Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000023622723 – 1661Complement C3Add BLAST1639
ChainiPRO_000023622823 – 665Complement C3 beta chainBy similarityAdd BLAST643
ChainiPRO_0000430428567 – 665C3-beta-cBy similarityAdd BLAST99
ChainiPRO_0000236229670 – 1661Complement C3 alpha chainBy similarityAdd BLAST992
ChainiPRO_0000236230670 – 746C3a anaphylatoxinBy similarityAdd BLAST77
ChainiPRO_0000419934670 – 745Acylation stimulating proteinBy similarityAdd BLAST76
ChainiPRO_0000236231747 – 1661Complement C3b alpha' chainBy similarityAdd BLAST915
ChainiPRO_0000273938747 – 953Complement C3c alpha' chain fragment 1By similarityAdd BLAST207
ChainiPRO_0000273939954 – 1302Complement C3dg fragmentBy similarityAdd BLAST349
ChainiPRO_0000273940954 – 1000Complement C3g fragmentBy similarityAdd BLAST47
ChainiPRO_00002362321001 – 1302Complement C3d fragmentBy similarityAdd BLAST302
PeptideiPRO_00002739411303 – 1319Complement C3f fragmentBy similarityAdd BLAST17
ChainiPRO_00002739421320 – 1661Complement C3c alpha' chain fragment 2By similarityAdd BLAST342

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei38PhosphoserineBy similarity1
Modified residuei70PhosphoserineBy similarity1
Disulfide bondi557 ↔ 815Interchain (between beta and alpha chains)PROSITE-ProRule annotation
Disulfide bondi625 ↔ 660By similarity
Modified residuei670PhosphoserineBy similarity1
Disulfide bondi691 ↔ 718By similarity
Disulfide bondi692 ↔ 725By similarity
Disulfide bondi705 ↔ 726By similarity
Disulfide bondi872 ↔ 1511By similarity
Glycosylationi938N-linked (GlcNAc...)Sequence analysis1
Modified residuei967PhosphoserineBy similarity1
Cross-linki1009 ↔ 1012Isoglutamyl cysteine thioester (Cys-Gln)By similarity
Disulfide bondi1100 ↔ 1157By similarity
Modified residuei1320PhosphoserineBy similarity1
Disulfide bondi1357 ↔ 1487By similarity
Disulfide bondi1388 ↔ 1456By similarity
Disulfide bondi1504 ↔ 1509By similarity
Disulfide bondi1516 ↔ 1588By similarity
Disulfide bondi1535 ↔ 1659By similarity
Modified residuei1571PhosphoserineBy similarity1
Disulfide bondi1635 ↔ 1644By similarity
Glycosylationi1649N-linked (GlcNAc...)Sequence analysis1

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)DescriptionActionsGraphical viewLength
Sitei745 – 746Cleavage; by carboxypeptidasesBy similarity2
Sitei746 – 747Cleavage; by C3 convertaseBy similarity2
Sitei953 – 954Cleavage; by factor IBy similarity2
Sitei1302 – 1303Cleavage; by factor IBy similarity2
Sitei1319 – 1320Cleavage; by factor IBy similarity2

Keywords - PTMi

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

Proteomic databases

PaxDbiQ2UVX4.
PeptideAtlasiQ2UVX4.
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

