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Entry version 168 (29 Sep 2021)
Sequence version 1 (01 Jan 1998)
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Protein

Endoplasmic reticulum transmembrane helix translocase

Gene

cta4

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
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

Endoplasmic reticulum translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum. Acts as a dislocase that mediates the ATP-dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane. Specifically binds mitochondrial tail-anchored transmembrane proteins: has an atypically large substrate-binding pocket that recognizes and binds moderately hydrophobic transmembranes with short hydrophilic lumenal domains (By similarity).

Involved in controlling nuclear calcium ion levels. Required for cytokinesis and stabilizing microtubules (PubMed:12058018).

Required for assembly of the forespore membrane (PubMed:16394583).

Involved in calcium transport to the endoplasmic reticulum (PubMed:22132152).

By similarity3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei4854-aspartylphosphate intermediateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi485MagnesiumBy similarity1
Metal bindingi487MagnesiumBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei587ATPBy similarity1
Binding sitei644ATPBy similarity1
Binding sitei710ATPBy similarity1
Metal bindingi824MagnesiumBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi485 – 487ATPBy similarity3
Nucleotide bindingi824 – 828ATPBy similarity5

<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 processCell cycle, Cell division, Protein transport, Sporulation, Transport
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SPO-936837, Ion transport by P-type ATPases

<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_and_taxonomy_section">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:
Endoplasmic reticulum transmembrane helix translocaseCurated (EC:7.4.2.-By similarity)
Alternative name(s):
P-type ATPase cta42 Publications
P5A-type ATPase cta41 Publication
Sporulation protein essential for vegetative growth 41 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:cta43 Publications
Synonyms:sev41 Publication
ORF Names:SPAC2E11.07c, SPACUNK4.07cImported, SPAPYUK71.01Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri284812 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000002485 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome I

Organism-specific databases

Schizosaccharomyces pombe database

More...
PomBasei
SPACUNK4.07c, cta4

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:SPACUNK4.07c

<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_location_section">'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 – 23CytoplasmicSequence analysisAdd BLAST23
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei24 – 44HelicalSequence analysisAdd BLAST21
Topological domaini45 – 54LumenalSequence analysis10
Transmembranei55 – 75HelicalSequence analysisAdd BLAST21
Topological domaini76 – 191CytoplasmicSequence analysisAdd BLAST116
Transmembranei192 – 212HelicalSequence analysisAdd BLAST21
Topological domaini213 – 216LumenalSequence analysis4
Transmembranei217 – 237HelicalSequence analysisAdd BLAST21
Topological domaini238 – 397CytoplasmicSequence analysisAdd BLAST160
Transmembranei398 – 418HelicalSequence analysisAdd BLAST21
Topological domaini419 – 1057LumenalSequence analysisAdd BLAST639
Transmembranei1058 – 1078HelicalSequence analysisAdd BLAST21
Topological domaini1079 – 1100CytoplasmicSequence analysisAdd BLAST22
Transmembranei1101 – 1121HelicalSequence analysisAdd BLAST21
Topological domaini1122 – 1136LumenalSequence analysisAdd BLAST15
Transmembranei1137 – 1157HelicalSequence analysisAdd BLAST21
Topological domaini1158 – 1174CytoplasmicSequence analysisAdd BLAST17
Transmembranei1175 – 1195HelicalSequence analysisAdd BLAST21
Topological domaini1196 – 1211LumenalSequence analysisAdd BLAST16

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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Increased levels of intracellular calcium. Impaired ATP-dependent calcium transport in endoplasmic reticulum (ER) membranes, but up-regulated vacuolar calcium transport. Sensitive to ER stress inducers DTT and tunicamycin, which inhibit the protein disulfide bond formation and N-glycosylation, respectively, and is thus sensitive to accumulation of misfolded proteins in the ER. Stimulated calcineurin phosphatase activity (PubMed:22132152). Cells conjugate to form zygotes at a lower efficiency than wild-type and they do not sporulate (PubMed:16394583).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi615G → E in sev4-L5; growth defects at high and low temperatures, and sensitivity to high and extremely low concentrations of calcium ions. Conjugates to form zygotes at a lower efficiency than wild-type. Meiotic nuclear divisions proceed normally, but is not forming spores. Incomplete structure alteration of the spindle pole body, and hence forespore membrane formation is severely impaired. 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_00000463501 – 1211Endoplasmic reticulum transmembrane helix translocaseAdd BLAST1211

