have recurrent invasive
infections. {ECO:0000269|PubMed:8621452,
ECO:0000269|PubMed:9670930}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: C2 is a major histocompatibility complex class-III
protein.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=C2base; Note=C2 mutation db;
URL="http://structure.bmc.lu.se/idbase/C2base/";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/c2/";
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EMBL; X04481; CAA28169.1; -; mRNA.
EMBL; M26301; AAA35614.1; -; mRNA.
EMBL; L09708; AAB97607.1; -; Genomic_DNA.
EMBL; L09706; AAB97607.1; JOINED; Genomic_DNA.
EMBL; L09707; AAB97607.1; JOINED; Genomic_DNA.
EMBL; AF019413; AAB67975.1; -; Genomic_DNA.
EMBL; AY349611; AAQ15273.1; -; Genomic_DNA.
EMBL; AK298311; BAG60565.1; -; mRNA.
EMBL; AK300892; BAG62532.1; -; mRNA.
EMBL; AL645922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL662834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL662849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL671762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL844853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX005143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR388219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR759782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR759784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR933857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC043484; AAH43484.1; -; mRNA.
EMBL; M15549; AAA59649.1; -; Genomic_DNA.
EMBL; M15082; AAA59624.1; -; Genomic_DNA.
CCDS; CCDS4728.1; -. [P06681-1]
CCDS; CCDS54991.1; -. [P06681-3]
CCDS; CCDS56416.1; -. [P06681-2]
PIR; A25971; C2HU.
RefSeq; NP_000054.2; NM_000063.5. [P06681-1]
RefSeq; NP_001139375.1; NM_001145903.2. [P06681-3]
RefSeq; NP_001171534.1; NM_001178063.2. [P06681-2]
UniGene; Hs.408903; -.
PDB; 2I6Q; X-ray; 2.10 A; A=244-752.
PDB; 2I6S; X-ray; 2.70 A; A=244-752.
PDB; 2ODP; X-ray; 1.90 A; A=244-752.
PDB; 2ODQ; X-ray; 2.30 A; A=244-752.
PDB; 3ERB; X-ray; 1.80 A; A=21-243.
PDBsum; 2I6Q; -.
PDBsum; 2I6S; -.
PDBsum; 2ODP; -.
PDBsum; 2ODQ; -.
PDBsum; 3ERB; -.
ProteinModelPortal; P06681; -.
SMR; P06681; -.
BioGrid; 107178; 2.
IntAct; P06681; 4.
STRING; 9606.ENSP00000299367; -.
MEROPS; S01.194; -.
iPTMnet; P06681; -.
PhosphoSitePlus; P06681; -.
DMDM; 3915642; -.
PaxDb; P06681; -.
PeptideAtlas; P06681; -.
PRIDE; P06681; -.
Ensembl; ENST00000299367; ENSP00000299367; ENSG00000166278. [P06681-1]
Ensembl; ENST00000375510; ENSP00000364660; ENSG00000204364. [P06681-1]
Ensembl; ENST00000383362; ENSP00000372853; ENSG00000206372. [P06681-1]
Ensembl; ENST00000411803; ENSP00000402278; ENSG00000235696. [P06681-1]
Ensembl; ENST00000413548; ENSP00000407961; ENSG00000231543. [P06681-1]
Ensembl; ENST00000416252; ENSP00000405800; ENSG00000235017. [P06681-1]
Ensembl; ENST00000442278; ENSP00000395683; ENSG00000166278. [P06681-3]
Ensembl; ENST00000448206; ENSP00000392835; ENSG00000226560. [P06681-1]
Ensembl; ENST00000452323; ENSP00000392322; ENSG00000166278. [P06681-2]
Ensembl; ENST00000548973; ENSP00000446728; ENSG00000206372. [P06681-3]
Ensembl; ENST00000548995; ENSP00000449286; ENSG00000204364. [P06681-3]
Ensembl; ENST00000549972; ENSP00000447632; ENSG00000235696. [P06681-3]
Ensembl; ENST00000550682; ENSP00000446639; ENSG00000231543. [P06681-3]
Ensembl; ENST00000551081; ENSP00000450387; ENSG00000235017. [P06681-3]
Ensembl; ENST00000551648; ENSP00000449715; ENSG00000226560. [P06681-3]
Ensembl; ENST00000612228; ENSP00000482616; ENSG00000231543. [P06681-2]
Ensembl; ENST00000615380; ENSP00000481651; ENSG00000226560. [P06681-2]
Ensembl; ENST00000618254; ENSP00000483231; ENSG00000235017. [P06681-2]
Ensembl; ENST00000621558; ENSP00000480739; ENSG00000206372. [P06681-2]
GeneID; 717; -.
