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Protein

Complement C3

Gene

C3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates (By similarity).By similarity
Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. In chronic inflammation, acts as a chemoattractant for neutrophils (By similarity).By similarity
C3-beta-c: Acts as a chemoattractant for neutrophils in chronic inflammation.By similarity
Acylation stimulating protein: adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-internalization and recycling of C5AR2 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Complement alternate pathway, Complement pathway, Fatty acid metabolism, Immunity, Inflammatory response, Innate immunity, Lipid metabolism

Protein family/group databases

MEROPSiI39.950.

Names & Taxonomyi

Protein namesi
Gene namesi
Name:C3
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 16611639Complement C3PRO_0000236227Add
BLAST
Chaini23 – 665643Complement C3 beta chainBy similarityPRO_0000236228Add
BLAST
Chaini567 – 66599C3-beta-cBy similarityPRO_0000430428Add
BLAST
Chaini670 – 1661992Complement C3 alpha chainBy similarityPRO_0000236229Add
BLAST
Chaini670 – 74677C3a anaphylatoxinBy similarityPRO_0000236230Add
BLAST
Chaini670 – 74576Acylation stimulating proteinBy similarityPRO_0000419934Add
BLAST
Chaini747 – 1661915Complement C3b alpha' chainBy similarityPRO_0000236231Add
BLAST
Chaini747 – 953207Complement C3c alpha' chain fragment 1By similarityPRO_0000273938Add
BLAST
Chaini954 – 1302349Complement C3dg fragmentBy similarityPRO_0000273939Add
BLAST
Chaini954 – 100047Complement C3g fragmentBy similarityPRO_0000273940Add
BLAST
Chaini1001 – 1302302Complement C3d fragmentBy similarityPRO_0000236232Add
BLAST
Peptidei1303 – 131917Complement C3f fragmentBy similarityPRO_0000273941Add
BLAST
Chaini1320 – 1661342Complement C3c alpha' chain fragment 2By similarityPRO_0000273942Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381PhosphoserineBy similarity
Modified residuei70 – 701PhosphoserineBy similarity
Disulfide bondi557 ↔ 815Interchain (between beta and alpha chains)PROSITE-ProRule annotation
Disulfide bondi625 ↔ 660By similarity
Modified residuei670 – 6701PhosphoserineBy similarity
Disulfide bondi691 ↔ 718By similarity
Disulfide bondi692 ↔ 725By similarity
Disulfide bondi705 ↔ 726By similarity
Disulfide bondi872 ↔ 1511By similarity
Glycosylationi938 – 9381N-linked (GlcNAc...)Sequence analysis
Modified residuei967 – 9671PhosphoserineBy similarity
Cross-linki1009 ↔ 1012Isoglutamyl cysteine thioester (Cys-Gln)By similarity
Disulfide bondi1100 ↔ 1157By similarity
Modified residuei1320 – 13201PhosphoserineBy similarity
Disulfide bondi1357 ↔ 1487By similarity
Disulfide bondi1388 ↔ 1456By similarity
Disulfide bondi1504 ↔ 1509By similarity
Disulfide bondi1516 ↔ 1588By similarity
Disulfide bondi1535 ↔ 1659By similarity
Modified residuei1571 – 15711PhosphoserineBy similarity
Disulfide bondi1635 ↔ 1644By similarity
Glycosylationi1649 – 16491N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

C3b is rapidly split in two positions by factor I and a cofactor to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha' chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other proteases produce other fragments such as C3d or C3g. C3a is further processed by carboxypeptidases to release the C-terminal arginine residue generating the acylation stimulating protein (ASP). Levels of ASP are increased in adipocytes in the postprandial period and by dietary chylomicrons (By similarity).By similarity
Phosphorylated by FAM20C in the extracellular medium.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei745 – 7462Cleavage; by carboxypeptidasesBy similarity
Sitei746 – 7472Cleavage; by C3 convertaseBy similarity
Sitei953 – 9542Cleavage; by factor IBy similarity
Sitei1302 – 13032Cleavage; by factor IBy similarity
Sitei1319 – 13202Cleavage; by factor IBy similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Thioester bond

Proteomic databases

PaxDbiQ2UVX4.
PRIDEiQ2UVX4.

