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Entry version 161 (07 Apr 2021)
Sequence version 2 (01 Nov 1997)
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Protein

Antigen peptide transporter 1

Gene

Tap1

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

ABC transporter associated with antigen processing (PubMed:17018292). In complex with TAP2 mediates unidirectional translocation of peptide antigens from cytosol to endoplasmic reticulum (ER) for loading onto MHC class I (MHCI) molecules (By similarity). Uses the chemical energy of ATP to export peptides against the concentration gradient (By similarity). During the transport cycle alternates between 'inward-facing' state with peptide binding site facing the cytosol to 'outward-facing' state with peptide binding site facing the ER lumen. Peptide antigen binding to ATP-loaded TAP1-TAP2 induces a switch to hydrolysis-competent 'outward-facing' conformation ready for peptide loading onto nascent MHCI molecules. Subsequently ATP hydrolysis resets the transporter to the 'inward facing' state for a new cycle (By similarity). As a component of the peptide loading complex (PLC), acts as a molecular scaffold essential for peptide-MHCI assembly and antigen presentation (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

Mg2+2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei17Inter-subunit salt bridge with TAPBPBy similarity1
<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 bindingi522MagnesiumCombined sources2 Publications1
<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 sitei678ATPCombined sources2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi515 – 523ATPPROSITE-ProRule annotationCombined sources1 Publication9
Nucleotide bindingi618 – 624ATPCombined sources2 Publications7

<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 functionTranslocase
Biological processAdaptive immunity, Immunity, Peptide transport, Protein transport, Transport
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1236974, ER-Phagosome pathway
R-RNO-983170, Antigen Presentation: Folding, assembly and peptide loading of class I MHC

<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:
Antigen peptide transporter 1 (EC:7.4.2.-1 Publication)
Short name:
APT1
Alternative name(s):
ATP-binding cassette sub-family B member 2
Peptide transporter TAP1
<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:Tap1
Synonyms:Abcb2, Mtp1
<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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
3817, Tap1

<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 domaini1 – 8CytoplasmicSequence analysis8
<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>Transmembranei9 – 29Helical; Name=1PROSITE-ProRule annotationAdd BLAST21
Topological domaini30 – 38LumenalSequence analysis9
Transmembranei39 – 60Helical; Name=2PROSITE-ProRule annotationAdd BLAST22
Topological domaini61 – 67CytoplasmicSequence analysis7
Transmembranei68 – 88Helical; Name=3PROSITE-ProRule annotationAdd BLAST21
Topological domaini89 – 110LumenalSequence analysisAdd BLAST22
Transmembranei111 – 131Helical; Name=4PROSITE-ProRule annotationAdd BLAST21
Topological domaini132 – 163CytoplasmicSequence analysisAdd BLAST32
Transmembranei164 – 184Helical; Name=5PROSITE-ProRule annotationAdd BLAST21
Topological domaini185 – 204LumenalSequence analysisAdd BLAST20
Transmembranei205 – 225Helical; Name=6PROSITE-ProRule annotationAdd BLAST21
Topological domaini226 – 275CytoplasmicSequence analysisAdd BLAST50
Transmembranei276 – 296Helical; Name=7PROSITE-ProRule annotationAdd BLAST21
Topological domaini297 – 305LumenalSequence analysis9
Transmembranei306 – 326Helical; Name=8PROSITE-ProRule annotationAdd BLAST21
Topological domaini327 – 395CytoplasmicSequence analysisAdd BLAST69
Transmembranei396 – 416Helical; Name=9PROSITE-ProRule annotationAdd BLAST21
Topological domaini417 – 420LumenalSequence analysis4
Transmembranei421 – 441Helical; Name=10PROSITE-ProRule annotationAdd BLAST21
Topological domaini442 – 725CytoplasmicSequence analysisAdd BLAST284