KEGG; hsa:717; -.
UCSC; uc010jtk.5; human. [P06681-1]
CTD; 717; -.
DisGeNET; 717; -.
EuPathDB; HostDB:ENSG00000166278.14; -.
GeneCards; C2; -.
HGNC; HGNC:1248; C2.
HPA; CAB016775; -.
MalaCards; C2; -.
MIM; 217000; phenotype.
MIM; 603075; phenotype.
MIM; 613927; gene.
neXtProt; NX_P06681; -.
OpenTargets; ENSG00000166278; -.
Orphanet; 169147; Immunodeficiency due to an early component of complement deficiency.
PharmGKB; PA25637; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00530000063826; -.
HOGENOM; HOG000038034; -.
HOVERGEN; HBG002567; -.
InParanoid; P06681; -.
KO; K01332; -.
OMA; RNVSEFY; -.
OrthoDB; EOG093702XZ; -.
PhylomeDB; P06681; -.
TreeFam; TF330194; -.
Reactome; R-HSA-166663; Initial triggering of complement.
Reactome; R-HSA-174577; Activation of C3 and C5.
Reactome; R-HSA-977606; Regulation of Complement cascade.
SABIO-RK; P06681; -.
ChiTaRS; C2; human.
EvolutionaryTrace; P06681; -.
GeneWiki; Complement_component_2; -.
GenomeRNAi; 717; -.
PMAP-CutDB; P06681; -.
PRO; PR:P06681; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000166278; -.
CleanEx; HS_C2; -.
ExpressionAtlas; P06681; baseline and differential.
Genevisible; P06681; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0006956; P:complement activation; IMP:BHF-UCL.
GO; GO:0006958; P:complement activation, classical pathway; TAS:ProtInc.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:2000427; P:positive regulation of apoptotic cell clearance; IMP:BHF-UCL.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
CDD; cd00033; CCP; 3.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR011360; Compl_C2_B.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF00084; Sushi; 2.
Pfam; PF00089; Trypsin; 1.
Pfam; PF00092; VWA; 1.
PIRSF; PIRSF001154; Compl_C2_B; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00032; CCP; 3.
SMART; SM00020; Tryp_SPc; 1.
SMART; SM00327; VWA; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF57535; SSF57535; 3.
PROSITE; PS50923; SUSHI; 3.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complement pathway;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; Glycoprotein; Hydrolase; Immunity; Innate immunity;
Metal-binding; Polymorphism; Protease; Reference proteome; Repeat;
Secreted; Serine protease; Signal; Sushi.
SIGNAL 1 20 {ECO:0000269|PubMed:10734221,
ECO:0000269|PubMed:6922702}.
CHAIN 21 752 Complement C2.
/FTId=PRO_0000027610.
CHAIN 21 243 Complement C2b fragment.
/FTId=PRO_0000027611.
CHAIN 244 752 Complement C2a fragment.
/FTId=PRO_0000027612.
DOMAIN 22 86 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 87 146 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 149 206 Sushi 3. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 254 452 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 464 744 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
MOTIF 260 264 MIDAS-like motif.
ACT_SITE 507 507 Charge relay system.
{ECO:0000269|PubMed:17027507}.
ACT_SITE 561 561 Charge relay system.
{ECO:0000269|PubMed:17027507}.
ACT_SITE 679 679 Charge relay system.
{ECO:0000269|PubMed:17027507}.
METAL 262 262 Divalent metal cation.
METAL 264 264 Divalent metal cation.
METAL 337 337 Divalent metal cation.
CARBOHYD 29 29 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 112 112 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:17027507,
ECO:0000269|PubMed:19159218}.
CARBOHYD 467 467 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:17027507}.
CARBOHYD 471 471 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 621 621 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:17027507}.
CARBOHYD 651 651 N-linked (GlcNAc...) (complex)
asparagine.
{ECO:0000269|PubMed:16335952}.
DISULFID 24 64
DISULFID 51 84
DISULFID 89 131
DISULFID 117 144
DISULFID 151 191
DISULFID 177 204
DISULFID 492 508 {ECO:0000250}.
