Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 165 (02 Jun 2021)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
Add a publicationFeedback
Protein

Lanosterol 14-alpha demethylase

Gene

Cyp51a1

Organism
Rattus norvegicus (Rat)
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

A cytochrome P450 monooxygenase involved in sterol biosynthesis. Catalyzes 14-alpha demethylation of lanosterol and 24,25-dihydrolanosterol likely through sequential oxidative conversion of 14-alpha methyl group to hydroxymethyl, then to carboxylaldehyde, followed by the formation of the delta 14,15 double bond in the sterol core and concomitant release of formic acid (PubMed:7665087, PubMed:10544287, PubMed:11328599).

Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:7665087, PubMed:10544287, PubMed:11328599).

3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

hemeBy similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Inhibited by azalanstat (PubMed:7665087). Inhibited by azole antifungal agents ketoconazole, itraconazole and fluconazole (PubMed:10544287).2 Publications

<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=10.5 µM for lanosterol1 Publication
  2. KM=20.0 µM for 24,25-dihydrolanosterol1 Publication
  1. Vmax=13.9 nmol/min/nmol enzyme toward lanosterol1 Publication
  2. Vmax=20.0 nmol/min/nmol enzyme toward 24,25-dihydrolanosterol1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: zymosterol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes zymosterol from lanosterol.1 Publication This subpathway is part of the pathway zymosterol biosynthesis, which is itself part of Steroid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes zymosterol from lanosterol, the pathway zymosterol biosynthesis and in Steroid biosynthesis.

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 bindingi449Iron (heme axial ligand)By 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

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 functionMonooxygenase, Oxidoreductase
Biological processCholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.14.14.154, 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-191273, Cholesterol biosynthesis
R-RNO-211976, Endogenous sterols

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00770;UER00754

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001302

<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:
Lanosterol 14-alpha demethylase1 Publication (EC:1.14.14.1543 Publications)
Short name:
LDM
Alternative name(s):
CYPLI
Cytochrome P450 51A1
Cytochrome P450-14DM
Short name:
Cytochrome P45014DM
Cytochrome P450LI
Sterol 14-alpha demethylase
<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:Cyp51a11 PublicationImported
Synonyms:Cyp51
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 4

Organism-specific databases

Rat genome database

More...
RGDi
2481, Cyp51

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei24 – 44HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

<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%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>Mutagenesisi130V → A: Decreases lanosterol 14-alpha demethylase activity. 1 Publication1
Mutagenesisi136T → A or V: Decreases lanosterol 14-alpha demethylase activity. 1 Publication1
Mutagenesisi139F → A: Impairs lanosterol 14-alpha demethylase activity. 1 Publication1
Mutagenesisi144A → I or V: Decreases lanosterol 14-alpha demethylase activity. Increases the susceptibility to ketoconazole. 1 Publication1
Mutagenesisi227Y → A: Significatly decreases lanosterol 14-alpha demethylase activity. Increases the susceptibility to ketoconazole. 1 Publication1
Mutagenesisi231D → A or E: Significatly decreases lanosterol 14-alpha demethylase activity. 1 Publication1
Mutagenesisi314H → F, A, K or D: Significatly decreases lanosterol 14-alpha demethylase activity. Increases the susceptibility to ketoconazole. 1 Publication1
Mutagenesisi315T → A, V, K or N: Impairs lanosterol 14-alpha demethylase activity. Increases the susceptibility to ketoconazole. 1 Publication1
Mutagenesisi316S → T, V or L: Significatly decreases lanosterol 14-alpha demethylase activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4981

DrugCentral

More...
DrugCentrali
Q64654

<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 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_00000520011 – 503Lanosterol 14-alpha demethylaseAdd BLAST503

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q64654

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

More...
PaxDbi
Q64654

PRoteomics IDEntifications database

More...
PRIDEi
Q64654

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000007234, Expressed in liver and 22 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q64654, RN

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
247462, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000009985

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q64654

<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
Q64654

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

<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 cytochrome P450 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0684, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00930000151026

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_001570_15_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q64654

Identification of Orthologs from Complete Genome Data

More...
OMAi
AWTLIEL

Database of Orthologous Groups

More...
OrthoDBi
572303at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q64654

TreeFam database of animal gene trees

More...
TreeFami
TF105091

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.630.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001128, Cyt_P450
IPR017972, Cyt_P450_CS
IPR002403, Cyt_P450_E_grp-IV
IPR036396, Cyt_P450_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00067, p450, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00465, EP450IV
PR00385, P450

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48264, SSF48264, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00086, CYTOCHROME_P450, 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.

