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Entry version 91 (02 Dec 2020)
Sequence version 2 (05 Jul 2004)
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Protein

Pro-opiomelanocortin A

Gene

pomc-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

Stimulates the adrenal glands to release cortisol.
Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes.
Increases the pigmentation of skin by increasing melanin production in melanocytes.
Endogenous orexigenic opiate.
Endogenous opiate.

<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 functionEndorphin, Hormone

<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:
Pro-opiomelanocortin A
Short name:
POMC-A
Alternative name(s):
Corticotropin-lipotropin A
Cleaved into the following 10 chains:
Alternative name(s):
Gamma-MSH
Alternative name(s):
Adrenocorticotropic hormone
Short name:
ACTH
Alternative name(s):
Melanotropin alpha
Alternative name(s):
Beta-LPH
Alternative name(s):
Gamma-LPH
Alternative name(s):
Melanotropin beta
<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:pomc-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

Xenopus laevis and tropicalis biology and genomics resource

More...
Xenbasei
XB-GENE-483707, pomc.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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<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 – 25By similarityAdd BLAST25
<p>This subsection of the 'PTM / Processing' section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_000002515026 – 101NPPBy similarityAdd BLAST76
PeptideiPRO_000002515176 – 86Melanotropin gammaBy similarityAdd BLAST11
<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_0000025152104 – 137Add BLAST34
PeptideiPRO_0000025153140 – 178CorticotropinBy similarityAdd BLAST39
PeptideiPRO_0000025154140 – 152Melanocyte-stimulating hormone alphaAdd BLAST13
PeptideiPRO_0000025155158 – 178Corticotropin-like intermediary peptideBy similarityAdd BLAST21
PeptideiPRO_0000025156181 – 259Lipotropin betaBy similarityAdd BLAST79
PeptideiPRO_0000025157181 – 226Lipotropin gammaBy similarityAdd BLAST46
PeptideiPRO_0000025158210 – 226Melanocyte-stimulating hormone betaAdd BLAST17
PeptideiPRO_0000025159229 – 259Beta-endorphinBy similarityAdd BLAST31
PeptideiPRO_0000025160229 – 233Met-enkephalinBy similarity5

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei26Pyrrolidone carboxylic acidBy similarity1
Modified residuei86Phenylalanine amideBy similarity1
<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>Glycosylationi90N-linked (GlcNAc...) asparagine1
Modified residuei152Valine amideBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Specific enzymatic cleavages at paired basic residues yield the different active peptides.

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Glycoprotein, Pyrrolidone carboxylic acid

<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

GO - Molecular functioni

<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 POMC family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

Database of Orthologous Groups

More...
OrthoDBi
1168862at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013531, Mcrtin_ACTH_cent
IPR013593, Melanocortin_N
IPR013532, Opioid_neuropept
IPR001941, PMOC

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00976, ACTH_domain, 3 hits
PF08384, NPP, 1 hit
PF08035, Op_neuropeptide, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00383, MELANOCORTIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01363, ACTH_domain, 3 hits
SM01364, NPP, 1 hit
SM01365, Op_neuropeptide, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P06298-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFRPLWGCFL AILGICIFHI GEVQSQCWES SRCADLSSED GVLECIKACK
60 70 80 90 100
TDLSAESPVF PGNGHLQPLS ESIRKYVMTH FRWNKFGRRN STGNDGSNTG
110 120 130 140 150
YKREDISSYP VFSLFPLSDQ NAPGDNMEEE PLDRQENKRA YSMEHFRWGK
160 170 180 190 200
PVGRKRRPIK VYPNGVEEES AESYPMELRR ELSLELDYPE IDLDEDIEDN
210 220 230 240 250
EVESALTKKN GNYRMHHFRW GSPPKDKRYG GFMTPERSQT PLMTLFKNAI

IKNSHKKGQ
Length:259
Mass (Da):29,879
Last modified:July 5, 2004 - 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:i4D3804ABEE3EED20
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 CAA27465 differs from that shown. Reason: Erroneous initiation.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 conflicti57S → L in AAA49932 (PubMed:3840481).Curated1
Sequence conflicti203E → K (PubMed:3754961).Curated1
Sequence conflicti203E → K (PubMed:3840481).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
X03843 mRNA Translation: CAA27460.1
X03843 mRNA Translation: CAA27461.1 Sequence problems.
X03843 mRNA Translation: CAA27462.1 Sequence problems.
X03843 mRNA Translation: CAA27463.1 Sequence problems.
X03843 mRNA Translation: CAA27464.1 Sequence problems.
X03843 mRNA Translation: CAA27465.1 Different initiation.
X59370 Genomic DNA Translation: CAA42013.2
BC054160 mRNA Translation: AAH54160.1
M11346 mRNA Translation: AAA49932.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A01460, CTXLPA

NCBI Reference Sequences

More...
RefSeqi
NP_001080838.1, NM_001087369.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
380532

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
xla:380532

<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
X03843 mRNA Translation: CAA27460.1
X03843 mRNA Translation: CAA27461.1 Sequence problems.
X03843 mRNA Translation: CAA27462.1 Sequence problems.
X03843 mRNA Translation: CAA27463.1 Sequence problems.
X03843 mRNA Translation: CAA27464.1 Sequence problems.
X03843 mRNA Translation: CAA27465.1 Different initiation.
X59370 Genomic DNA Translation: CAA42013.2
BC054160 mRNA Translation: AAH54160.1
M11346 mRNA Translation: AAA49932.1
PIRiA01460, CTXLPA
RefSeqiNP_001080838.1, NM_001087369.2

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Genome annotation databases

GeneIDi380532
KEGGixla:380532

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
380532
XenbaseiXB-GENE-483707, pomc.L

Phylogenomic databases

OrthoDBi1168862at2759

Family and domain databases

InterProiView protein in InterPro
IPR013531, Mcrtin_ACTH_cent
IPR013593, Melanocortin_N
IPR013532, Opioid_neuropept
IPR001941, PMOC
PfamiView protein in Pfam
PF00976, ACTH_domain, 3 hits
PF08384, NPP, 1 hit
PF08035, Op_neuropeptide, 1 hit
PRINTSiPR00383, MELANOCORTIN
SMARTiView protein in SMART
SM01363, ACTH_domain, 3 hits
SM01364, NPP, 1 hit
SM01365, Op_neuropeptide, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCOLI1_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: P06298
Secondary accession number(s): P87464, Q91824, Q9PU10
<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: January 1, 1988
Last sequence update: July 5, 2004
Last modified: December 2, 2020
This is version 91 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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