DISULFID 675 705 {ECO:0000250}.
VAR_SEQ 1 147 MGPLMVLFCLLFLYPGLADSAPSCPQNVNISGGTFTLSHGW
APGSLLTYSCPQGLYPSPASRLCKSSGQWQTPGATRSLSKA
VCKPVRCPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFIL
RGSPVRQCRPNGMWDGETAVCDNG -> MRALCIRETCSSE
LGFSRNWSRRK (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043038.
VAR_SEQ 16 147 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046103.
VAR_SEQ 238 328 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043039.
VARIANT 131 131 C -> Y (in C2D; dbSNP:rs760744400).
{ECO:0000269|PubMed:9670930}.
/FTId=VAR_008544.
VARIANT 209 209 S -> F (in C2D; dbSNP:rs28934590).
{ECO:0000269|PubMed:8621452}.
/FTId=VAR_008545.
VARIANT 318 318 E -> D (in dbSNP:rs9332739).
{ECO:0000269|PubMed:16518403,
ECO:0000269|Ref.5}.
/FTId=VAR_019158.
VARIANT 464 464 G -> R (in C2D; dbSNP:rs151340617).
{ECO:0000269|PubMed:8621452}.
/FTId=VAR_008546.
VARIANT 533 533 F -> L (in dbSNP:rs1042664).
/FTId=VAR_011772.
VARIANT 734 734 R -> C (in dbSNP:rs4151648).
{ECO:0000269|Ref.5}.
/FTId=VAR_019159.
CONFLICT 30 30 I -> L (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 34 34 T -> S (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 211 211 D -> G (in Ref. 6; BAG62532).
{ECO:0000305}.
CONFLICT 249 249 R -> S (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 253 253 L -> K (in Ref. 9; AA sequence).
{ECO:0000305}.
STRAND 34 39 {ECO:0000244|PDB:3ERB}.
STRAND 46 50 {ECO:0000244|PDB:3ERB}.
STRAND 55 59 {ECO:0000244|PDB:3ERB}.
STRAND 61 64 {ECO:0000244|PDB:3ERB}.
STRAND 83 86 {ECO:0000244|PDB:3ERB}.
STRAND 88 90 {ECO:0000244|PDB:3ERB}.
STRAND 98 102 {ECO:0000244|PDB:3ERB}.
STRAND 105 108 {ECO:0000244|PDB:3ERB}.
STRAND 112 117 {ECO:0000244|PDB:3ERB}.
STRAND 122 125 {ECO:0000244|PDB:3ERB}.
STRAND 127 131 {ECO:0000244|PDB:3ERB}.
STRAND 137 139 {ECO:0000244|PDB:3ERB}.
STRAND 143 145 {ECO:0000244|PDB:3ERB}.
STRAND 149 151 {ECO:0000244|PDB:3ERB}.
STRAND 160 163 {ECO:0000244|PDB:3ERB}.
STRAND 172 177 {ECO:0000244|PDB:3ERB}.
STRAND 182 185 {ECO:0000244|PDB:3ERB}.
STRAND 187 191 {ECO:0000244|PDB:3ERB}.
STRAND 197 199 {ECO:0000244|PDB:3ERB}.
STRAND 203 205 {ECO:0000244|PDB:3ERB}.
HELIX 207 211 {ECO:0000244|PDB:3ERB}.
STRAND 249 260 {ECO:0000244|PDB:2I6S}.
HELIX 267 284 {ECO:0000244|PDB:2I6S}.
TURN 285 287 {ECO:0000244|PDB:2I6S}.
STRAND 291 306 {ECO:0000244|PDB:2I6S}.
HELIX 311 314 {ECO:0000244|PDB:2I6S}.
HELIX 316 324 {ECO:0000244|PDB:2I6S}.
HELIX 328 331 {ECO:0000244|PDB:2I6S}.
HELIX 339 357 {ECO:0000244|PDB:2I6S}.
STRAND 359 361 {ECO:0000244|PDB:2I6S}.
HELIX 362 365 {ECO:0000244|PDB:2I6S}.
STRAND 367 375 {ECO:0000244|PDB:2I6S}.
STRAND 381 383 {ECO:0000244|PDB:2I6S}.
HELIX 386 395 {ECO:0000244|PDB:2I6S}.
