UniProtKB - Q2UVX4 (CO3_BOVIN)
Complement C3
C3
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 similarityDerived 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 similarityActs as a chemoattractant for neutrophils in chronic inflammation.
By similarityAdipogenic 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 similaritySites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 1661 | Coordinates Mg2+ for interaction with Complement factor B Bb fragmentBy similarity | 1 |
GO - Molecular functioni
- C5L2 anaphylatoxin chemotactic receptor binding Source: UniProtKB
- endopeptidase inhibitor activity Source: InterPro
GO - Biological processi
- amyloid-beta clearance Source: Ensembl
- cell surface receptor signaling pathway involved in cell-cell signaling Source: Ensembl
- complement activation Source: GO_Central
- complement activation, alternative pathway Source: UniProtKB-KW
- complement activation, classical pathway Source: UniProtKB-KW
- complement-dependent cytotoxicity Source: Ensembl
- complement-mediated synapse pruning Source: Ensembl
- fatty acid metabolic process Source: UniProtKB-KW
- inflammatory response Source: UniProtKB-KW
- neuron remodeling Source: Ensembl
- oviduct epithelium development Source: Ensembl
- positive regulation of activation of membrane attack complex Source: Ensembl
- positive regulation of angiogenesis Source: Ensembl
- positive regulation of apoptotic cell clearance Source: Ensembl
- positive regulation of glucose transmembrane transport Source: UniProtKB
- positive regulation of G protein-coupled receptor signaling pathway Source: UniProtKB
- positive regulation of lipid storage Source: UniProtKB
- positive regulation of phagocytosis, engulfment Source: Ensembl
- positive regulation of protein phosphorylation Source: UniProtKB
- positive regulation of receptor-mediated endocytosis Source: Ensembl
- positive regulation of type IIa hypersensitivity Source: Ensembl
- positive regulation of vascular endothelial growth factor production Source: Ensembl
- regulation of triglyceride biosynthetic process Source: UniProtKB
- response to bacterium Source: Ensembl
- vertebrate eye-specific patterning Source: Ensembl
Keywordsi
Biological process | Complement alternate pathway, Complement pathway, Fatty acid metabolism, Immunity, Inflammatory response, Innate immunity, Lipid metabolism |
Protein family/group databases
MEROPSi | I39.950 |
Names & Taxonomyi
Protein namesi | Recommended name: Complement C3Cleaved into the following 12 chains: Alternative name(s): C3adesArg |
Gene namesi | Name:C3 |
Organismi | Bos taurus (Bovine) |
Taxonomic identifieri | 9913 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | HostDB:ENSBTAG00000017280 |
VGNCi | VGNC:26638, C3 |
Subcellular locationi
Extracellular region or secreted
Extracellular region or secreted
- extracellular space Source: GO_Central
Other locations
- cell surface Source: Ensembl
- protein-containing complex Source: Ensembl
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 22 | By similarityAdd BLAST | 22 | |
ChainiPRO_0000236227 | 23 – 1661 | Complement C3Add BLAST | 1639 | |
ChainiPRO_0000236228 | 23 – 665 | Complement C3 beta chainBy similarityAdd BLAST | 643 | |
ChainiPRO_0000430428 | 567 – 665 | C3-beta-cBy similarityAdd BLAST | 99 | |
ChainiPRO_0000236229 | 670 – 1661 | Complement C3 alpha chainBy similarityAdd BLAST | 992 | |
ChainiPRO_0000236230 | 670 – 746 | C3a anaphylatoxinBy similarityAdd BLAST | 77 | |
