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Entry version 105 (08 May 2019)
Sequence version 2 (31 Oct 2012)
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Protein

Complement C3

Gene

C3

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 post-prandial 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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Protein family/group databases

MEROPS protease database

More...
MEROPSi
I39.950

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:C3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSus scrofa (Pig)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9823 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000008227 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 22Sequence analysisAdd BLAST22
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000041992223 – 1661Complement C3Add BLAST1639
ChainiPRO_000041992323 – 665Complement C3 beta chainBy similarityAdd BLAST643
ChainiPRO_0000430432567 – 665C3-beta-cBy similarityAdd BLAST99
ChainiPRO_0000419924670 – 1661Complement C3 alpha chainBy similarityAdd BLAST992
ChainiPRO_0000419925670 – 746C3a anaphylatoxinAdd BLAST77
ChainiPRO_0000419926670 – 745Acylation stimulating proteinBy similarityAdd BLAST76
ChainiPRO_0000419927747 – 1661Complement C3b alpha' chainBy similarityAdd BLAST915
ChainiPRO_0000419928747 – 953Complement C3c alpha' chain fragment 1By similarityAdd BLAST207
ChainiPRO_0000419929954 – 1302Complement C3dg fragmentBy similarityAdd BLAST349
ChainiPRO_0000419930954 – 1000Complement C3g fragmentBy similarityAdd BLAST47
ChainiPRO_00004199311001 – 1302Complement C3d fragmentBy similarityAdd BLAST302
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_00004199321303 – 1319Complement C3f fragmentBy similarityAdd BLAST17
ChainiPRO_00004199331320 – 1661Complement C3c alpha' chain fragment 2By similarityAdd BLAST342

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei38PhosphoserineBy similarity1
Modified residuei70PhosphoserineBy similarity1
Modified residuei302PhosphoserineBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi557 ↔ 814Interchain (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 bondi871 ↔ 1511By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi937N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei966PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki1008 ↔ 1011Isoglutamyl cysteine thioester (Cys-Gln)By similarity
Disulfide bondi1099 ↔ 1156By similarity
Modified residuei1319PhosphoserineBy similarity1
Disulfide bondi1356 ↔ 1487By similarity
Disulfide bondi1387 ↔ 1456By similarity
Disulfide bondi1504 ↔ 1509By similarity
Disulfide bondi1516 ↔ 1588By similarity
Disulfide bondi1535 ↔ 1659By similarity
Modified residuei1571PhosphoserineBy similarity1
Glycosylationi1615N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1635 ↔ 1644By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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 carboxylases to release the C-termianl arginine residue generating the acylation stimulating protein (ASP). Levels of ASP are increased in adipocytes in the postprandial period and by insulin and dietary chylomicrons (By similarity).By similarity
Phosphorylated by FAM20C in the extracellular medium.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei745 – 746Cleavage; by carboxypeptidasesBy similarity2
Sitei746 – 747Cleavage; by C3 convertaseBy similarity2
Sitei1301 – 1302Cleavage; by factor IBy similarity2
Sitei1318 – 1319Cleavage; by factor IBy similarity2

Keywords - PTMi

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

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P01025

PeptideAtlas

More...
PeptideAtlasi
P01025

PRoteomics IDEntifications database

More...
PRIDEi
P01025

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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). 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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
gCC7EYC82EBI-11688674,EBI-11688666From Suid alphaherpesvirus 1.

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P01025, 1 interactor

STRING: functional protein association networks

More...
STRINGi
9823.ENSSSCP00000014399

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P01025

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini691 – 726Anaphylatoxin-likePROSITE-ProRule annotationAdd BLAST36
Domaini1516 – 1659NTRPROSITE-ProRule annotationAdd BLAST144

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1422 – 1454Properdin-bindingBy similarityAdd BLAST33

Keywords - Domaini

Signal

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P01025

KEGG Orthology (KO)

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KOi
K03990

Database of Orthologous Groups

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OrthoDBi
23785at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00017 ANATO, 1 hit
cd03583 NTR_complement_C3, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.10, 2 hits
2.60.40.690, 1 hit

Integrated resource of protein families, domains and functional sites

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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