Interactioni

Subunit structurei

C3 precursor is first processed by the removal of 4 Arg residues, forming two chains, beta and alpha, linked by a disulfide bond. C3 convertase activates C3 by cleaving the alpha chain, releasing C3a anaphylatoxin and generating C3b (beta chain + alpha' chain). C3dg interacts with CR2 (via the N-terminal Sushi domains 1 and 2). Interacts with VSIG4. Interacts (both C3a and ASP) with C5AR2; the interaction occurs with higher affinity for ASP, enhancing the phosphorylation and activation of C5AR2, recruitment of ARRB2 to the cell surface and endocytosis of GRP77 (By similarity). Interacts with BHV-1 glycoprotein C.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022979.

Structurei

Secondary structure

1
1661
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 344Combined sources
Beta strandi38 – 458Combined sources
Beta strandi51 – 544Combined sources
Beta strandi62 – 643Combined sources
Beta strandi75 – 773Combined sources
Turni78 – 814Combined sources
Beta strandi82 – 898Combined sources
Beta strandi105 – 1117Combined sources
Beta strandi114 – 1229Combined sources
Beta strandi128 – 1347Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi142 – 15110Combined sources
Beta strandi162 – 1687Combined sources
Beta strandi171 – 1799Combined sources
Turni181 – 1855Combined sources
Beta strandi189 – 1935Combined sources
Beta strandi201 – 2099Combined sources
Beta strandi212 – 22312Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi238 – 2414Combined sources
Beta strandi252 – 2554Combined sources
Beta strandi257 – 2615Combined sources
Beta strandi266 – 27510Combined sources
Helixi284 – 2863Combined sources
Beta strandi288 – 2958Combined sources
Beta strandi297 – 2993Combined sources
Turni303 – 3064Combined sources
Beta strandi307 – 3093Combined sources
Helixi314 – 3174Combined sources
Beta strandi318 – 3203Combined sources
Beta strandi324 – 3318Combined sources
Turni332 – 3343Combined sources
Beta strandi351 – 3533Combined sources
Beta strandi356 – 3583Combined sources
Beta strandi361 – 3633Combined sources
Beta strandi365 – 3706Combined sources
Turni378 – 3803Combined sources
Beta strandi388 – 3903Combined sources
Beta strandi400 – 4023Combined sources
Beta strandi408 – 4114Combined sources
Beta strandi418 – 4247Combined sources
Beta strandi427 – 4293Combined sources
Beta strandi437 – 4437Combined sources
Helixi447 – 4493Combined sources
Beta strandi453 – 4575Combined sources
Beta strandi468 – 4769Combined sources
Turni479 – 4813Combined sources
Helixi482 – 4843Combined sources
Beta strandi487 – 4937Combined sources
Beta strandi495 – 50511Combined sources
Beta strandi513 – 5186Combined sources
Helixi521 – 5233Combined sources
Beta strandi527 – 5337Combined sources
Beta strandi545 – 5517Combined sources
Beta strandi562 – 5676Combined sources
Beta strandi578 – 5858Combined sources
Beta strandi590 – 5967Combined sources
Helixi598 – 6014Combined sources
Helixi605 – 6073Combined sources
Helixi611 – 6188Combined sources
Beta strandi621 – 6233Combined sources
Helixi632 – 6398Combined sources
Beta strandi646 – 6483Combined sources
Helixi672 – 68211Combined sources
Helixi688 – 6947Combined sources
Helixi705 – 7084Combined sources
Helixi709 – 7113Combined sources
Helixi716 – 73621Combined sources
Turni756 – 7583Combined sources
Beta strandi769 – 7746Combined sources
Beta strandi786 – 7938Combined sources
Beta strandi799 – 8057Combined sources
Beta strandi807 – 8093Combined sources