ChainiPRO_0000419934 | 670 – 745 | Acylation stimulating proteinBy similarityAdd BLAST | 76 | |
ChainiPRO_0000236231 | 747 – 1661 | Complement C3b alpha' chainBy similarityAdd BLAST | 915 | |
ChainiPRO_0000273938 | 747 – 953 | Complement C3c alpha' chain fragment 1By similarityAdd BLAST | 207 | |
ChainiPRO_0000273939 | 954 – 1302 | Complement C3dg fragmentBy similarityAdd BLAST | 349 | |
ChainiPRO_0000273940 | 954 – 1000 | Complement C3g fragmentBy similarityAdd BLAST | 47 | |
ChainiPRO_0000236232 | 1001 – 1302 | Complement C3d fragmentBy similarityAdd BLAST | 302 | |
PeptideiPRO_0000273941 | 1303 – 1319 | Complement C3f fragmentBy similarityAdd BLAST | 17 | |
ChainiPRO_0000273942 | 1320 – 1661 | Complement C3c alpha' chain fragment 2By similarityAdd BLAST | 342 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 38 | PhosphoserineBy similarity | 1 | |
Modified residuei | 70 | PhosphoserineBy similarity | 1 | |
Disulfide bondi | 557 ↔ 815 | Interchain (between beta and alpha chains)PROSITE-ProRule annotation | ||
Disulfide bondi | 625 ↔ 660 | By similarity | ||
Modified residuei | 670 | PhosphoserineBy similarity | 1 | |
Disulfide bondi | 691 ↔ 718 | By similarity | ||
Disulfide bondi | 692 ↔ 725 | By similarity | ||
Disulfide bondi | 705 ↔ 726 | By similarity | ||
Disulfide bondi | 872 ↔ 1511 | By similarity | ||
Glycosylationi | 938 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 967 | PhosphoserineBy similarity | 1 | |
Cross-linki | 1009 ↔ 1012 | Isoglutamyl cysteine thioester (Cys-Gln)By similarity | ||
Disulfide bondi | 1100 ↔ 1157 | By similarity | ||
Modified residuei | 1320 | PhosphoserineBy similarity | 1 | |
Disulfide bondi | 1357 ↔ 1487 | By similarity | ||
Disulfide bondi | 1388 ↔ 1456 | By similarity | ||
Disulfide bondi | 1504 ↔ 1509 | By similarity | ||
Disulfide bondi | 1516 ↔ 1588 | By similarity | ||
Disulfide bondi | 1535 ↔ 1659 | By similarity | ||
Modified residuei | 1571 | PhosphoserineBy similarity | 1 | |
Disulfide bondi | 1635 ↔ 1644 | By similarity | ||
Glycosylationi | 1649 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 745 – 746 | Cleavage; by carboxypeptidasesBy similarity | 2 | |
Sitei | 746 – 747 | Cleavage; by C3 convertaseBy similarity | 2 | |
Sitei | 953 – 954 | Cleavage; by factor IBy similarity | 2 | |
Sitei | 1302 – 1303 | Cleavage; by factor IBy similarity | 2 | |
Sitei | 1319 – 1320 | Cleavage; by factor IBy similarity | 2 |
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Thioester bondProteomic databases
PaxDbi | Q2UVX4 |
PeptideAtlasi | Q2UVX4 |
PRIDEi | Q2UVX4 |
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). Forms the pro-C3-convertase enzyme complex by binding to Complement factor B Bb fragment (Bb), which is then stabilized by binding CFP, allowing the complex to become active (By similarity). The interaction with Bb is dependent on Mg2+ (By similarity). C3b interacts with CR1 (via Sushi 8 and Sushi 9 domains). C3b interacts with CFH. C3d interacts with CFH. C3dg interacts with CR2 (via the N-terminal Sushi domains 1 and 2). During pregnancy, C3dg exists as a complex (probably a 2:2:2 heterohexamer) with AGT and the proform of PRG2.
Interacts with VSIG4.
Interacts with S.aureus immunoglobulin-binding protein sbi, this prevents interaction between C3dg and CR2.
Interacts with S.aureus fib.
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(Microbial infection) Interacts with BHV-1 GLYCOPROTEIN C.