The PANTHER Classification System

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PANTHERi
PTHR11412:SF81 PTHR11412:SF81, 1 hit

Pfam protein domain database

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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

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00004 ANAPHYLATOXN

Simple Modular Architecture Research Tool; a protein domain database

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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

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47686 SSF47686, 1 hit
SSF48239 SSF48239, 1 hit
SSF49410 SSF49410, 1 hit
SSF50242 SSF50242, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00477 ALPHA_2_MACROGLOBULIN, 1 hit
PS01177 ANAPHYLATOXIN_1, 1 hit
PS01178 ANAPHYLATOXIN_2, 1 hit
PS50189 NTR, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P01025-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGSTSGPRLL LLLLTSLPLA LGDPIYTIIT PNVLRLESEE MVVLEAHEGQ
60 70 80 90 100
GDIRVSVTVH DFPAKRQVLS SETTTLNNAN NYLSTVNIKI PASKEFKSEK
110 120 130 140 150
GHKFVTVQAL FGNVQVEKVV LVSLQSGYLF IQTDKTIYTP GSTVLYRIFT
160 170 180 190 200
VDHKLLPVGQ TIVVTIETPE GIDIKRDSLS SHNQFGILAL SWNIPELVNM
210 220 230 240 250
GQWKIRAHYE DAPQQVFSAE FEVKEYVLPS FEVQVEPSEK FYYIDDPNGL
260 270 280 290 300
TVNIIARFLY GESVDGTAFV IFGVQDGDQR ISLSQSLTRV PIIDGTGEAT
310 320 330 340 350
LSQGVLLNGV HYSSVNDLVG KSIYVSVTVI LNSGSDMVEA ERTGIPIVTS
360 370 380 390 400
PYQIHFTKTP KFFKPAMPFD LMVYVTNPDG SPARHIPVVT EDFKVRSLTQ
410 420 430 440 450
EDGVAKLSIN TPDNRNSLPI TVRTEKDGIP AARQASKTMH VLPYNTQGNS
460 470 480 490 500
KNYLHLSLPR VELKPGENLN VNFHLRTDPG YQDKIRYFTY LIMNKGKLLK
510 520 530 540 550
VGRQPRESGQ VVVVLPLTIT TDFIPSFRLV AYYTLIAANG QREVVADSVW
560 570 580 590 600
VDVKDSCVGT LVVKGGGKQD KQHRPGQQMT LEIQGERGAR VGLVAVDKGV
610 620 630 640 650
FVLNKKNKLT QRRIWDVVEK ADIGCTPGSG KDFAGVFTDA GLAFKSSKGL
660 670 680 690 700
QTPQRADLEC PKPAARKRRS VQLMEKRMDK LGQYSKDVRR CCEHGMRDNP
710 720 730 740 750
MKFSCQRRAQ FIQHGDACVK AFLDCCEYIA KLRQQHSRNK PLGLARSDLD
760 770 780 790 800
EEIIPEEDII SRSQFPESWL WTIEEFKEPD KNGISTKTMN VFLKDSITTW
810 820 830 840 850
EILAVSLSDK KGICVADPYE VVVKQDFFID LRLPYSVVRN EQVEIRAILY
860 870 880 890 900
NYREAEDLKV RVELLYNPAF CSLATAKKRH QQTLTVPAKS SVPVPYIIVP
910 920 930 940 950
LKTGLQEVEV KAAVYNHFIS DGVKKTLKVV PEGMRVNKTV VTRTLDPEHK
960 970 980 990 1000
GQQGVQREEI PPADLSDQVP DTESETKILL QGTPVAQMVE DAIDGDRLKH
1010 1020 1030 1040 1050
LIQTPSGCGE QNMIGMTPTV IAVHYLDSTE QWEKFGLEKR QEALELIKKG
1060 1070 1080 1090 1100
YTQQLAFRQK NSAFAAFQDR LSSTLLTAYV VKVFAMAANL IAIDSQVLCG
1110 1120 1130 1140 1150
AVKWLILEKQ KPDGVFEENG PVIHQEMIGG FKNTEEKDVS LTAFVLIALQ
1160 1170 1180 1190 1200
EAKDICEPQV NSLLRSINKA RDFLADYYLE LKRPYTVAIA GYALALSDKL
1210 1220 1230 1240 1250
DEPFLNKLLS TAKERNRWEE PGQKLHNVEA TSYALLALLV VKDFDSVPPI
1260 1270 1280 1290 1300
VRWLNEQRYY GGGYGSTQAT FMVFQALAQY QKDVPDHKDL NLDVSIHLPS
1310 1320 1330 1340 1350
RSAPVRHRIL WESASLLRSE ETKENEGFTL IAEGKGQGTL SVVTMYHGKA
1360 1370 1380 1390 1400
KGKTTCKKFD LKVSIHPAPE PVKKPQEAKS SMVLDICTRY LGNQDATMSI
1410 1420 1430 1440 1450
LDISMMTGFS PDTEDLKLLS TGVDRYISKY ELNKALSNKN TLIIYLDKIS
1460 1470 1480 1490 1500
HTLEDCISFK VHQYFNVGLI QPGSVKVYSY YNLDESCTRF YHPEKEDGML
1510 1520 1530 1540 1550
NKLCHKEMCR CAEENCFMHH DEEEVTLDDR LERACEPGVD YVYKTRLLKK
1560 1570 1580 1590 1600
ELSDDFDDYI MVIEQIIKSG SDEVQVGQER RFISHIKCRE ALKLKEGGHY
1610 1620 1630 1640 1650
LVWGVSSDLW GEKPNISYII GKDTWVELWP DGDVCQDEEN QKQCQDLANF
1660
SENMVVFGCP N
Length:1,661
Mass (Da):186,807
Last modified:October 31, 2012 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4899D0914BE3310C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti679D → N AA sequence (PubMed:956663).Curated1
Sequence conflicti687 – 688DV → EL AA sequence (PubMed:956663).Curated2
Sequence conflicti698D → N AA sequence (PubMed:956663).Curated1
Sequence conflicti713 – 716QHGD → HQGN AA sequence (PubMed:956663).Curated4
Sequence conflicti724D → N AA sequence (PubMed:956663).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF154933 mRNA Translation: AAG40565.1
AJ494748 Genomic DNA Translation: CAD38823.2
AF110278 mRNA Translation: AAC99785.1