Turni810 – 8123Combined sources
Beta strandi813 – 8153Combined sources
Beta strandi820 – 8234Combined sources
Beta strandi827 – 8337Combined sources
Beta strandi838 – 8414Combined sources
Beta strandi843 – 85210Combined sources
Beta strandi859 – 8657Combined sources
Beta strandi882 – 8876Combined sources
Beta strandi892 – 90110Combined sources
Beta strandi905 – 92016Combined sources
Beta strandi922 – 93110Combined sources
Beta strandi933 – 94614Combined sources
Helixi948 – 9514Combined sources
Beta strandi953 – 9553Combined sources
Beta strandi957 – 9615Combined sources
Beta strandi967 – 9693Combined sources
Beta strandi976 – 9849Combined sources
Helixi987 – 9937Combined sources
Turni996 – 9983Combined sources
Helixi999 – 10013Combined sources
Beta strandi1002 – 10054Combined sources
Helixi1012 – 10165Combined sources
Helixi1018 – 103013Combined sources
Helixi1033 – 10353Combined sources
Helixi1040 – 105617Combined sources
Helixi1075 – 108814Combined sources
Turni1089 – 10913Combined sources
Helixi1096 – 110914Combined sources
Helixi1140 – 115213Combined sources
Turni1153 – 11608Combined sources
Helixi1164 – 117815Combined sources
Turni1179 – 11813Combined sources
Helixi1185 – 119713Combined sources
Helixi1203 – 121210Combined sources
Turni1215 – 12173Combined sources
Helixi1225 – 124218Combined sources
Turni1245 – 12473Combined sources
Helixi1249 – 12579Combined sources
Helixi1268 – 128417Combined sources
Helixi1288 – 12903Combined sources
Beta strandi1296 – 12983Combined sources
Beta strandi1300 – 13045Combined sources
Beta strandi1310 – 13156Combined sources
Beta strandi1317 – 13215Combined sources
Beta strandi1329 – 13335Combined sources
Beta strandi1339 – 134911Combined sources
Beta strandi1358 – 136811Combined sources
Beta strandi1382 – 139110Combined sources
Beta strandi1393 – 13953Combined sources
Beta strandi1399 – 14057Combined sources
Beta strandi1410 – 14123Combined sources
Helixi1414 – 14229Combined sources
Beta strandi1423 – 14253Combined sources
Beta strandi1429 – 143911Combined sources
Beta strandi1441 – 14477Combined sources
Beta strandi1451 – 14533Combined sources
Beta strandi1455 – 14639Combined sources
Beta strandi1465 – 14695Combined sources
Beta strandi1473 – 14797Combined sources
Beta strandi1485 – 14917Combined sources
Helixi1506 – 15116Combined sources
Turni1512 – 15165Combined sources
Turni1529 – 15346Combined sources
Beta strandi1539 – 155113Combined sources
Beta strandi1554 – 156613Combined sources
Beta strandi1576 – 15783Combined sources
Beta strandi1581 – 15855Combined sources
Turni1586 – 15883Combined sources
Helixi1589 – 15924Combined sources
Beta strandi1599 – 16068Combined sources
Helixi1633 – 16364Combined sources
Helixi1639 – 16468Combined sources
Helixi1647 – 16493Combined sources
Turni1650 – 16534Combined sources
Beta strandi1654 – 16563Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B39X-ray3.00A/B1-1661[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2UVX4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini691 – 72636Anaphylatoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini1516 – 1659144NTRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1423 – 145432Properdin-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 anaphylatoxin-like domain.PROSITE-ProRule annotation
Contains 1 NTR domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
HOGENOMiHOG000286028.
HOVERGENiHBG005110.
InParanoidiQ2UVX4.
KOiK03990.