Q64654-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVLLGLLQSG GSVLGQAMEQ VTGGNLLSTL LIACAFTLSL VYLFRLAVGH
60 70 80 90 100
MVQLPAGAKS PPYIYSPIPF LGHAIAFGKS PIEFLENAYE KYGPVFSFTM
110 120 130 140 150
VGKTFTYLLG SDAAALLFNS KNEDLNAEEV YGRLTTPVFG KGVAYDVPNA
160 170 180 190 200
VFLEQKKILK SGLNIAHFKQ YVSIIEKEAK EYFKSWGESG ERNVFEALSE
210 220 230 240 250
LIILTASHCL HGKEIRSQLN EKVAQLYADL DGGFSHAAWL LPGWLPLPSF
260 270 280 290 300
RRRDRAHREI KNIFYKAIQK RRLSKEPAED ILQTLLDSTY KDGRPLTDDE
310 320 330 340 350
IAGMLIGLLL AGQHTSSTTS AWMGFFLARD KPLQDKCYLE QKTVCGEDLP
360 370 380 390 400
PLTYEQLKDL NLLDRCIKET LRLRPPIMTM MRMAKTPQTV AGYTIPPGHQ
410 420 430 440 450
VCVSPTVNQR LKDSWVERLD FNPDRYLQDN PASGEKFAYV PFGAGRHRCI
460 470 480 490 500
GENFAYVQIK TIWSTMLRLY EFDLINGYFP SVNYTTMIHT PENPVIRYKR

RSK
Length:503
Mass (Da):56,707
Last modified:November 1, 1996 - 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:i33D8F345FFE9CF21
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 conflicti181E → K in AAA87074 (PubMed:7665087).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
D55681 mRNA Translation: BAA09529.1
AB004096 Genomic DNA Translation: BAA20354.1
BC087033 mRNA Translation: AAH87033.1
U17697 mRNA Translation: AAA87074.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JC4240
JC4758

NCBI Reference Sequences

More...
RefSeqi
NP_037073.1, NM_012941.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000009985; ENSRNOP00000009985; ENSRNOG00000007234

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
25427

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:25427

UCSC genome browser

More...
UCSCi
RGD:2481, rat

<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
D55681 mRNA Translation: BAA09529.1
AB004096 Genomic DNA Translation: BAA20354.1
BC087033 mRNA Translation: AAH87033.1
U17697 mRNA Translation: AAA87074.1
PIRiJC4240
JC4758
RefSeqiNP_037073.1, NM_012941.2

3D structure databases

SMRiQ64654
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi247462, 1 interactor
STRINGi10116.ENSRNOP00000009985

Chemistry databases

BindingDBiQ64654
ChEMBLiCHEMBL4981
DrugCentraliQ64654
SwissLipidsiSLP:000001302

Proteomic databases

jPOSTiQ64654
PaxDbiQ64654
PRIDEiQ64654

Genome annotation databases

EnsembliENSRNOT00000009985; ENSRNOP00000009985; ENSRNOG00000007234
GeneIDi25427
KEGGirno:25427
UCSCiRGD:2481, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
13121
RGDi2481, Cyp51

Phylogenomic databases

eggNOGiKOG0684, Eukaryota
GeneTreeiENSGT00930000151026
HOGENOMiCLU_001570_15_0_1
InParanoidiQ64654
OMAiAWTLIEL
OrthoDBi572303at2759
PhylomeDBiQ64654
TreeFamiTF105091

Enzyme and pathway databases

UniPathwayiUPA00770;UER00754
BRENDAi1.14.14.154, 5301
ReactomeiR-RNO-191273, Cholesterol biosynthesis
R-RNO-211976, Endogenous sterols

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q64654

Gene expression databases

BgeeiENSRNOG00000007234, Expressed in liver and 22 other tissues
GenevisibleiQ64654, RN

Family and domain databases

Gene3Di1.10.630.10, 1 hit
InterProiView protein in InterPro
IPR001128, Cyt_P450
IPR017972, Cyt_P450_CS
IPR002403, Cyt_P450_E_grp-IV
IPR036396, Cyt_P450_sf
PfamiView protein in Pfam
PF00067, p450, 1 hit
PRINTSiPR00465, EP450IV
PR00385, P450
SUPFAMiSSF48264, SSF48264, 1 hit
PROSITEiView protein in PROSITE
PS00086, CYTOCHROME_P450, 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 nameiCP51A_RAT
<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: Q64654
Secondary accession number(s): Q64549
<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: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 2, 2021
This is version 165 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 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again