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Entry version 88 (02 Jun 2021)
Sequence version 2 (19 Oct 2011)
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Protein

Chondroitin sulfate ABC endolyase

Gene
N/A
Organism
Proteus vulgaris
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

Endolytic, broad-specificity glycosaminoglycan lyase, which degrades the polysaccharides chondroitin, chondroitin-4-sulfate, chondroitin-6-sulfate, dermatan sulfate and to a lesser extent hyaluronan, by beta-elimination of 1,4-hexosaminidic bond to unsaturated tetrasaccharides and disaccharides. Is not active against keratan sulfate, heparan sulfate, and heparin. Is able to promote functional recovery in the injured central nervous system (CNS), via its role in the disruption of the normal organization of the extracellular matrix (ECM).

3 Publications

Caution

PubMed:7512814 shows amino acid differences at positions 317, 321, 410, 694, 738 and 866 due to incorrect translation of the nucleotide sequence.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Is inhibited by Zn2+, Ni2+, Fe2+ and Cu2+.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=66 µM for chondroitin 6-sulfate2 Publications
  2. KM=1.2 µM for chondroitin 6-sulfate2 Publications
  3. KM=1.5 µM for chondroitin 4-sulfate2 Publications
  4. KM=2.5 µM for dermatan sulfate2 Publications
  1. Vmax=310 µmol/min/mg enzyme with chondroitin 6-sulfate as substrate2 Publications

pH dependencei

Optimum pH is 8. Is essentially inactive at pH 9.0.2 Publications

Temperature dependencei

Optimum temperature is 37 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi43Sodium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi70Sodium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi73Sodium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi211SodiumCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei501Proton acceptor2 Publications1
Active sitei508Proton donorSequence analysis1
<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>Sitei560Transition state stabilizerSequence analysis1
Sitei653Important for catalytic activity1

<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

Molecular functionLyase
Biological processCarbohydrate metabolism
LigandCalcium, Metal-binding, Sodium

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-15788

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.2.2.20, 5049

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
PL8, Polysaccharide Lyase Family 8

<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
Recommended name:
Chondroitin sulfate ABC endolyase (EC:4.2.2.20)
Alternative name(s):
Chondroitin ABC endoeliminase
Chondroitin ABC lyase I
Chondroitin sulfate ABC lyase I
Short name:
ChS ABC lyase I
Chondroitinase ABC I
Short name:
cABC I
Endochondroitinase ABC
INN: Condoliase
<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>OrganismiProteus vulgaris
<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 identifieri585 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesMorganellaceaeProteus

<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

Periplasm

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi500R → A: Still active on both chondroitin 6-sulfate and dermatan sulfate, but with highly reduced catalytic efficiency. 2 Publications1
Mutagenesisi501H → A, K or R: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 2 Publications1
Mutagenesisi508Y → A: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 2 Publications1
Mutagenesisi508Y → F: Still active on both chondroitin 6-sulfate and dermatan sulfate, but with greatly reduced catalytic efficiency. 2 Publications1
Mutagenesisi560R → A: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 2 Publications1
Mutagenesisi561H → A: Still active on both chondroitin 6-sulfate and dermatan sulfate, but with reduced catalytic efficiency. 1 Publication1
Mutagenesisi653E → A or D: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 2 Publications1
Mutagenesisi653E → Q: Still active on both chondroitin 6-sulfate and dermatan sulfate, but with reduced catalytic efficiency. 2 Publications1
Mutagenesisi712H → A: Still active on both chondroitin 6-sulfate and dermatan sulfate, but with reduced catalytic efficiency. 1 Publication1

<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 – 241 PublicationAdd BLAST24
<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_000002492925 – 1021Chondroitin sulfate ABC endolyaseAdd BLAST997

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By chondroitin sulfate or its degraded products.1 Publication

<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

Monomer.

1 Publication

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P59807, 2 interactors

Molecular INTeraction database

More...
MINTi
P59807

STRING: functional protein association networks

More...
STRINGi
585.DR95_2846

<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

11021
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
P59807

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
P59807

<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

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Consists of three domains. The middle domain contains the catalytic site in a wide-open cleft.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the polysaccharide lyase 8 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502Z8J1, Bacteria

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.50.10.100, 1 hit
2.60.220.10, 1 hit
2.70.98.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR039174, Chondroitin_ABC_lyase
IPR008929, Chondroitin_lyas
IPR024200, Chondroitinase_ABC_I
IPR011013, Gal_mutarotase_sf_dom
IPR008979, Galactose-bd-like_sf
IPR014718, GH-type_carb-bd
IPR011071, Lyase_8-like_C
IPR004103, Lyase_8_C
IPR003159, Lyase_8_central_dom
IPR015177, Lyase_catalyt
IPR015176, Lyase_N

The PANTHER Classification System

More...
PANTHERi
PTHR37322, PTHR37322, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02278, Lyase_8, 1 hit
PF02884, Lyase_8_C, 1 hit
PF09093, Lyase_catalyt, 1 hit
PF09092, Lyase_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF034515, Chondroitinase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48230, SSF48230, 1 hit
SSF49785, SSF49785, 1 hit
SSF49863, SSF49863, 1 hit
SSF74650, SSF74650, 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>. 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_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.

