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UniProtKB - P10731 (AMD_BOVIN)

Entry version 167 (02 Jun 2021)
Sequence version 2 (01 Apr 1993)
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Protein

Peptidyl-glycine alpha-amidating monooxygenase

Gene

PAM

Organism
Bos taurus (Bovine)
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 the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides (PubMed:2059626).

Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme. The first step, catalyzed by peptidyl alpha-hydroxylating monoxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate (PubMed:2059626).

The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc-dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate (PubMed:2059626).

Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (By similarity).

By similarity1 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:

<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

PAM activity is inhibited by EDTA, phenylglyoxal and diethyl pyrocarbonate (By similarity). PAL activity is stimulated by cadmium and inhibited by mercury (By similarity).By similarity

<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>pH dependencei

Optimally active at acidic pHs.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 bindingi102Copper 1; via pros nitrogen; catalyticBy similarity1
Metal bindingi103Copper 1; via pros nitrogen; catalyticBy similarity1
Metal bindingi167Copper 1; via pros nitrogen; catalyticBy similarity1
Metal bindingi237Copper 2; via tele nitrogen; catalyticBy similarity1
Metal bindingi239Copper 2; via tele nitrogen; catalyticBy similarity1
Metal bindingi309Copper 2By similarity1
Metal bindingi517Calcium; via carbonyl oxygen; structuralBy similarity1
<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 sitei530SubstrateBy similarity1
Metal bindingi582Zinc; via tele nitrogen; catalyticBy similarity1
Metal bindingi584Calcium; via carbonyl oxygen; structuralBy similarity1
Binding sitei651SubstrateBy similarity1
Metal bindingi687Zinc; via tele nitrogen; catalyticBy similarity1
Binding sitei703SubstrateBy similarity1
Metal bindingi783Zinc; via tele nitrogen; catalyticBy similarity1
Metal bindingi784Calcium; structuralBy 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
LigandCalcium, Copper, Metal-binding, Vitamin C, 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 monooxygenaseBy similarity
Short name:
PAM1 Publication
Including the following 2 domains:
Peptidylglycine alpha-hydroxylating monooxygenaseBy similarity (EC:1.14.17.31 Publication)
Short name:
PHMBy similarity
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (EC:4.3.2.51 Publication)
Alternative name(s):
Peptidylamidoglycolate lyaseBy similarity
Short name:
PALBy similarity
<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
<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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
<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
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<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 domaini31 – 873IntragranularSequence analysisAdd BLAST843
<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>Transmembranei874 – 897HelicalSequence analysisAdd BLAST24
Topological domaini898 – 972CytoplasmicSequence analysisAdd BLAST75

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 – 20Sequence analysisAdd BLAST20
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000000635921 – 30Sequence analysis10
<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_000000636031 – 972Peptidyl-glycine alpha-amidating monooxygenaseAdd BLAST942

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 bondi42 ↔ 181By similarity
Disulfide bondi76 ↔ 121By similarity
Disulfide bondi109 ↔ 126By similarity
Disulfide bondi222 ↔ 329By similarity
Disulfide bondi288 ↔ 310By similarity
Disulfide bondi631 ↔ 652By similarity
Disulfide bondi699 ↔ 710By 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>Glycosylationi762N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei929PhosphoserineBy similarity1
Modified residuei942PhosphoserineBy similarity1
Modified residuei943PhosphothreonineBy similarity1
Modified residuei946Phosphoserine; by UHMK1By similarity1
Modified residuei957PhosphoserineBy similarity1

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

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

More...PaxDbi		P10731

PRoteomics IDEntifications database

More...PRIDEi		P10731

<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.

Interacts with RASSF9.

By similarity

Protein-protein interaction databases

Molecular INTeraction database

More...MINTi		P10731

STRING: functional protein association networks

More...STRINGi		9913.ENSBTAP00000016466

<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		P10731

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>Repeati498 – 541NHL 1Add BLAST44
Repeati567 – 608NHL 2Add BLAST42
Repeati617 – 662NHL 3Add BLAST46
Repeati670 – 714NHL 4Add BLAST45
Repeati766 – 809NHL 5Add 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 – 494Peptidylglycine alpha-hydroxylating monooxygenaseBy similarityAdd BLAST494
Regioni495 – 817Peptidyl-alpha-hydroxyglycine alpha-amidating lyaseBy similarityAdd BLAST323
Regioni925 – 942Interaction with RASSF9By similarityAdd BLAST18
Regioni937 – 972DisorderedSequence analysisAdd BLAST36

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3567, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P10731

Database of Orthologous Groups

More...OrthoDBi		476471at2759

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, 5 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>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.

