ID A0A151PIR2_ALLMI Unreviewed; 772 AA.
AC A0A151PIR2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Complement C2 {ECO:0000256|ARBA:ARBA00017023};
DE EC=3.4.21.43 {ECO:0000256|ARBA:ARBA00011908};
GN Name=C2 {ECO:0000313|EMBL:KYO48938.1};
GN ORFNames=Y1Q_0012722 {ECO:0000313|EMBL:KYO48938.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO48938.1};
RN [1] {ECO:0000313|EMBL:KYO48938.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO48938.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO48938.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKHW03000171; KYO48938.1; -; Genomic_DNA.
DR RefSeq; XP_006269030.2; XM_006268968.3.
DR AlphaFoldDB; A0A151PIR2; -.
DR STRING; 8496.A0A151PIR2; -.
DR GeneID; 102574290; -.
DR KEGG; amj:102574290; -.
DR eggNOG; KOG3627; Eukaryota.
DR OrthoDB; 3594820at2759; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
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 Gene3D; 2.10.70.10; Complement Module, domain 1; 3.
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; 3.
DR SMART; SM00020; Tryp_SPc; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50923; SUSHI; 3.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
DR PROSITE; PS50234; VWFA; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..772
FT /note="Complement C2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007587080"
FT DOMAIN 28..95
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 96..155
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 158..215
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 271..472
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 483..763
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 723..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 526
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001154-1"
FT ACT_SITE 574
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001154-1"
FT ACT_SITE 696
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001154-1"
FT DISULFID 126..153
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 186..213
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 772 AA; 85726 MW; D79C4827307E616A CRC64;
MVPPLCALLL LILTSGSGAR ALLPAESPQC SGDVGIQGGN VSLSDGLRPG SLLTYLCPLG
TYPYPQPSRL CQPSGHWTPL RTSSSTHNPT PTCRKMRCPP QLQFEHGTVG PRRTFYLVGS
ELTFECRDGY TLRGSALRRC LPTGRWDGEM PACDDGAEHC PEPGVPAGAL RRGSRYRQGD
RVSYRCQGTL ALVGSPEREC LPTGEWSGAE PTCRFPFSYD LPEDVTASFG ASLISVLGFV
ASSTSTDQNQ PVLKTYSLER RLILSQDSVL HLYLLVDASK SVSEANFQVF KDCVKIMVDR
IASFDVPVKF AVISYASKPI VIVPINGEEA GDADEVLERV ENHMSKKAHG NRTGTNIHDA
LQEIYHWIIF QKEALSKTNK PDEWKKVRHA VILLTDGKFN MGGSPKHAVT KIEDVLEVKP
DRNDYLDIYA FGVGQTDVEW EDLNAIASKK IGEQHAFKLN GPVELRTTLD SILDVKSIGE
VCGLGNHSEG ATAQQMNPWH VVIRPERGES CRGSLVADRW VLTAAHCFNN VQDTKLWRVN
IGSTDIQIAQ RFDHPQYNVR AKVDQGIPEF YDYDLSLLQL ERPVHFSATI RPICLPCTKE
ANRALRKPVR ATCKDHEVEL LRQARVPAQF ISLDNERLSV HIKTNEMWAR CTEGAVQPGT
LYAGKANVSD VVTQRFLCSG PESTGEPEAS TCKGESGGSL FVEKKMRYFQ VGVVSWGTYN
PCAQSRPDNQ GRMQRKPPPH RHHPRDFYLS LFQTQDWLRE HLSPALHFLP PA
//