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O14072

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

More...
PaxDbi
O14072

PRoteomics IDEntifications database

More...
PRIDEi
O14072

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O14072

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
278845, 2 interactors

STRING: functional protein association networks

More...
STRINGi
4896.SPACUNK4.07c.1

<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
O14072

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

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>Regioni155 – 185A-domain; part 1By similarityAdd BLAST31
Regioni250 – 388A-domain; part 2By similarityAdd BLAST139
Regioni464 – 493P-domain; part 1By similarityAdd BLAST30
Regioni495 – 685N-domainBy similarityAdd BLAST191
Regioni688 – 845P-domain; part 2By similarityAdd BLAST158
Regioni846 – 955Arm-likeBy similarityAdd BLAST110
Regioni956 – 971P-domain; part 3By similarityAdd BLAST16

<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

Contains a large substrate-binding pocket that recognizes alpha-helical transmembranes, which alternately faces the endoplasmic reticulum lumen and cytosol, while remaining accessible to the lipid bilayer through a lateral opening. The translocase alternates between two conformations: inward-open (E1) and outward-open (E2) states. Undergoes a series of conformational changes with ATP-binding, phosphorylation of the Asp active site and subsequent dephosphorylation in a Post-Albers cycle (i.e., E1 -> E1-ATP -> E1P-ADP -> E1P -> E2P -> E2-Pi -> E1). A substrate transmembrane helix with a short, preferentially positively charged lumenal segment binds to the outward-open pocket and the E2P-to-E1 transition flips the transmembrane by a switch from the outward-open to inward-open conformation.By similarity

<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
KOG0209, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_001828_4_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O14072

Identification of Orthologs from Complete Genome Data

More...
OMAi
SCIVNEA

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O14072

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1110.10, 1 hit
3.40.50.1000, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR023299, ATPase_P-typ_cyto_dom_N
IPR018303, ATPase_P-typ_P_site
IPR023298, ATPase_P-typ_TM_dom_sf
IPR008250, ATPase_P-typ_transduc_dom_A_sf
IPR036412, HAD-like_sf
IPR023214, HAD_sf
IPR006544, P-type_TPase_V
IPR001757, P_typ_ATPase
IPR044492, P_typ_ATPase_HD_dom

Structure-Function Linkage Database

More...
SFLDi
SFLDF00027, p-type_atpase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56784, SSF56784, 1 hit
SSF81653, SSF81653, 1 hit
SSF81660, SSF81660, 1 hit
SSF81665, SSF81665, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01494, ATPase_P-type, 2 hits
TIGR01657, P-ATPase-V, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00154, ATPASE_E1_E2, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