HELIX 403 405 {ECO:0000244|PDB:2I6S}.
STRAND 406 413 {ECO:0000244|PDB:2I6S}.
HELIX 420 426 {ECO:0000244|PDB:2I6S}.
STRAND 436 440 {ECO:0000244|PDB:2I6S}.
HELIX 442 451 {ECO:0000244|PDB:2I6S}.
HELIX 474 477 {ECO:0000244|PDB:2I6S}.
STRAND 481 485 {ECO:0000244|PDB:2I6S}.
STRAND 492 504 {ECO:0000244|PDB:2I6S}.
HELIX 506 509 {ECO:0000244|PDB:2I6S}.
HELIX 515 517 {ECO:0000244|PDB:2I6S}.
STRAND 519 522 {ECO:0000244|PDB:2I6S}.
STRAND 531 533 {ECO:0000244|PDB:2I6S}.
STRAND 535 540 {ECO:0000244|PDB:2I6S}.
HELIX 546 552 {ECO:0000244|PDB:2I6S}.
STRAND 563 569 {ECO:0000244|PDB:2I6S}.
STRAND 574 576 {ECO:0000244|PDB:2I6S}.
HELIX 586 591 {ECO:0000244|PDB:2I6S}.
HELIX 600 607 {ECO:0000244|PDB:2I6S}.
STRAND 610 618 {ECO:0000244|PDB:2I6S}.
STRAND 623 630 {ECO:0000244|PDB:2I6S}.
HELIX 632 639 {ECO:0000244|PDB:2I6S}.
HELIX 640 644 {ECO:0000244|PDB:2I6S}.
HELIX 655 657 {ECO:0000244|PDB:2I6S}.
STRAND 663 666 {ECO:0000244|PDB:2I6S}.
HELIX 676 678 {ECO:0000244|PDB:2I6S}.
STRAND 682 687 {ECO:0000244|PDB:2I6S}.
STRAND 690 701 {ECO:0000244|PDB:2I6S}.
TURN 704 707 {ECO:0000244|PDB:2I6S}.
STRAND 720 723 {ECO:0000244|PDB:2I6S}.
STRAND 727 731 {ECO:0000244|PDB:2I6S}.
HELIX 732 735 {ECO:0000244|PDB:2I6S}.
HELIX 736 743 {ECO:0000244|PDB:2I6S}.
TURN 744 746 {ECO:0000244|PDB:2I6S}.
SEQUENCE 752 AA; 83268 MW; 5A96A13E700CF444 CRC64;
MGPLMVLFCL LFLYPGLADS APSCPQNVNI SGGTFTLSHG WAPGSLLTYS CPQGLYPSPA
SRLCKSSGQW QTPGATRSLS KAVCKPVRCP APVSFENGIY TPRLGSYPVG GNVSFECEDG
FILRGSPVRQ CRPNGMWDGE TAVCDNGAGH CPNPGISLGA VRTGFRFGHG DKVRYRCSSN
LVLTGSSERE CQGNGVWSGT EPICRQPYSY DFPEDVAPAL GTSFSHMLGA TNPTQKTKES
LGRKIQIQRS GHLNLYLLLD CSQSVSENDF LIFKESASLM VDRIFSFEIN VSVAIITFAS
EPKVLMSVLN DNSRDMTEVI SSLENANYKD HENGTGTNTY AALNSVYLMM NNQMRLLGME
TMAWQEIRHA IILLTDGKSN MGGSPKTAVD HIREILNINQ KRNDYLDIYA IGVGKLDVDW
RELNELGSKK DGERHAFILQ DTKALHQVFE HMLDVSKLTD TICGVGNMSA NASDQERTPW
HVTIKPKSQE TCRGALISDQ WVLTAAHCFR DGNDHSLWRV NVGDPKSQWG KEFLIEKAVI
SPGFDVFAKK NQGILEFYGD DIALLKLAQK VKMSTHARPI CLPCTMEANL ALRRPQGSTC
RDHENELLNK QSVPAHFVAL NGSKLNINLK MGVEWTSCAE VVSQEKTMFP NLTDVREVVT
DQFLCSGTQE DESPCKGESG GAVFLERRFR FFQVGLVSWG LYNPCLGSAD KNSRKRAPRS
KVPPPRDFHI NLFRMQPWLR QHLGDVLNFL PL


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