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<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>Mutagenesisi621 – 622SG → AV: Complete loss of ATPase activity; when associated with N-645. Impairs peptide loading onto MHCI. 1 Publication2
Mutagenesisi645D → E: Increases ATPase activity by 8-fold; when associated with H-678. 1 Publication1
Mutagenesisi645D → N: Complete loss of ATPase activity; when associated with A-621 and V-622. 1 Publication1
Mutagenesisi645D → Q: Impairs ATPase activity; when associated with H-678. 1 Publication1
Mutagenesisi651D → A or N: Decreases ATP-driven nucleotide binding domain (NBD) dimerization. 1 Publication1
Mutagenesisi678Q → H: Increases ATPase activity by 8-fold; when associated with E-645. Impairs ATPase activity; when associated with Q-645. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section 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_00000933281 – 725Antigen peptide transporter 1Add BLAST725

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P36370

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

More...
PaxDbi
P36370

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P36370

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P36370

<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

Heterodimer of TAP1 and TAP2 (TAP1-TAP2). A component of the peptide loading complex (PLC), interacts via TAPBP with MHCI heterodimer; this interaction mediates peptide-MHCI assembly.

Interacts with PSMB5 and PSMB8.

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P36370, 3 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000000529

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1725
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P36370

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P36370

<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 <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini164 – 447ABC transmembrane type-1PROSITE-ProRule annotationAdd BLAST284
Domaini480 – 719ABC transporterPROSITE-ProRule annotationAdd BLAST240

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>Regioni352 – 397Part of the peptide-binding siteBy similarityAdd BLAST46
Regioni430 – 464Part of the peptide-binding siteBy similarityAdd BLAST35

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

The peptide-binding site is shared between the cytoplasmic loops of TAP1 and TAP2.By similarity
The nucleotide-binding domain (NBD) mediates ATP hydrolysis coupled to peptide translocation. Two ATP molecules are accommodated at distinct nucleotide binding sites (NBS) at TAP1-TAP2 dimer interface. Each NBS is formed by Walker A (GxxGxGKST) and Q-loop motifs from NBD of one subunit, while the NBD from the second subunit completes the active site by contributing the C loop motif (LSGGQ). Each ATP molecule is coordinated via the beta- and gamma-phosphates to a Mg2+ ion, which is necessary for ATP hydrolysis.1 Publication

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0058, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P36370

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P36370

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.1560.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003593, AAA+_ATPase
IPR011527, ABC1_TM_dom
IPR036640, ABC1_TM_sf
IPR013305, ABC_Tap-like
IPR003439, ABC_transporter-like
IPR017871, ABC_transporter_CS
IPR027417, P-loop_NTPase
IPR013306, Tap1/ABCB2
IPR039421, Type_1_exporter

The PANTHER Classification System

More...
PANTHERi
PTHR24221, PTHR24221, 1 hit
PTHR24221:SF249, PTHR24221:SF249, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00664, ABC_membrane, 1 hit
PF00005, ABC_tran, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00382, AAA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540, SSF52540, 1 hit
SSF90123, SSF90123, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00958, 3a01208, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50929, ABC_TM1F, 1 hit
PS00211, ABC_TRANSPORTER_1, 1 hit
PS50893, ABC_TRANSPORTER_2, 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>Sequence (1+)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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P36370-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAAHAWPTAA LLLLLVDWLL LRPVLPGIFS LLVPEVPLLR VWAVGLSRWA
60 70 80 90 100
ILGLGVRGVL GVTAGARGWL AALQPLVAAL GLALPGLASF RKLSAWGALR
110 120 130 140 150
EGDNAGLLHW NSRLDAFVLS YVAALPAAAL WHKLGGFWAP SGHKGAGDML
160 170 180 190 200
CRMLGFLDSK KGRLHLVLVL LILSCLGEMA IPFFTGRITD WILQDKTAPS
210 220 230 240 250
FARNMWLMCI LTIASTVLEF AGDGIYNITM GHMHSRVHGE VFRAVLHQET
260 270 280 290 300
GFFLKNPTGS ITSRVTEDTS NVCESISDKL NLFLWYLGRG LCLLAFMIWG
310 320 330 340 350
SFYLTVVTLL SLPLLFLLPR RLGKVYQSLA VKVQESLAKS TQVALEALSA
360 370 380 390 400
MPTVRSFANE EGEAQKFRQK LEEMKPLNKK EALAYVTEVW TMSVSGMLLK
410 420 430 440 450
VGILYLGGQL VVRGAVSSGN LVSFVLYQLQ FTRAVEVLLS IYPSMQKSVG
460 470 480 490 500
ASEKIFEYLD RTPCSPLSGS LAPLNMKGLV KFQDVSFAYP NHPNVQVLQG
510 520 530 540 550
LTFTLYPGKV TALVGPNGSG KSTVAALLQN LYQPTGGKVL LDGEPLVQYD
560 570 580 590 600
HHYLHTQVAA VGQEPLLFGR SFRENIAYGL TRTPTMEEIT AVAMESGAHD
610 620 630 640 650
FISGFPQGYD TEVGETGNQL SGGQRQAVAL ARALIRKPRL LILDDATSAL
660 670 680 690 700
DAGNQLRVQR LLYESPEWAS RTVLLITQQL SLAERAHHIL FLKEGSVCEQ
710 720
GTHLQLMERG GCYRSMVEAL AAPSD
Length:725
Mass (Da):79,150
Last modified:November 1, 1997 - 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:i3FA7215D0AC22EE0
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
P97949P97949_RAT
Antigen peptide transporter 1
Tap1 Arrb2-ps, Hla-dma, Hla-dmb, Psmb9, RT1-Ba
725Annotation score:

