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UniProtKB - P08478 (AMDA_XENLA)

Entry version 127 (02 Dec 2020)
Sequence version 3 (23 Mar 2010)
Previous versions | rss
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Protein

Peptidyl-glycine alpha-amidating monooxygenase A

Gene

pam-a

Organism
Xenopus laevis (African clawed frog)
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

Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.1 Publication

<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

Protein has several cofactor binding sites:

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 bindingi103Copper ABy similarity1
Metal bindingi104Copper ABy similarity1
Metal bindingi168Copper ABy similarity1
Metal bindingi238Copper BBy similarity1
Metal bindingi240Copper BBy similarity1
Metal bindingi310Copper BBy 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

Molecular functionLyase, Monooxygenase, Multifunctional enzyme, Oxidoreductase
LigandCopper, Metal-binding, Zinc

<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:
Peptidyl-glycine alpha-amidating monooxygenase A
Short name:
PAM-A
Alternative name(s):
Peptide C-terminal alpha-amidating enzyme I
Short name:
AE-I
Peptidyl-glycine alpha-amidating monooxygenase I
Including the following 2 domains:
Peptidylglycine alpha-hydroxylating monooxygenase A (EC:1.14.17.3)
Short name:
PHM-A
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase A (EC:4.3.2.5)
Alternative name(s):
Peptidylamidoglycolate lyase-A
Short name:
PAL-A
<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:pam-a
<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>OrganismiXenopus laevis (African clawed frog)
<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 identifieri8355 [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 › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Organism-specific databases

Xenopus laevis and tropicalis biology and genomics resource

More...Xenbasei		XB-GENE-950939, pam.L

<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 subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini37 – 825IntragranularSequence analysisAdd BLAST789
<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>Transmembranei826 – 846HelicalSequence analysisAdd BLAST21
Topological domaini847 – 935CytoplasmicSequence analysisAdd BLAST89

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

<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 – 36Sequence analysisAdd BLAST36
<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_000000636737 – 935Peptidyl-glycine alpha-amidating monooxygenase AAdd BLAST899

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi43 ↔ 182By similarity
Disulfide bondi77 ↔ 122By similarity
Disulfide bondi110 ↔ 127By similarity
Disulfide bondi223 ↔ 330By similarity
Disulfide bondi289 ↔ 311By similarity
Disulfide bondi526 ↔ 547By similarity
Disulfide bondi594 ↔ 605By 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>Glycosylationi658N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi739N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P08478

<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

Monomer.

By similarity

<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		P08478

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 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati463 – 504NHL 1Add BLAST42
Repeati512 – 557NHL 2Add BLAST46
Repeati565 – 609NHL 3Add BLAST45
Repeati662 – 705NHL 4Add BLAST44

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>Regioni1 – 390Peptidylglycine alpha-hydroxylating monooxygenaseBy similarityAdd BLAST390
Regioni391 – 712Peptidyl-alpha-hydroxyglycine alpha-amidating lyaseBy similarityAdd BLAST322

<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

In the C-terminal section; belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family.Curated
In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.120.10.30, 1 hit
2.60.120.230, 1 hit
2.60.120.310, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011042, 6-blade_b-propeller_TolB-like
IPR014784, Cu2_ascorb_mOase-like_C
IPR020611, Cu2_ascorb_mOase_CS-1
IPR014783, Cu2_ascorb_mOase_CS-2
IPR000323, Cu2_ascorb_mOase_N
IPR036939, Cu2_ascorb_mOase_N_sf
IPR024548, Cu2_monoox_C
IPR001258, NHL_repeat
IPR013017, NHL_repeat_subgr
IPR000720, PHM/PAL
IPR008977, PHM/PNGase_F_dom_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03712, Cu2_monoox_C, 1 hit
PF01082, Cu2_monooxygen, 1 hit
PF01436, NHL, 3 hits

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00790, PAMONOXGNASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49742, SSF49742, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00084, CU2_MONOOXYGENASE_1, 1 hit
PS00085, CU2_MONOOXYGENASE_2, 1 hit
PS51125, NHL, 4 hits

<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>Sequences (2)i

<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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P08478-1) [UniParc]FASTAAdd to basket
Also known as: AE-III