1 PublicationGO - Molecular functioni
- C5L2 anaphylatoxin chemotactic receptor binding Source: UniProtKB
Protein-protein interaction databases
STRINGi | 9913.ENSBTAP00000022979 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | Q2UVX4 |
SMRi | Q2UVX4 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q2UVX4 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 691 – 726 | Anaphylatoxin-likePROSITE-ProRule annotationAdd BLAST | 36 | |
Domaini | 1516 – 1659 | NTRPROSITE-ProRule annotationAdd BLAST | 144 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1632 – 1657 | Interaction with CFP/properdinBy similarityAdd BLAST | 26 |
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | KOG1366, Eukaryota |
GeneTreei | ENSGT00940000154063 |
InParanoidi | Q2UVX4 |
OMAi | QATNTMQ |
OrthoDBi | 23785at2759 |
Family and domain databases
CDDi | cd00017, ANATO, 1 hit cd03583, NTR_complement_C3, 1 hit |
Gene3Di | 2.40.50.120, 1 hit 2.60.40.10, 2 hits 2.60.40.690, 1 hit |
InterProi | View protein in InterPro IPR009048, A-macroglobulin_rcpt-bd IPR036595, A-macroglobulin_rcpt-bd_sf IPR011625, A2M_N_BRD IPR011626, Alpha-macroglobulin_TED IPR000020, Anaphylatoxin/fibulin IPR018081, Anaphylatoxin_comp_syst IPR001840, Anaphylatoxn_comp_syst_dom IPR041425, C3/4/5_MG1 IPR035711, Complement_C3-like IPR013783, Ig-like_fold IPR001599, Macroglobln_a2 IPR019742, MacrogloblnA2_CS IPR002890, MG2 IPR041555, MG3 IPR040839, MG4 IPR001134, Netrin_domain IPR018933, Netrin_module_non-TIMP IPR035815, NTR_complement_C3 IPR008930, Terpenoid_cyclase/PrenylTrfase IPR008993, TIMP-like_OB-fold |
PANTHERi | PTHR11412:SF81, PTHR11412:SF81, 1 hit |
Pfami | View protein in Pfam PF00207, A2M, 1 hit PF07703, A2M_BRD, 1 hit PF07677, A2M_recep, 1 hit PF01821, ANATO, 1 hit PF17790, MG1, 1 hit PF01835, MG2, 1 hit PF17791, MG3, 1 hit PF17789, MG4, 1 hit PF01759, NTR, 1 hit PF07678, TED_complement, 1 hit |
PRINTSi | PR00004, ANAPHYLATOXN |
SMARTi | View protein in SMART SM01360, A2M, 1 hit SM01359, A2M_N_2, 1 hit SM01361, A2M_recep, 1 hit SM00104, ANATO, 1 hit SM00643, C345C, 1 hit |
SUPFAMi | SSF47686, SSF47686, 1 hit SSF48239, SSF48239, 1 hit SSF49410, SSF49410, 1 hit SSF50242, SSF50242, 1 hit |
PROSITEi | View protein in PROSITE PS00477, ALPHA_2_MACROGLOBULIN, 1 hit PS01178, ANAPHYLATOXIN_2, 1 hit PS50189, NTR, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All
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
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A3Q1M2B2 | A0A3Q1M2B2_BOVIN | Complement C3 | C3 | 1,630 | Annotation score: | ||
A0A3Q1MGT0 | A0A3Q1MGT0_BOVIN | Complement C3 | C3 | 1,610 | Annotation score: | ||
A0A3Q1MHV6 | A0A3Q1MHV6_BOVIN | Complement C3 | C3 | 1,601 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 533 | Y → N in AAI12453 (Ref. 2) Curated | 1 | |
Sequence conflicti | 747 | S → I in AAI12453 (Ref. 2) Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AM086793 Genomic DNA Translation: CAJ31249.1 BC112452 mRNA Translation: AAI12453.1 |
