ID G3HCL6_CRIGR Unreviewed; 1626 AA.
AC G3HCL6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Complement C3 {ECO:0000256|ARBA:ARBA00017018};
GN ORFNames=I79_008227 {ECO:0000313|EMBL:EGV93753.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGV93753.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
CC -!- FUNCTION: Acts as a chemoattractant for neutrophils in chronic
CC inflammation. {ECO:0000256|ARBA:ARBA00003326}.
CC -!- FUNCTION: C3 plays a central role in the activation of the complement
CC system. Its processing by C3 convertase is the central reaction in both
CC classical and alternative complement pathways. After activation C3b can
CC bind covalently, via its reactive thioester, to cell surface
CC carbohydrates or immune aggregates. {ECO:0000256|ARBA:ARBA00002877}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; JH000282; EGV93753.1; -; Genomic_DNA.
DR STRING; 10029.G3HCL6; -.
DR MEROPS; I39.950; -.
DR PaxDb; 10029-XP_007614575-1; -.
DR eggNOG; KOG1366; Eukaryota.
DR InParanoid; G3HCL6; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR CDD; cd00017; ANATO; 1.
DR CDD; cd02896; complement_C3_C4_C5; 1.
DR CDD; cd03583; NTR_complement_C3; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.20.130.20; -; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 2.60.120.1540; -; 1.
DR Gene3D; 2.60.40.1930; -; 3.
DR Gene3D; 2.60.40.1940; -; 1.
DR Gene3D; 6.20.50.160; -; 1.
DR Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR Gene3D; 1.20.91.20; Anaphylotoxins (complement system); 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR000020; Anaphylatoxin/fibulin.
DR InterPro; IPR018081; Anaphylatoxin_comp_syst.
DR InterPro; IPR001840; Anaphylatoxn_comp_syst_dom.
DR InterPro; IPR041425; C3/4/5_MG1.
DR InterPro; IPR049466; C3_CUB1.
DR InterPro; IPR048848; C3_CUB2.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR035815; NTR_complement_C3.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11412:SF81; COMPLEMENT C3; 1.
DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF01821; ANATO; 1.
DR Pfam; PF21406; C3_CUB1; 1.
DR Pfam; PF21308; C3_CUB2; 1.
DR Pfam; PF17790; MG1; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF17789; MG4; 1.
DR Pfam; PF01759; NTR; 1.
DR Pfam; PF07678; TED_complement; 1.
DR PRINTS; PR00004; ANAPHYLATOXN.
DR SFLD; SFLDG01179; Complement_C3/C4_Like; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SMART; SM00104; ANATO; 1.
DR SMART; SM00643; C345C; 1.
DR SMART; SM01419; Thiol-ester_cl; 1.
DR SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR SUPFAM; SSF47686; Anaphylotoxins (complement system); 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR SUPFAM; SSF50242; TIMP-like; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
DR PROSITE; PS50189; NTR; 1.
PE 4: Predicted;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Complement alternate pathway {ECO:0000256|ARBA:ARBA00023162};
KW Complement pathway {ECO:0000256|ARBA:ARBA00022875};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Inflammatory response {ECO:0000256|ARBA:ARBA00023198};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Thioester bond {ECO:0000256|ARBA:ARBA00022966}.
FT DOMAIN 667..702
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
FT DOMAIN 1481..1624
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
SQ SEQUENCE 1626 AA; 182191 MW; 01E5FFF08E3704D8 CRC64;
MFSIITPNVL RLESEETIVL EAHEAQGDVP VTVTVHDFPK KQVLTSEKTV LTSATGHLSS
ITIKIPASKE FQSNKGQKYV TVVASFGATI VEKVVLVSFQ SGYLFIQTDK TIYTPGSTVL
YRIFTVDNKL LPVARTVIVT IETPDGVPIK RDTLSSHNQY GILSLSWNIP ELVNMGQWKI
RAFYEHSPQK IFTAEFEVKE YVLPSFEVLV EPAEKFYYID DPKGLEVSIT ARFLYGKNVD
GMAFVIFGVQ DGDKKISLAH SLTRVMIEDG LGEAVLKRQV LLDGVRPSNA DALVGKSLYV
SATVILHSGS DMVEAERTGI PIVTSPYEIH FTKTSKFFKP AMPFDLMVFV TNPDGSPARR
VPVVTQGSDA QALTQDDGVA KLSVNTPNNR NALKITVRTK KEGIPEARQA TNTMNAQPYG
TMHNSNNYLH LSVSRVELKP RDNLNVNFHL RTDPGQDAKI HYYTYLVMNK GKLLKAGRQI
REPGQDLVVL SLPITPDFIP SFRLVAYYTL IGASGRREVV ADSVWVDVKD SCVGTLVVKG
DQRDNRQPAP GQQMTLRIEG NQGARVGLVA VDKGVFVLNK KNKLTQSKIW DVVEKADIGC
TPGSGKDYAG VFMDAGLAFK TSDGLQTEQR KDPECTKPAA RRRRSVQLME KRMGKVGQYT
DKGLRKCCED GMRDIPMRLS CQRRARFITQ GESCVKAFTD CCNYMAELRQ KHQRDQVLGL
ARSDMDEDII PEEDIVSRTQ FPESWLWTIE ELKEPERNGI STKVMNIFLK DSITTWEILA
VSLSDKKGIC VADPYEITVM QDFFIDLRLP YSVVRNEQVE IRAVLFNYRE QDKLKVRVEL
LHNPAFCSLA TAKKRYYQII EIPAKSSVAV PYVIVPLKTG LQEVEVKAAV YGHFISDGIK
KTLKVVPEGM RVNKTVAIHT LDPEHLGKGG VQKVDIPAAD LSDQVPDTDS ETRILLQGTP
VVQMTEDAVD GERLKHLIVT PSGCGEQNMI GMTPTVIAVH YLDQTEQWEK FGLEKRQESL
ELIKKGYTQQ LAFKQPSFAY AAFNNRPPST WLTAYVVKVF SLAANLIAID SQVLCGAVKW
LILEKQKPDG VFQEDGPVIH QEMIGGLRNA KEADVSLTAF VLIALQEARE ICEGQINSLP
GSINKAGEYI EASYLNLKRP YTVAIAAYAL ALMGKLEEPY LTKFLNTATE RNRWEEPGQK
LYNVEATSYA LLALLLLKDF DSVPPVVRWL NEQRYYGGGY GSTQANVPDH KDLNMDVSFH
LPSRSSPTMF RLHWEAGSLL RSEETKQNEA FSLTAKGKGQ GTLSVVTVYH AKVKGKGKVP
CKKFDLRVSI DPAPETAKKP QEAQSTKILN ICTRYLGDVD ATMSILDISM MTGFVPDTND
LELLSSGVDR YISKYEMTKA YSTRSTLIIY LEKISHSEEE CLSFKVHQFF NVGLIQPGSV
KVYSYYNLDE SCTQFYHLDK ADGMLSKLCH NEMCRCAEEN CFMHQAQEKV SLNERLEKAC
EPGVDYVYKT KLVTTELSDD FDEYIMTIEQ VIKSGSDEVQ AGQERRFISH IKCREALKLQ
KGKHYLIWGL SSDLWGEKPN TSYIIGKDTW VELWPEAEEC QDAENQKQCE NLGAFTETMV
VFGCPN
//