P59807-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPIFRFTALA MTLGLLSAPY NAMAATSNPA FDPKNLMQSE IYHFAQNNPL
60 70 80 90 100
ADFSSDKNSI LTLSDKRSIM GNQSLLWKWK GGSSFTLHKK LIVPTDKEAS
110 120 130 140 150
KAWGRSSTPV FSFWLYNEKP IDGYLTIDFG EKLISTSEAQ AGFKVKLDFT
160 170 180 190 200
GWRAVGVSLN NDLENREMTL NATNTSSDGT QDSIGRSLGA KVDSIRFKAP
210 220 230 240 250
SNVSQGEIYI DRIMFSVDDA RYQWSDYQVK TRLSEPEIQF HNVKPQLPVT
260 270 280 290 300
PENLAAIDLI RQRLINEFVG GEKETNLALE ENISKLKSDF DALNIHTLAN
310 320 330 340 350
GGTQGRHLIT DKQIIIYQPE NLNSQDKQLF DNYVILGNYT TLMFNISRAY
360 370 380 390 400
VLEKDPTQKA QLKQMYLLMT KHLLDQGFVK GSALVTTHHW GYSSRWWYIS
410 420 430 440 450
TLLMSDALKE ANLQTQVYDS LLWYSREFKS SFDMKVSADS SDLDYFNTLS
460 470 480 490 500
RQHLALLLLE PDDQKRINLV NTFSHYITGA LTQVPPGGKD GLRPDGTAWR
510 520 530 540 550
HEGNYPGYSF PAFKNASQLI YLLRDTPFSV GESGWNNLKK AMVSAWIYSN
560 570 580 590 600
PEVGLPLAGR HPFNSPSLKS VAQGYYWLAM SAKSSPDKTL ASIYLAISDK
610 620 630 640 650
TQNESTAIFG ETITPASLPQ GFYAFNGGAF GIHRWQDKMV TLKAYNTNVW
660 670 680 690 700
SSEIYNKDNR YGRYQSHGVA QIVSNGSQLS QGYQQEGWDW NRMQGATTIH
710 720 730 740 750
LPLKDLDSPK PHTLMQRGER GFSGTSSLEG QYGMMAFDLI YPANLERFDP
760 770 780 790 800
NFTAKKSVLA ADNHLIFIGS NINSSDKNKN VETTLFQHAI TPTLNTLWIN
810 820 830 840 850
GQKIENMPYQ TTLQQGDWLI DSNGNGYLIT QAEKVNVSRQ HQVSAENKNR
860 870 880 890 900
QPTEGNFSSA WIDHSTRPKD ASYEYMVFLD ATPEKMGEMA QKFRENNGLY
910 920 930 940 950
QVLRKDKDVH IILDKLSNVT GYAFYQPASI EDKWIKKVNK PAIVMTHRQK
960 970 980 990 1000
DTLIVSAVTP DLNMTRQKAA TPVTINVTIN GKWQSADKNS EVKYQVSGDN
1010 1020
TELTFTSYFG IPQEIKLSPL P
Length:1,021
Mass (Da):115,092
Last modified:October 19, 2011 - 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:i299406E6466568AC
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence described in PubMed:7512814 differs from that shown. Reason: Frameshift.Curated

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 conflicti125L → P no nucleotide entry (PubMed:7512814).Curated1
Sequence conflicti369M → V no nucleotide entry (PubMed:7512814).Curated1
Sequence conflicti670A → G no nucleotide entry (PubMed:7512814).Curated1
Sequence conflicti865S → R no nucleotide entry (PubMed:7512814).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
GQ996964 Genomic DNA Translation: ACY01450.1

<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
GQ996964 Genomic DNA Translation: ACY01450.1

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
1HN0X-ray1.90A1-1021[»]
SMRiP59807
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP59807, 2 interactors
MINTiP59807
STRINGi585.DR95_2846

Protein family/group databases

CAZyiPL8, Polysaccharide Lyase Family 8

Phylogenomic databases

eggNOGiENOG502Z8J1, Bacteria

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15788
BRENDAi4.2.2.20, 5049

Miscellaneous databases

EvolutionaryTraceiP59807

Family and domain databases

Gene3Di1.50.10.100, 1 hit
2.60.220.10, 1 hit
2.70.98.10, 1 hit
InterProiView protein in InterPro
IPR039174, Chondroitin_ABC_lyase
IPR008929, Chondroitin_lyas
IPR024200, Chondroitinase_ABC_I
IPR011013, Gal_mutarotase_sf_dom
IPR008979, Galactose-bd-like_sf
IPR014718, GH-type_carb-bd
IPR011071, Lyase_8-like_C
IPR004103, Lyase_8_C
IPR003159, Lyase_8_central_dom
IPR015177, Lyase_catalyt
IPR015176, Lyase_N
PANTHERiPTHR37322, PTHR37322, 1 hit
PfamiView protein in Pfam
PF02278, Lyase_8, 1 hit
PF02884, Lyase_8_C, 1 hit
PF09093, Lyase_catalyt, 1 hit
PF09092, Lyase_N, 1 hit
PIRSFiPIRSF034515, Chondroitinase, 1 hit
SUPFAMiSSF48230, SSF48230, 1 hit
SSF49785, SSF49785, 1 hit
SSF49863, SSF49863, 1 hit
SSF74650, SSF74650, 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 nameiCABC1_PROVU
<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: P59807
Secondary accession number(s): D0V0C9
<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: August 15, 2003
Last sequence update: October 19, 2011
Last modified: June 2, 2021
This is version 88 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 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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