RefSeqi | NP_001035559.2, NM_001040469.2 XP_010805188.1, XM_010806886.2 |
Genome annotation databases
Ensembli | ENSBTAT00000022979; ENSBTAP00000022979; ENSBTAG00000017280 |
GeneIDi | 280677 |
KEGGi | bta:280677 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AM086793 Genomic DNA Translation: CAJ31249.1 BC112452 mRNA Translation: AAI12453.1 |
RefSeqi | NP_001035559.2, NM_001040469.2 XP_010805188.1, XM_010806886.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2B39 | X-ray | 3.00 | A/B | 1-1661 | [»] | |
AlphaFoldDBi | Q2UVX4 | |||||
SMRi | Q2UVX4 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 9913.ENSBTAP00000022979 |
Protein family/group databases
MEROPSi | I39.950 |
Proteomic databases
PaxDbi | Q2UVX4 |
PeptideAtlasi | Q2UVX4 |
PRIDEi | Q2UVX4 |
Genome annotation databases
Ensembli | ENSBTAT00000022979; ENSBTAP00000022979; ENSBTAG00000017280 |
GeneIDi | 280677 |
KEGGi | bta:280677 |
Organism-specific databases
CTDi | 718 |
VEuPathDBi | HostDB:ENSBTAG00000017280 |
VGNCi | VGNC:26638, C3 |
Phylogenomic databases
eggNOGi | KOG1366, Eukaryota |
GeneTreei | ENSGT00940000154063 |
InParanoidi | Q2UVX4 |
OMAi | QATNTMQ |
OrthoDBi | 23785at2759 |
Miscellaneous databases
EvolutionaryTracei | Q2UVX4 |
Gene expression databases
ExpressionAtlasi | Q2UVX4, baseline and differential |
Family and domain databases
CDDi | cd00017, ANATO, 1 hit cd03583, NTR_complement_C3, 1 hit |
Gene3Di | 2.40.50.120, 1 hit 2.60.40.10, 2 hits 2.60.40.690, 1 hit |
InterProi | View protein in InterPro IPR009048, A-macroglobulin_rcpt-bd IPR036595, A-macroglobulin_rcpt-bd_sf IPR011625, A2M_N_BRD IPR011626, Alpha-macroglobulin_TED IPR000020, Anaphylatoxin/fibulin IPR018081, Anaphylatoxin_comp_syst IPR001840, Anaphylatoxn_comp_syst_dom IPR041425, C3/4/5_MG1 IPR035711, Complement_C3-like IPR013783, Ig-like_fold IPR001599, Macroglobln_a2 IPR019742, MacrogloblnA2_CS IPR002890, MG2 IPR041555, MG3 IPR040839, MG4 IPR001134, Netrin_domain IPR018933, Netrin_module_non-TIMP IPR035815, NTR_complement_C3 IPR008930, Terpenoid_cyclase/PrenylTrfase IPR008993, TIMP-like_OB-fold |
PANTHERi | PTHR11412:SF81, PTHR11412:SF81, 1 hit |
Pfami | View protein in Pfam PF00207, A2M, 1 hit PF07703, A2M_BRD, 1 hit PF07677, A2M_recep, 1 hit PF01821, ANATO, 1 hit PF17790, MG1, 1 hit PF01835, MG2, 1 hit PF17791, MG3, 1 hit PF17789, MG4, 1 hit PF01759, NTR, 1 hit PF07678, TED_complement, 1 hit |
PRINTSi | PR00004, ANAPHYLATOXN |
SMARTi | View protein in SMART SM01360, A2M, 1 hit SM01359, A2M_N_2, 1 hit SM01361, A2M_recep, 1 hit SM00104, ANATO, 1 hit SM00643, C345C, 1 hit |
SUPFAMi | SSF47686, SSF47686, 1 hit SSF48239, SSF48239, 1 hit SSF49410, SSF49410, 1 hit SSF50242, SSF50242, 1 hit |
PROSITEi | View protein in PROSITE PS00477, ALPHA_2_MACROGLOBULIN, 1 hit PS01178, ANAPHYLATOXIN_2, 1 hit PS50189, NTR, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CO3_BOVIN | |
Accessioni | Q2UVX4Primary (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: | May 25, 2022 | |
This is version 111 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references