Family and domain databases

Gene3Di1.20.91.20. 1 hit.
1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProiIPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_comp_syst.
IPR001840. Anaphylatoxn_comp_syst_dom.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008993. TIMP-like_OB-fold.
[Graphical view]
PfamiPF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF01821. ANATO. 1 hit.
PF01759. NTR. 1 hit.
PF10569. Thiol-ester_cl. 1 hit.
[Graphical view]
PRINTSiPR00004. ANAPHYLATOXN.
SMARTiSM01360. A2M. 1 hit.
SM01359. A2M_N_2. 1 hit.
SM01361. A2M_recep. 1 hit.
SM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view]
SUPFAMiSSF47686. SSF47686. 1 hit.
SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF50242. SSF50242. 1 hit.
PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2UVX4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPTSGPSLL LLLLASLPMA LGNPMYSMIT PNILRLESEE TVVLEAHGGQ
60 70 80 90 100
GTIQVSVTVH DFPAKKQVLS NENTQLNSNN GYLSTVTIKI PASKELKSDK
110 120 130 140 150
GHKFVTVVAT FGNVQVEKVV LISLQSGYLF IQTDKTIYTP GSTVLYRVFT
160 170 180 190 200
VDHKLLPVGQ TVFITIETPD GIPVKRDSKS SQNQFGILTL SWNIPELVNM
210 220 230 240 250
GVWKIKAYYE DSPQQVFSAE FEVKEYVLPS FEVQLEPEEK FYYIDDPDGL
260 270 280 290 300
KVNIIARFLY GEQVDGTAFV IFGVQDGDRR ISLTHSLTRV PINDGNGEAI
310 320 330 340 350
LKRQVLLNGV QPSRADALVG KSIYVSATVI LQSGSDMVEA ERTGIPIVTS
360 370 380 390 400
PYQIHFTKTP KFFKPAMPFD LMVYVTNPDG SPARHIPVVT QGSNVQSLTQ
410 420 430 440 450
DDGVAKLSIN TQNKRDPLTI TVRTKKDNIP EGRQATRTMQ ALPYNTQGNS
460 470 480 490 500
NNYLHLSVPR VELKPGETLN VNFHLRTDPG EQAKIRYYTY MIMNKGKLLK
510 520 530 540 550
VGRQYREPGQ DLVVLPLTIT SDFIPSFRLV AYYTLINAKG QREVVADSVW
560 570 580 590 600
VDVKDSCMGT LVVKNGGKEE KHHRPGQQIT LKIEADQGAR VGLVAVDKGV
610 620 630 640 650
FVLNKKNKLT QRKIWDVVEK ADIGCTPGSG RNYAGVFTDA GLTLKTSQGL
660 670 680 690 700
ETQQRADPQC PQPATRRRRS VQLMEKRMDK AGQYSSDLRK CCEDGMRDNP
710 720 730 740 750
MKFPCQRRAQ FILQGDACVK AFLDCCEYIT QLRQQHSRDG ALELARSDLD
760 770 780 790 800
DDIIPEEDII SRSQFPESWL WTVIEDLKQA DKNGISTKLM NVFLKDSITT
810 820 830 840 850
WEILAVSLSD KKGICVADPY EVTVMQDFFI DLRLPYSVVR NEQVEIRAIL
860 870 880 890 900
YNYREAENLK VRVELLYNPA FCSLATAKKR HQQTITIPAR SSVAVPYVIV
910 920 930 940 950
PLKIGLHEVE VKAAVYNHFI SDGVKKTLKV VPEGVRVNKT VAVRTLNPEH
960 970 980 990 1000
LGQGGVQREE VPAADLSDQV PDTESETKIL LQGTPVAQMT EDAIDGERLK
1010 1020 1030 1040 1050
HLIQTPSGCG EQNMIGMTPT VIAVHYLDST DQWEKFGLEK RQESLELIRK
1060 1070 1080 1090 1100
GYTQQLAFRQ KSSAYAAFQY RPPSTWLTAY VVKVFALAAN LIAIDSKDLC
1110 1120 1130 1140 1150
ETVKWLILEK QKPDGIFQED GPVIHQEMIG GFRDTREKDV SLTAFVLIAL
1160 1170 1180 1190 1200
HEAKDICEAQ VNSLGRSIAK AGDFLENHYR ELRRPYTVAI AAYALALLGK
1210 1220 1230 1240 1250
LEGDRLTKFL NTAKEKNRWE EPNQKLYNVE ATSYALLALL ARKDYDTTPP
1260 1270 1280 1290 1300
VVRWLNEQRY YGGGYGSTQA TFMVFQALAQ YQKDVPDHKE LNLDVSIQLP
1310 1320 1330 1340 1350
SRNSAVRHRI LWESASLLRS EETKENERFT VKAEGKGQGT LSVVTVYHAK
1360 1370 1380 1390 1400
LKGKVSCKKF DLRVSIRPAP ETVKKPQDAK GSMILDICTK YLGDQDATMS
1410 1420 1430 1440 1450
ILDISMMTGF SPDVEDLKTL STGVDRYISK YEMNRDSNKN TLIIYLDKVS
1460 1470 1480 1490 1500
HTVEDCLSFK VHQYFNVGLI QPGAVKVYSY YNLDETCIRF YHPDKEDGML
1510 1520 1530 1540 1550
SKLCHKDTCR CAEENCFMHH TEKEVTLEDR LDKACEPGVD YVYKTRLIQK
1560 1570 1580 1590 1600
KLEDDFDEYI MVIENIIKSG SDEVQVKQER KFISHIKCRE ALKLKEGAHY
1610 1620 1630 1640 1650
LVWGVSSDLW GEKPKISYII GKDTWVELWP EAEECQDEEN QKQCEDLANF
1660
TENMVVFGCP N
Length:1,661
Mass (Da):187,253
Last modified:January 23, 2007 - v2
Checksum:i3EBBE948F0638AD2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti533 – 5331Y → N in AAI12453 (Ref. 2) Curated
Sequence conflicti747 – 7471S → I in AAI12453 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM086793 Genomic DNA. Translation: CAJ31249.1.
BC112452 mRNA. Translation: AAI12453.1.
RefSeqiNP_001035559.2. NM_001040469.2.
XP_010805188.1. XM_010806886.2.
UniGeneiBt.19562.