Protein sequence database of the Protein Information Resource

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PIRi
A01259

NCBI Reference Sequences

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RefSeqi
NP_999174.1, NM_214009.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
397072

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
ssc:397072

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF154933 mRNA Translation: AAG40565.1
AJ494748 Genomic DNA Translation: CAD38823.2
AF110278 mRNA Translation: AAC99785.1
PIRiA01259
RefSeqiNP_999174.1, NM_214009.1

3D structure databases

SMRiP01025
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP01025, 1 interactor
STRINGi9823.ENSSSCP00000014399

Protein family/group databases

MEROPSiI39.950

Proteomic databases

PaxDbiP01025
PeptideAtlasiP01025
PRIDEiP01025

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397072
KEGGissc:397072

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
718

Phylogenomic databases

InParanoidiP01025
KOiK03990
OrthoDBi23785at2759

Family and domain databases

CDDicd00017 ANATO, 1 hit
cd03583 NTR_complement_C3, 1 hit
Gene3Di2.60.40.10, 2 hits
2.60.40.690, 1 hit
InterProiView 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
PANTHERiPTHR11412:SF81 PTHR11412:SF81, 1 hit
PfamiView 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
PRINTSiPR00004 ANAPHYLATOXN
SMARTiView 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
SUPFAMiSSF47686 SSF47686, 1 hit
SSF48239 SSF48239, 1 hit
SSF49410 SSF49410, 1 hit
SSF50242 SSF50242, 1 hit
PROSITEiView protein in PROSITE
PS00477 ALPHA_2_MACROGLOBULIN, 1 hit
PS01177 ANAPHYLATOXIN_1, 1 hit
PS01178 ANAPHYLATOXIN_2, 1 hit
PS50189 NTR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCO3_PIG
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P01025
Secondary accession number(s): O97940, Q9GKP1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 31, 2012
Last modified: May 8, 2019
This is version 105 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
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