ID A0A0G2JL69_HUMAN Unreviewed; 723 AA.
AC A0A0G2JL69;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Complement C2 {ECO:0000256|ARBA:ARBA00017023};
DE EC=3.4.21.43 {ECO:0000256|ARBA:ARBA00011908};
DE AltName: Full=C3/C5 convertase {ECO:0000256|ARBA:ARBA00029636};
GN Name=C2 {ECO:0000313|Ensembl:ENSP00000449823.2};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000449823.2, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000449823.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [2] {ECO:0007829|PubMed:24275569}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [3] {ECO:0000313|Ensembl:ENSP00000449823.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2022) to UniProtKB.
CC -!- FUNCTION: Component C2 which is part of the classical pathway of the
CC complement system is cleaved by activated factor C1 into two fragments:
CC C2b and C2a. C2a, a serine protease, then combines with complement
CC factor C4b to generate the C3 or C5 convertase.
CC {ECO:0000256|ARBA:ARBA00025003}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Ser bond in complement component
CC C3 alpha-chain to form C3a and C3b, and Arg-|-Xaa bond in complement
CC component C5 alpha-chain to form C5a and C5b.; EC=3.4.21.43;
CC Evidence={ECO:0000256|ARBA:ARBA00000095};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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DR EMBL; AL662834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX005143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR388219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR933857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001269387.1; NM_001282458.1.
DR AlphaFoldDB; A0A0G2JL69; -.
DR SMR; A0A0G2JL69; -.
DR MassIVE; A0A0G2JL69; -.
DR DNASU; 717; -.
DR Ensembl; ENST00000547984.3; ENSP00000449345.2; ENSG00000206372.11.
DR Ensembl; ENST00000548828.4; ENSP00000447458.2; ENSG00000204364.10.
DR Ensembl; ENST00000549997.5; ENSP00000450180.2; ENSG00000231543.9.
DR Ensembl; ENST00000550045.5; ENSP00000449366.2; ENSG00000235696.8.
DR Ensembl; ENST00000550363.4; ENSP00000448602.2; ENSG00000235017.9.
DR Ensembl; ENST00000552638.3; ENSP00000449823.2; ENSG00000226560.10.
DR GeneID; 717; -.
DR CTD; 717; -.
DR HGNC; HGNC:1248; C2.
DR OrthoDB; 3594820at2759; -.
DR BioGRID-ORCS; 717; 13 hits in 1148 CRISPR screens.
DR ChiTaRS; C2; human.
DR GenomeRNAi; 717; -.
DR Proteomes; UP000005640; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR CDD; cd01470; vWA_complement_factors; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR011360; Compl_C2_B.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR46393:SF2; COMPLEMENT C2; 1.
DR PANTHER; PTHR46393; SUSHI DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00089; Trypsin; 1.
DR Pfam; PF00092; VWA; 1.
DR PIRSF; PIRSF001154; Compl_C2_B; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00032; CCP; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50923; SUSHI; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Complement pathway {ECO:0000256|ARBA:ARBA00022875};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00302}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Proteomics identification {ECO:0007829|MaxQB:A0A0G2JL69,
KW ECO:0007829|PeptideAtlas:A0A0G2JL69};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}.
FT DOMAIN 58..117
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 120..177
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 225..423
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 435..715
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 478
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001154-1"
FT ACT_SITE 532
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001154-1"
FT ACT_SITE 650
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001154-1"
FT DISULFID 88..115
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 148..175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 723 AA; 80150 MW; 40EB07EA5B050DD5 CRC64;
MAGLLGAFSP TPAPRACTHP QHHGCARAAD SGRPQEPPGL CLRRSANVRL PVGFAQAVRC
PAPVSFENGI YTPRLGSYPV GGNVSFECED GFILRGSPVR QCRPNGMWDG ETAVCDNGAG
HCPNPGISLG AVRTGFRFGH GDKVRYRCSS NLVLTGSSER ECQGNGVWSG TEPICRQPYS
YDFPEDVAPA LGTSFSHMLG ATNPTQKTKE SLGRKIQIQR SGHLNLYLLL DCSQSVSEND
FLIFKESASL MVDRIFSFEI NVSVAIITFA SEPKVLMSVL NDNSRDMTEV ISSLENANYK
DHENGTGTNT YAALNSVYLM MNNQMRLLGM ETMAWQEIRH AIILLTDGKS NMGGSPKTAV
DHIREILNIN QKRNDYLDIY AIGVGKLDVD WRELNELGSK KDGERHAFIL QDTKALHQVF
EHMLDVSKLT DTICGVGNMS ANASDQERTP WHVTIKPKSQ ETCRGALISD QWVLTAAHCF
RDGNDHSLWR VNVGDPKSQW GKEFLIEKAV ISPGFDVFAK KNQGILEFYG DDIALLKLAQ
KVKMSTHARP ICLPCTMEAN LALRRPQGST CRDHENELLN KQSVPAHFVA LNGSKLNINL
KMGVEWTSCA EVVSQEKTMF PNLTDVREVV TDQFLCSGTQ EDESPCKGES GGAVFLERRF
RFFQVGLVSW GLYNPCLGSA DKNSRKRAPR SKVPPPRDFH INLFRMQPWL RQHLGDVLNF
LPL
//