P10731-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAGFRSLLVL LLVFPSGCVG FRSPLSVFKR FKETTRSFSN ECLGTTRPVI 
        60         70         80         90        100
PIDSSDFALD IRMPGVTPKQ SDTYFCMSVR LPMDEEAFVI DFKPRASMDT 
       110        120        130        140        150
VHHMLLFGCN MPASTGNYWF CDEGTCTDKA NILYAWARNA PPTRLPKGVG 
       160        170        180        190        200
FRVGGETGSK YFVLQVHYGD ISAFRDNHKD CSGVSLHLTR LPQPLIAGMY 
       210        220        230        240        250
LMMSVDTVIP PGGKVVNSDI SCHYKKYPMH VFAYRVHTHH LGKVVSGYRV 
       260        270        280        290        300
RNGQWTLIGR QSPQLPQAFY PVEHPVDVSF GDILAARCVF TGEGRTEVTH 
       310        320        330        340        350
IGGTSSDEMC NLYIMYYMEA KHAVSFMTCT QNVAPDIFRT IPPEANIPIP 
       360        370        380        390        400
VKSDMVMMHG HHKETENKDK TSLLQQPKRE EEGVLEQGDF YSLLSKLLGE 
       410        420        430        440        450
REDVVHVHKY NPTEKAESES DLVAEIANVV QKKDLGRSDT RESAEQERGN 
       460        470        480        490        500
AILVRDRIHK FHRLVSTLRP AESRVLSLQQ PLPGEGTWEP EHTGDFHVEE 
       510        520        530        540        550
ALDWPGVYLL PGQVSGVALD PQNNLVIFHR GDHVWDGNSF DSKFVYQQRG 
       560        570        580        590        600
LGPIEEDTIL VIDPNNAAVL QSSGKNLFYL PHGLSIDKDG NYWVTDVALH 
       610        620        630        640        650
QVFKLDPKSK EGPLLTLGRS MQPGSDQNHF CQPTDVAVDP DTGTIYVSDG 
       660        670        680        690        700
YCNSRLVQFS PSGKFITQWG EASLESSPKP GQFRVPHSLA LVPPLGQLCV 
       710        720        730        740        750
ADRENGRIQC FKTDTKEFVR EIKHPSFGRN VFAISYIPGL LFAVNGKPYF 
       760        770        780        790        800
EDQEPVQGFV MNFSSGEIID VFKPVRKHFD MPHDIAASED GTVYVGDAHT 
       810        820        830        840        850
NTVWKFTSTE KMEHRSVKKA GIEVQEIKES EAVVETKMEN KPASSELQKI 
       860        870        880        890        900
QEKQKLVKEP GSGVPAVLIT TLLVIPVVVL LAIALFIRWK KSRAFGDSER 
       910        920        930        940        950
KLEASSGRVL GRLRGKGGGG LNLGNFFASR KGYSRKGFDR LSTEGSDQEK 
       960        970 
DEDASESEEE YSAPPPAPAP SS
Length:972
Mass (Da):108,177
Last modified:April 1, 1993 - 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:iEBD41F83E341BAF1
GO

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
M18683 mRNA Translation: AAA30683.1

Protein sequence database of the Protein Information Resource

More...PIRi		A40063, URBOAP

NCBI Reference Sequences

More...RefSeqi		NP_776373.1, NM_173948.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		280890

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bta:280890

<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
M18683 mRNA Translation: AAA30683.1
PIRiA40063, URBOAP
RefSeqiNP_776373.1, NM_173948.2

3D structure databases

SMRiP10731
ModBaseiSearch...

Protein-protein interaction databases

MINTiP10731
STRINGi9913.ENSBTAP00000016466

Proteomic databases

PaxDbiP10731
PRIDEiP10731

Genome annotation databases

GeneIDi280890
KEGGibta:280890

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5066

Phylogenomic databases

eggNOGiKOG3567, Eukaryota
InParanoidiP10731
OrthoDBi476471at2759

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, 5 hits

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 nameiAMD_BOVIN
<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: P10731
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 1, 1993
Last modified: June 2, 2021
This is version 167 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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