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UniProtKB - P07173 (CYCR_BLAVI)

Entry version 141 (10 Feb 2021)
Sequence version 1 (01 Apr 1988)
Previous versions | rss
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Protein

Photosynthetic reaction center cytochrome c subunit

Gene

pufC

Organism
Blastochloris viridis (Rhodopseudomonas viridis)
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

The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor.1 Publication

Redox potential

E0 is -60 mV for heme 1. E0 is +320 mV for heme 2. E0 is +380 mV for heme 3. E0 is +15 mV for heme 4.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi94Iron (heme 1 axial ligand)Combined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei107Heme 1 (covalent)Combined sources1 Publication1
Binding sitei110Heme 1 (covalent)Combined sources1 Publication1
Metal bindingi111Iron (heme 1 axial ligand); via tele nitrogenCombined sources1 Publication1
Metal bindingi130Iron (heme 2 axial ligand)Combined sources1 Publication1
Metal bindingi144Iron (heme 4 axial ligand); via tele nitrogenCombined sources1 Publication1
Binding sitei152Heme 2 (covalent)Combined sources1 Publication1
Binding sitei155Heme 2 (covalent)Combined sources1 Publication1
Metal bindingi156Iron (heme 2 axial ligand); via tele nitrogenCombined sources1 Publication1
Metal bindingi253Iron (heme 3 axial ligand)Combined sources1 Publication1
Binding sitei264Heme 3 (covalent)Combined sources1 Publication1
Binding sitei267Heme 3 (covalent)Combined sources1 Publication1
Metal bindingi268Iron (heme 3 axial ligand); via tele nitrogenCombined sources1 Publication1
Binding sitei325Heme 4 (covalent)Combined sources1 Publication1
Binding sitei328Heme 4 (covalent)Combined sources1 Publication1
Metal bindingi329Iron (heme 4 axial ligand); via tele nitrogenCombined sources1 Publication1

<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

  • photosynthesis Source: UniProtKB
  • photosynthesis, light reaction Source: InterPro
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 processElectron transport, Photosynthesis, Transport
LigandHeme, Iron, Metal-binding

<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
Recommended name:
Photosynthetic reaction center cytochrome c subunitUniRule annotation
Alternative name(s):
Cytochrome c558/c559
<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:pufCImported
Synonyms:cytC
ORF Names:BVIRIDIS_00500Imported
<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>OrganismiBlastochloris viridis (Rhodopseudomonas viridis)
<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 identifieri1079 [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 lineageiBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Hyphomicrobiaceae › Blastochloris
<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
  • UP000065734 <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: Chromosome I

<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

GO - Cellular componenti

  • plasma membrane-derived chromatophore membrane Source: UniProtKB
  • plasma membrane light-harvesting complex Source: InterPro
Complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Membrane, Reaction center

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Lack of photosynthesis.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi284R → K: 110 mV decrease in redox potential of heme 3. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB07552, (2R)-2-{[4-chloro-6-(ethylamino)-1,3,5-triazin-2-yl]amino}-2-methylbutanenitrile
DB07551, (2S)-2-{[4-chloro-6-(ethylamino)-1,3,5-triazin-2-yl]amino}-2-methylbutanenitrile
DB07392, Atrazine
DB04147, Dodecyldimethylamine N-oxide
DB04464, N-Formylmethionine
DB08215, Terbutryn
DB08689, Ubiquinone Q1
DB08690, Ubiquinone Q2

<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 – 20Add BLAST20
<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_000000655121 – 356Photosynthetic reaction center cytochrome c subunitAdd BLAST336

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi21S-diacylglycerol cysteinePROSITE-ProRule annotationCombined sources2 Publications1

<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

Binds 4 heme groups per subunit.6 Publications
After the signal sequence is removed, the N-terminal cysteine is modified to form a diacylglyceride thioether, but the alpha-amino group is free and is not N-palmitoylated.2 Publications

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>Sitei21Not N-palmitoylatedCombined sources2 Publications1

Keywords - PTMi

Lipoprotein

<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

Component of the photosynthetic reaction center composed of protein subunits L (PufL), M (PufM), H (PuhA) and cytochrome C (PufC).

5 Publications

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		P07173, 6 interactors

<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

Secondary structure

1356
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P07173

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P07173

<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

Keywords - Domaini

Signal

Phylogenomic databases

Identification of Orthologs from Complete Genome Data

More...OMAi		CTYCHNT

Family and domain databases

Conserved Domains Database

More...CDDi		cd09224, CytoC_RC, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.468.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011031, Multihaem_cyt
IPR023119, Multihaem_cyt_PRC_cyt_su-like
IPR036280, Multihaem_cyt_sf
IPR003158, Photosyn_RC_cyt_c-su

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02276, CytoC_RC, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000017, RC_cytochrome, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48695, SSF48695, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51008, MULTIHEME_CYTC, 1 hit
PS51257, PROKAR_LIPOPROTEIN, 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.

