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UniProtKB - P01025 (CO3_PIG)

Entry version 116 (23 Feb 2022)
Sequence version 2 (31 Oct 2012)
Previous versions | rss
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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

Acts as a chemoattractant for neutrophils in chronic inflammation.

By similarity

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

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>Sitei1661Coordinates Mg2+ for interaction with Complement factor B Bb fragmentBy similarity1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Suina › Suidae › Sus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000314985 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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
  • UP000008227 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

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 – 22By similarityAdd BLAST22
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<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%5Fprocessing%5Fsection">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%5Fprocessing%5Fsection">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%5Fprocessing%5Fsection">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
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%5Fsection">'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%5Fsection">'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). 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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		P01025, 1 interactor

STRING: functional protein association networks

More...STRINGi		9823.ENSSSCP00000027363

<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

More...ModBasei		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%5Fand%5Fdomains%5Fsection">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>Regioni947 – 969DisorderedSequence analysisAdd BLAST23
Regioni1632 – 1657Interaction with CFP/properdinBy similarityAdd BLAST26

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1366, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P01025

Database of Orthologous Groups

More...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

More...Gene3Di		2.40.50.120, 1 hit
2.60.40.10, 2 hits
2.60.40.690, 1 hit

Integrated resource of protein families, domains and functional sites

More...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

More...PANTHERi		PTHR11412:SF81, PTHR11412:SF81, 1 hit

Pfam protein domain database

More...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

More...PRINTSi		PR00004, ANAPHYLATOXN

Simple Modular Architecture Research Tool; a protein domain database

More...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

More...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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

More...PIRi		A01259

NCBI Reference Sequences

More...RefSeqi		NP_999174.1, NM_214009.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		397072

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...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...

Protein-protein interaction databases

IntActiP01025, 1 interactor
STRINGi9823.ENSSSCP00000027363

Protein family/group databases

MEROPSiI39.950

Proteomic databases

PaxDbiP01025
PeptideAtlasiP01025
PRIDEiP01025

Genome annotation databases

GeneIDi397072
KEGGissc:397072

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		718

Phylogenomic databases

eggNOGiKOG1366, Eukaryota
InParanoidiP01025
OrthoDBi23785at2759

Family and domain databases

CDDicd00017, ANATO, 1 hit
cd03583, NTR_complement_C3, 1 hit
Gene3Di2.40.50.120, 1 hit
2.60.40.10, 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

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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%5Fand%5Fisoforms">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: February 23, 2022
This is version 116 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

Direct protein sequencing, Reference proteome
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