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MASLSSSFLV LFLLFQNSCY CFRSPLSVFK RYEESTRSLS NDCLGTTRPV 
        60         70         80         90        100
MSPGSSDYTL DIRMPGVTPT ESDTYLCKSY RLPVDDEAYV VDFRPHANMD 
       110        120        130        140        150
TAHHMLLFGC NIPSSTDDYW DCSAGTCMDK SSIMYAWAKN APPTKLPEGV 
       160        170        180        190        200
GFRVGGKSGS RYFVLQVHYG NVKAFQDKHK DCTGVTVRVT PEKQPQIAGI 
       210        220        230        240        250
YLSMSVDTVI PPGEEAVNSD IACLYNRPTI HPFAYRVHTH QLGQVVSGFR 
       260        270        280        290        300
VRHGKWSLIG RQSPQLPQAF YPVEHPVEIS PGDIIATRCL FTGKGRTSAT 
       310        320        330        340        350
YIGGTSNDEM CNLYIMYYMD AAHATSYMTC VQTGEPKLFQ NIPEIANVPI 
       360        370        380        390        400
PVSPDMMMMM GHGHHHTEAE PEKNTGLQQP KREEEEVLDQ DVHLEEDTDW 
       410        420        430        440        450
PGVNLKVGQV SGLALDPKNN LAIFHRGDHV WDENSFDRNF VYQQRGIGPI 
       460        470        480        490        500
QESTILVVDP SSSKVLKSTG KNLFFLPHGL TIDRDGNYWV TDVALHQVFK 
       510        520        530        540        550
LGAGKETPLL VLGRAFQPGS DRKHFCQPTD VAVDPITGNF FVADGYCNSR 
       560        570        580        590        600
IMQFSPNGMF IMQWGEETSS NVPRPGQFRI PHSLTMVPDQ GQLCVADREN 
       610        620        630        640        650
GRIQCFHAET GNFVKQIKHQ EFGREVFAVS YAPGGVLYAV NGKPYYGYSA 
       660        670        680        690        700
PVQGFMLNFS NGDILDTFIP ARKNFDMPHD IAAADDGTVY VGDAHANAVW 
       710        720        730        740        750
KFSPSKAEHR SVKKAGIEVE EITETEIFET HIRSRPKTNE SVEKQTQEKQ 
       760        770        780        790        800
QKQKNSAGVS TQEKQNVVQE INAGVPTQEK QNVVQESSAG VPTQEKQSVV 
       810        820        830        840        850
QESSAGVSTQ EKQSVVQESS AGVSFVLIIT LLIIPIAVLI AIAIFIRWRK 
       860        870        880        890        900
VRMYGGDIDH KSESSSVGIL GKLRGKGSGG LNLGTFFATH KGYSRKGFDR 
       910        920        930 
LSTEGSDQEK DDDDGSDSEE EYSAPPIPPA PVSSS
Length:935
Mass (Da):103,389
Last modified:March 23, 2010 - v3
<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:iE9C2BF75733AB83C
GO
Isoform 2 (identifier: P08478-2) [UniParc]FASTAAdd to basket
Also known as: AE-I

The sequence of this isoform differs from the canonical sequence as follows:
     391-400: DVHLEEDTDW → GLITLGDSAV
     401-935: Missing.

Show »
Length:400
Mass (Da):44,457
Checksum:iFE4E8FA261D1EA33
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 conflicti792P → S in CAA44615 (PubMed:1935950).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_020312391 – 400DVHLEEDTDW → GLITLGDSAV in isoform 2. 2 Publications10
Alternative sequenceiVSP_020313401 – 935Missing in isoform 2. 2 PublicationsAdd BLAST535

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
M18134 mRNA Translation: AAA49640.1
X62771 mRNA Translation: CAA44615.1
BC043987 mRNA Translation: AAH43987.1
BC170012 mRNA Translation: AAI70012.1
BC170016 mRNA Translation: AAI70016.1

Protein sequence database of the Protein Information Resource

More...PIRi		A29726, URXLA1
S17855

NCBI Reference Sequences

More...RefSeqi		NP_001079520.2, NM_001086051.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		379207

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		xla:379207

Keywords - Coding sequence diversityi

Alternative splicing

<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
M18134 mRNA Translation: AAA49640.1
X62771 mRNA Translation: CAA44615.1
BC043987 mRNA Translation: AAH43987.1
BC170012 mRNA Translation: AAI70012.1
BC170016 mRNA Translation: AAI70016.1
PIRiA29726, URXLA1
S17855
RefSeqiNP_001079520.2, NM_001086051.2

3D structure databases

SMRiP08478
ModBaseiSearch...

Proteomic databases

PRIDEiP08478

Genome annotation databases

GeneIDi379207
KEGGixla:379207

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		379207
XenbaseiXB-GENE-950939, pam.L

Family and domain databases

Gene3Di2.120.10.30, 1 hit
2.60.120.230, 1 hit
2.60.120.310, 1 hit
InterProiView protein in InterPro
IPR011042, 6-blade_b-propeller_TolB-like
IPR014784, Cu2_ascorb_mOase-like_C
IPR020611, Cu2_ascorb_mOase_CS-1
IPR014783, Cu2_ascorb_mOase_CS-2
IPR000323, Cu2_ascorb_mOase_N
IPR036939, Cu2_ascorb_mOase_N_sf
IPR024548, Cu2_monoox_C
IPR001258, NHL_repeat
IPR013017, NHL_repeat_subgr
IPR000720, PHM/PAL
IPR008977, PHM/PNGase_F_dom_sf
PfamiView protein in Pfam
PF03712, Cu2_monoox_C, 1 hit
PF01082, Cu2_monooxygen, 1 hit
PF01436, NHL, 3 hits
PRINTSiPR00790, PAMONOXGNASE
SUPFAMiSSF49742, SSF49742, 2 hits
PROSITEiView protein in PROSITE
PS00084, CU2_MONOOXYGENASE_1, 1 hit
PS00085, CU2_MONOOXYGENASE_2, 1 hit
PS51125, NHL, 4 hits

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 nameiAMDA_XENLA
<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: P08478
Secondary accession number(s): B7ZR22, Q5D0B6, Q91697
<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: August 1, 1988
Last sequence update: March 23, 2010
Last modified: December 2, 2020
This is version 127 of the entry and version 3 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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