ID M3YGU6_MUSPF Unreviewed; 1184 AA.
AC M3YGU6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=CFB {ECO:0000313|Ensembl:ENSMPUP00000010553.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000010553.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000010553.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) 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; AEYP01101408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3YGU6; -.
DR STRING; 9669.ENSMPUP00000010553; -.
DR Ensembl; ENSMPUT00000010723.1; ENSMPUP00000010553.1; ENSMPUG00000010632.1.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000158605; -.
DR HOGENOM; CLU_264178_0_0_1; -.
DR InParanoid; M3YGU6; -.
DR OMA; GRWQTPG; -.
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; 3.
DR CDD; cd00190; Tryp_SPc; 1.
DR CDD; cd01470; vWA_complement_factors; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 4.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 4.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 2.
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; 4.
DR Pfam; PF00089; Trypsin; 2.
DR Pfam; PF00092; VWA; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00453; VWFADOMAIN.
DR SMART; SM00032; CCP; 4.
DR SMART; SM00020; Tryp_SPc; 2.
DR SMART; SM00327; VWA; 2.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 4.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR SUPFAM; SSF53300; vWA-like; 2.
DR PROSITE; PS50923; SUSHI; 4.
DR PROSITE; PS50240; TRYPSIN_DOM; 2.
DR PROSITE; PS00134; TRYPSIN_HIS; 2.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
DR PROSITE; PS50234; VWFA; 2.
PE 4: Predicted;
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 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 1..58
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 88..213
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 225..504
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 451..516
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 517..576
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 579..636
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 686..885
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 893..1177
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 29..56
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 547..574
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 607..634
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1184 AA; 132562 MW; 51B95052ED832F8F CRC64;
GHCPNPGISV GAVRTGSRFG LGDKVSYRCS SNLVLTGSAE RECQANGAWS GTEPICRQPY
SYDFPEDVGP AMGASFSHLL GATNPTQKKT NHENGTGTNT YAALNSVHIM MNNQMQRLGM
KTAAWQEIRH AIILLTDGKS NMGGSPKLAV DNIKEILNIN QQRSDYLDIY AIGVGKLDVD
WRELNELGSK KDGERHAFIL QDTEALYQVF EHMLDVSQLT HTICGVGNMS ANASVQERTP
WHVTIKPKGQ ETCRGALISD QWVLTAAHCF RNAENSSLWR VSVGDPKSQW GKDFSIDKVV
ISSGFDVFAK KDQGIREFYG DDIALLKLAE KVKMSTHARP ICLPCTVEAN LALRRPPGST
CRDHESELLN KLSIPAHFVA LSGKKMNINL KTGTEWTSCI EAVSQDKITF PDLKDVREVV
TDQFLCSGTE NDDNPCKGGS TTPLPGVRPQ SSCSLEGVEI KGGFFNLLKK GQALEYVCPS
GFYPYPVQAR TCRSTGSWSA LQTQDQKIVK KAECRAIRCP RPQEFENGEY WPRAPYYNLS
DEISFHCYDG YTLRGSANRT CQANGRWDGQ TAICDNGAGY CPNPGIPIGT RKVGSQYRLE
DSVTYYCSRG LTLRGSQRRT CQEGGSWSGT EPSCQDSFMY DTPEEVAEAF LSSLTETIEG
VDAEDGHSPG EQKKRKIVLD PSGSMNIYLV LDGSDSIGIG NFTRAKNCLR DFIEKVASYG
VKPKYGLVTY ATDPKVWVKV RDENSSDADW VTRTLNKISY EDHKHKGGTN TKKALQEVYN
MMSWPANRAL ESWNRTRHVI ILMTDGLHNM GGDPVSVIHE IRDFLNIGRD RKNLREDYLD
IYVFGVGPLV NQENINALAS KKDKEQHVFK VKDMENLEDV FIQMLDETRT LGLCGMVWEH
KAGTDYHKQP WQAKISVTRP SKGHESCMGA VVSEYFVLTA AHCFTVHDEA HSIKVSVGGR
RQDLDIEEVL FHPDYSINRK KEKGINEFYD YDVALIKLRQ KLTYDQTVRP ICIPCTERTN
QALRLPLSTT CQQQMQELLP AKDIKAMFVS ELLKDSKKML VRKEVYIKNG DKKASCERDA
RFAPGYEKVK DISEVVTPRF LCTGGVDPYA DPNTCKGDSG GPLIIHKRNR FIQVGVISWG
VVDVCKNQKR WQEVPTHARD FHVNLFQVLP WLKDKLKDED LDFL
//