P07173-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKQLIVNSVA TVALASLVAG CFEPPPATTT QTGFRGLSMG EVLHPATVKA 
        60         70         80         90        100
KKERDAQYPP ALAAVKAEGP PVSQVYKNVK VLGNLTEAEF LRTMTAITEW 
       110        120        130        140        150
VSPQEGCTYC HDENNLASEA KYPYVVARRM LEMTRAINTN WTQHVAQTGV 
       160        170        180        190        200
TCYTCHRGTP LPPYVRYLEP TLPLNNRETP THVERVETRS GYVVRLAKYT 
       210        220        230        240        250
AYSALNYDPF TMFLANDKRQ VRVVPQTALP LVGVSRGKER RPLSDAYATF 
       260        270        280        290        300
ALMMSISDSL GTNCTFCHNA QTFESWGKKS TPQRAIAWWG IRMVRDLNMN 
       310        320        330        340        350
YLAPLNASLP ASRLGRQGEA PQADCRTCHQ GVTKPLFGAS RLKDYPELGP 

IKAAAK
Length:356
Mass (Da):39,371
Last modified:April 1, 1988 - v1
<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:iECE3D64F1BB0877A
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 conflicti63A → P in ACK86664 (PubMed:22054235).Curated1
Sequence conflicti97I → M in ACK86664 (PubMed:22054235).Curated1
Sequence conflicti104Q → E in ACK86664 (PubMed:22054235).Curated1
Sequence conflicti272T → S in ACK86664 (PubMed:22054235).Curated1
Sequence conflicti275S → T in ACK86664 (PubMed:22054235).Curated1
Sequence conflicti297L → M in ACK86664 (PubMed:22054235).Curated1
Sequence conflicti307 – 308AS → TV in ACK86664 (PubMed:22054235).Curated2
Sequence conflicti343K → Q in ACK86664 (PubMed:22054235).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
X05768 Genomic DNA Translation: CAA29223.1
FJ483785 Genomic DNA Translation: ACK86664.1
HQ009849 Genomic DNA Translation: ADN94690.1
LN907867 Genomic DNA Translation: CUU41065.1
M16317 Genomic DNA Translation: AAA26093.1

Protein sequence database of the Protein Information Resource

More...PIRi		S00139

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		CUU41065; CUU41065; BVIRIDIS_00500

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1079.6.peg.623

<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
X05768 Genomic DNA Translation: CAA29223.1
FJ483785 Genomic DNA Translation: ACK86664.1
HQ009849 Genomic DNA Translation: ADN94690.1
LN907867 Genomic DNA Translation: CUU41065.1
M16317 Genomic DNA Translation: AAA26093.1
PIRiS00139

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DXRX-ray2.00C21-356[»]
1PRCX-ray2.30C21-356[»]
1R2CX-ray2.86C21-356[»]
1VRNX-ray2.20C21-352[»]
2I5NX-ray1.96C21-356[»]
2JBLX-ray2.40C1-356[»]
2PRCX-ray2.45C21-356[»]
2WJMX-ray1.95C21-356[»]
2WJNX-ray1.86C21-356[»]
2X5UX-ray3.00C21-356[»]
2X5VX-ray3.00C21-356[»]
3D38X-ray3.21C21-356[»]
3G7FX-ray2.50C21-356[»]
3PRCX-ray2.40C21-356[»]
3T6DX-ray1.95C1-356[»]
3T6EX-ray1.92C1-356[»]
4AC5X-ray8.20C21-356[»]
4CASX-ray3.50A1-356[»]
5M7JX-ray3.50A1-356[»]
5M7KX-ray3.50A1-356[»]
5M7LX-ray3.60A1-356[»]
5NJ4X-ray2.40C21-356[»]
5O4CX-ray2.80C21-356[»]
5O64X-ray3.30C21-356[»]
5PRCX-ray2.35C21-356[»]
6ET5electron microscopy3.00C21-353[»]
6PRCX-ray2.30C21-356[»]
7PRCX-ray2.65C21-356[»]
SMRiP07173
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP07173, 6 interactors

Chemistry databases

DrugBankiDB07552, (2R)-2-{[4-chloro-6-(ethylamino)-1,3,5-triazin-2-yl]amino}-2-methylbutanenitrile
DB07551, (2S)-2-{[4-chloro-6-(ethylamino)-1,3,5-triazin-2-yl]amino}-2-methylbutanenitrile
DB07392, Atrazine
DB04147, Dodecyldimethylamine N-oxide
DB04464, N-Formylmethionine
DB08215, Terbutryn
DB08689, Ubiquinone Q1
DB08690, Ubiquinone Q2

Genome annotation databases

EnsemblBacteriaiCUU41065; CUU41065; BVIRIDIS_00500
PATRICifig|1079.6.peg.623

Phylogenomic databases

OMAiCTYCHNT

Miscellaneous databases

EvolutionaryTraceiP07173

Family and domain databases

CDDicd09224, CytoC_RC, 1 hit
Gene3Di1.10.468.10, 2 hits
InterProiView protein in InterPro
IPR011031, Multihaem_cyt
IPR023119, Multihaem_cyt_PRC_cyt_su-like
IPR036280, Multihaem_cyt_sf
IPR003158, Photosyn_RC_cyt_c-su
PfamiView protein in Pfam
PF02276, CytoC_RC, 1 hit
PIRSFiPIRSF000017, RC_cytochrome, 1 hit
SUPFAMiSSF48695, SSF48695, 1 hit
PROSITEiView protein in PROSITE
PS51008, MULTIHEME_CYTC, 1 hit
PS51257, PROKAR_LIPOPROTEIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiCYCR_BLAVI
<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: P07173
Secondary accession number(s): B8Y5U8, E2J7X6
<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: April 1, 1988
Last sequence update: April 1, 1988
Last modified: February 10, 2021
This is version 141 of the entry and version 1 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 programProkaryotic 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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