Genome annotation databases

GeneIDi280677.
KEGGibta:280677.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM086793 Genomic DNA. Translation: CAJ31249.1.
BC112452 mRNA. Translation: AAI12453.1.
RefSeqiNP_001035559.2. NM_001040469.2.
XP_010805188.1. XM_010806886.2.
UniGeneiBt.19562.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B39X-ray3.00A/B1-1661[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022979.

Protein family/group databases

MEROPSiI39.950.

Proteomic databases

PaxDbiQ2UVX4.
PRIDEiQ2UVX4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi280677.
KEGGibta:280677.

Organism-specific databases

CTDi718.

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
HOGENOMiHOG000286028.
HOVERGENiHBG005110.
InParanoidiQ2UVX4.
KOiK03990.

Miscellaneous databases

EvolutionaryTraceiQ2UVX4.

Family and domain databases

Gene3Di1.20.91.20. 1 hit.
1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProiIPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_comp_syst.
IPR001840. Anaphylatoxn_comp_syst_dom.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008993. TIMP-like_OB-fold.
[Graphical view]
PfamiPF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF01821. ANATO. 1 hit.
PF01759. NTR. 1 hit.
PF10569. Thiol-ester_cl. 1 hit.
[Graphical view]
PRINTSiPR00004. ANAPHYLATOXN.
SMARTiSM01360. A2M. 1 hit.
SM01359. A2M_N_2. 1 hit.
SM01361. A2M_recep. 1 hit.
SM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view]
SUPFAMiSSF47686. SSF47686. 1 hit.
SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF50242. SSF50242. 1 hit.
PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The structure of bovine complement component 3 reveals the basis for thioester function."
    Fredslund F., Jenner L., Husted L.B., Nyborg J., Andersen G.R., Sottrup-Jensen L.
    J. Mol. Biol. 361:115-127(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF C3.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Liver.
  3. "Species selective interaction of Alphaherpesvirinae with the 'unspecific' immune system of the host."
    Huemer H.P., Larcher C., van Drunen Littel-van den Hurk S., Babiuk L.A.
    Arch. Virol. 130:353-364(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BHV-1 GLYCOPROTEIN C.

Entry informationi

Entry nameiCO3_BOVIN
AccessioniPrimary (citable) accession number: Q2UVX4
Secondary accession number(s): Q2KIZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.