11661
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi31 – 34Combined sources4
Beta strandi38 – 45Combined sources8
Beta strandi51 – 54Combined sources4
Beta strandi62 – 64Combined sources3
Beta strandi75 – 77Combined sources3
Turni78 – 81Combined sources4
Beta strandi82 – 89Combined sources8
Beta strandi105 – 111Combined sources7
Beta strandi114 – 122Combined sources9
Beta strandi128 – 134Combined sources7
Beta strandi136 – 138Combined sources3
Beta strandi142 – 151Combined sources10
Beta strandi162 – 168Combined sources7
Beta strandi171 – 179Combined sources9
Turni181 – 185Combined sources5
Beta strandi189 – 193Combined sources5
Beta strandi201 – 209Combined sources9
Beta strandi212 – 223Combined sources12
Beta strandi234 – 236Combined sources3
Beta strandi238 – 241Combined sources4
Beta strandi252 – 255Combined sources4
Beta strandi257 – 261Combined sources5
Beta strandi266 – 275Combined sources10
Helixi284 – 286Combined sources3
Beta strandi288 – 295Combined sources8
Beta strandi297 – 299Combined sources3
Turni303 – 306Combined sources4
Beta strandi307 – 309Combined sources3
Helixi314 – 317Combined sources4
Beta strandi318 – 320Combined sources3
Beta strandi324 – 331Combined sources8
Turni332 – 334Combined sources3
Beta strandi351 – 353Combined sources3
Beta strandi356 – 358Combined sources3
Beta strandi361 – 363Combined sources3
Beta strandi365 – 370Combined sources6
Turni378 – 380Combined sources3
Beta strandi388 – 390Combined sources3
Beta strandi400 – 402Combined sources3
Beta strandi408 – 411Combined sources4
Beta strandi418 – 424Combined sources7
Beta strandi427 – 429Combined sources3
Beta strandi437 – 443Combined sources7
Helixi447 – 449Combined sources3
Beta strandi453 – 457Combined sources5
Beta strandi468 – 476Combined sources9
Turni479 – 481Combined sources3
Helixi482 – 484Combined sources3
Beta strandi487 – 493Combined sources7
Beta strandi495 – 505Combined sources11
Beta strandi513 – 518Combined sources6
Helixi521 – 523Combined sources3
Beta strandi527 – 533Combined sources7
Beta strandi545 – 551Combined sources7
Beta strandi562 – 567Combined sources6
Beta strandi578 – 585Combined sources8
Beta strandi590 – 596Combined sources7
Helixi598 – 601Combined sources4
Helixi605 – 607Combined sources3
Helixi611 – 618Combined sources8
Beta strandi621 – 623Combined sources3
Helixi632 – 639Combined sources8
Beta strandi646 – 648Combined sources3
Helixi672 – 682Combined sources11
Helixi688 – 694Combined sources7
Helixi705 – 708Combined sources4
Helixi709 – 711Combined sources3
Helixi716 – 736Combined sources21
Turni756 – 758Combined sources3
Beta strandi769 – 774Combined sources6
Beta strandi786 – 793Combined sources8
Beta strandi799 – 805Combined sources7
Beta strandi807 – 809Combined sources3
Turni810 – 812Combined sources3
Beta strandi813 – 815Combined sources3
Beta strandi820 – 823Combined sources4
Beta strandi827 – 833Combined sources7
Beta strandi838 – 841Combined sources4
Beta strandi843 – 852Combined sources10
Beta strandi859 – 865Combined sources7
Beta strandi882 – 887Combined sources6
Beta strandi892 – 901Combined sources10
Beta strandi905 – 920Combined sources16
Beta strandi922 – 931Combined sources10
Beta strandi933 – 946Combined sources14
Helixi948 – 951Combined sources4
Beta strandi953 – 955Combined sources3
Beta strandi957 – 961Combined sources5
Beta strandi967 – 969Combined sources3
Beta strandi976 – 984Combined sources9
Helixi987 – 993Combined sources7
Turni996 – 998Combined sources3
Helixi999 – 1001Combined sources3
Beta strandi1002 – 1005Combined sources4
Helixi1012 – 1016Combined sources5
Helixi1018 – 1030Combined sources13
Helixi1033 – 1035Combined sources3
Helixi1040 – 1056Combined sources17
Helixi1075 – 1088Combined sources14
Turni1089 – 1091Combined sources3
Helixi1096 – 1109Combined sources14
Helixi1140 – 1152Combined sources13
Turni1153 – 1160Combined sources8
Helixi1164 – 1178Combined sources15
Turni1179 – 1181Combined sources3
Helixi1185 – 1197Combined sources13
Helixi1203 – 1212Combined sources10
Turni1215 – 1217Combined sources3
Helixi1225 – 1242Combined sources18
Turni1245 – 1247Combined sources3
Helixi1249 – 1257Combined sources9
Helixi1268 – 1284Combined sources17
Helixi1288 – 1290Combined sources3
Beta strandi1296 – 1298Combined sources3
Beta strandi1300 – 1304Combined sources5
Beta strandi1310 – 1315Combined sources6
Beta strandi1317 – 1321Combined sources5
Beta strandi1329 – 1333Combined sources5
Beta strandi1339 – 1349Combined sources11
Beta strandi1358 – 1368Combined sources11
Beta strandi1382 – 1391Combined sources10
Beta strandi1393 – 1395Combined sources3
Beta strandi1399 – 1405Combined sources7
Beta strandi1410 – 1412Combined sources3
Helixi1414 – 1422Combined sources9
Beta strandi1423 – 1425Combined sources3
Beta strandi1429 – 1439Combined sources11
Beta strandi1441 – 1447Combined sources7
Beta strandi1451 – 1453Combined sources3
Beta strandi1455 – 1463Combined sources9
Beta strandi1465 – 1469Combined sources5
Beta strandi1473 – 1479Combined sources7
Beta strandi1485 – 1491Combined sources7
Helixi1506 – 1511Combined sources6
Turni1512 – 1516Combined sources5
Turni1529 – 1534Combined sources6
Beta strandi1539 – 1551Combined sources13
Beta strandi1554 – 1566Combined sources13
Beta strandi1576 – 1578Combined sources3
Beta strandi1581 – 1585Combined sources5
Turni1586 – 1588Combined sources3
Helixi1589 – 1592Combined sources4
Beta strandi1599 – 1606Combined sources8
Helixi1633 – 1636Combined sources4
Helixi1639 – 1646Combined sources8
Helixi1647 – 1649Combined sources3
Turni1650 – 1653Combined sources4
Beta strandi1654 – 1656Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B39X-ray3.00A/B1-1661[»]
SMRiQ2UVX4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2UVX4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini691 – 726Anaphylatoxin-likePROSITE-ProRule annotationAdd BLAST36
Domaini1516 – 1659NTRPROSITE-ProRule annotationAdd BLAST144

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1423 – 1454Properdin-bindingBy similarityAdd BLAST32

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)DescriptionActionsGraphical viewLength
Sequence conflicti533Y → N in AAI12453 (Ref. 2) Curated1
Sequence conflicti747S → I in AAI12453 (Ref. 2) Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B39X-ray3.00A/B1-1661[»]
SMRiQ2UVX4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022979.

Protein family/group databases

MEROPSiI39.950.

Proteomic databases

PaxDbiQ2UVX4.
PeptideAtlasiQ2UVX4.
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...

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: November 2, 2016
This is version 84 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.