Annotation score:4 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>
A0A0G2JY71A0A0G2JY71_RAT
Antigen peptide transporter 1
Tap1
82Annotation score:

Annotation score:1 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>

<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 CAA40742 differs from that shown. Reason: Erroneous initiation.Curated

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
X57523 mRNA Translation: CAA40742.1 Different initiation.
Y10231 mRNA Translation: CAA71280.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S13426

Genome annotation databases

UCSC genome browser

More...
UCSCi
RGD:3817, 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
X57523 mRNA Translation: CAA40742.1 Different initiation.
Y10231 mRNA Translation: CAA71280.1
PIRiS13426

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IXEX-ray2.00A/D465-725[»]
2IXFX-ray2.00A/B/C/D465-725[»]
2IXGX-ray2.70A465-725[»]
4K8OX-ray2.65A465-725[»]
SMRiP36370
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP36370, 3 interactors
STRINGi10116.ENSRNOP00000000529

PTM databases

iPTMnetiP36370
PhosphoSitePlusiP36370

Proteomic databases

jPOSTiP36370
PaxDbiP36370

Genome annotation databases

UCSCiRGD:3817, rat

Organism-specific databases

RGDi3817, Tap1

Phylogenomic databases

eggNOGiKOG0058, Eukaryota
InParanoidiP36370
PhylomeDBiP36370

Enzyme and pathway databases

ReactomeiR-RNO-1236974, ER-Phagosome pathway
R-RNO-983170, Antigen Presentation: Folding, assembly and peptide loading of class I MHC

Miscellaneous databases

EvolutionaryTraceiP36370

Protein Ontology

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PROi
PR:P36370

Family and domain databases

Gene3Di1.20.1560.10, 1 hit
InterProiView protein in InterPro
IPR003593, AAA+_ATPase
IPR011527, ABC1_TM_dom
IPR036640, ABC1_TM_sf
IPR013305, ABC_Tap-like
IPR003439, ABC_transporter-like
IPR017871, ABC_transporter_CS
IPR027417, P-loop_NTPase
IPR013306, Tap1/ABCB2
IPR039421, Type_1_exporter
PANTHERiPTHR24221, PTHR24221, 1 hit
PTHR24221:SF249, PTHR24221:SF249, 1 hit
PfamiView protein in Pfam
PF00664, ABC_membrane, 1 hit
PF00005, ABC_tran, 1 hit
SMARTiView protein in SMART
SM00382, AAA, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
SSF90123, SSF90123, 1 hit
TIGRFAMsiTIGR00958, 3a01208, 1 hit
PROSITEiView protein in PROSITE
PS50929, ABC_TM1F, 1 hit
PS00211, ABC_TRANSPORTER_1, 1 hit
PS50893, ABC_TRANSPORTER_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiTAP1_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: P36370
<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: June 1, 1994
Last sequence update: November 1, 1997
Last modified: April 7, 2021
This is version 161 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

3D-structure, Reference proteome

Documents

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