O14072-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGSKALITSP DISSGQLYIK LPTFFHLYVW PFALFVYPYI GYVYQNKLYS
60 70 80 90 100
EEVRYLTYIA VGTIHALFWL AGEWNTKVYC LMTCRKTDKV EQATHILVTP
110 120 130 140 150
SKIGESSSVE PITKLVLPDS QTIQYSFSFQ RKRFIYEPEK GCFANITFPM
160 170 180 190 200
DEPSTIGTLK KSTGLTNIQS EIFLYRYGKN CFDIPIPTFG TLFKEHAVAP
210 220 230 240 250
FFVFQIFCCV LWCLDDYWYF SLFSMFMIIA LECSVVWQRQ RTLTEFRTMS
260 270 280 290 300
IKPYEIQVYR NKHWFPISTE DLLPNDVVSV LHNKEDSGLP CDLLLLSGSC
310 320 330 340 350
VVNEAMLSGE STPLVKESIE LRPEEAVIDV DELDKNAVLF GGTRVLQVTQ
360 370 380 390 400
SPFCKLKTPD NGVPAIVLRT GFETSQGSLV RTMVFSSEKV TANNRESLYF
410 420 430 440 450
ILFLLVFAIA ASGYVWHVGS KTERSRYKLM LDCVMIITSV VPSELPMELS
460 470 480 490 500
MAVNASLGAL SKYYIYCTEP FRIPLSGHLD ICCFDKTGTL TEEHMVVQGI
510 520 530 540 550
AGVNRKDPYS LEKLSDASND AILAIATAHT LVLLEQEGET PKVVGDPMEK
560 570 580 590 600
ATVENLGWSI EKKNFVSAPE GSVFYKGKVQ IIRNFQFSSA LKRQSSVSNV
610 620 630 640 650
RVSGGSFKTF VSVKGAPEVI ATMLREVPKD YEKIYKDYGR KGSRVLALGY
660 670 680 690 700
KYFKNYIPEN QVSDLSRESI ESDLVFAGFL IFTSPLKEDA RQTVQMLNNS
710 720 730 740 750
SHRCMMITGD NPLTAVYVAE QVGIVEKPTL VLDIKHENEK ILEWKSTDDT
760 770 780 790 800
INLPMNPHKS LEASLYEKYD LCITGRALSQ IINPDVIMSI FTHAWVYARV
810 820 830 840 850
SPSQKEFMIS TLKHNGYITL MCGDGTNDVG ALKQAHVGVA LLNASEEDML
860 870 880 890 900
EMQERARNQK LMGVYEKQIQ LAKRFNLPTP PVPPALCHAF PPGPNNPHRE
910 920 930 940 950
KTQEGLNKVL EDLETKKASD VQLTEAEKAA ERRANLANKM FDTLANASDD
960 970 980 990 1000
EAPKLKLGDA SVAAPFTSKL AVVSSITNIV RQGRCTLVAL VQMHKILALN
1010 1020 1030 1040 1050
CLITAYSLSV LHLDGIKFGD TQYTISGMLM SVCFYCVSRA RPLETLSKER
1060 1070 1080 1090 1100
PQAGIFNTYI IGSVLGQFAI HIVTLIYITR VVYLYEDPLE KVDLEETFKP
1110 1120 1130 1140 1150
SLLNTAIYLL QLIQQVSTFA INYQGRPFRE ALSENKGMYY GLLGIAFVAI
1160 1170 1180 1190 1200
AGVTEFSPEL NAKLQLVKMA YNFQIQLLAT MVVDYAACWI IEELMKKYFR
1210
DNKPKEIVLR N
Length:1,211
Mass (Da):136,261
Last modified:January 1, 1998 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6FEE4228CA5A57EC
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
CU329670 Genomic DNA Translation: CAA20137.1
AB027853 Genomic DNA Translation: BAA87157.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T41702

NCBI Reference Sequences

More...
RefSeqi
NP_593971.1, NM_001019398.2

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
SPACUNK4.07c.1; SPACUNK4.07c.1:pep; SPACUNK4.07c

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2542381

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
spo:SPACUNK4.07c

<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
CU329670 Genomic DNA Translation: CAA20137.1
AB027853 Genomic DNA Translation: BAA87157.1
PIRiT41702
RefSeqiNP_593971.1, NM_001019398.2

3D structure databases

SMRiO14072
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi278845, 2 interactors
STRINGi4896.SPACUNK4.07c.1

PTM databases

iPTMnetiO14072

Proteomic databases

MaxQBiO14072
PaxDbiO14072
PRIDEiO14072

Genome annotation databases

EnsemblFungiiSPACUNK4.07c.1; SPACUNK4.07c.1:pep; SPACUNK4.07c
GeneIDi2542381
KEGGispo:SPACUNK4.07c

Organism-specific databases

PomBaseiSPACUNK4.07c, cta4
VEuPathDBiFungiDB:SPACUNK4.07c

Phylogenomic databases

eggNOGiKOG0209, Eukaryota
HOGENOMiCLU_001828_4_1_1
InParanoidiO14072
OMAiSCIVNEA
PhylomeDBiO14072

Enzyme and pathway databases

ReactomeiR-SPO-936837, Ion transport by P-type ATPases

Miscellaneous databases

Protein Ontology

More...
PROi
PR:O14072

Family and domain databases

Gene3Di3.40.1110.10, 1 hit
3.40.50.1000, 1 hit
InterProiView protein in InterPro
IPR023299, ATPase_P-typ_cyto_dom_N
IPR018303, ATPase_P-typ_P_site
IPR023298, ATPase_P-typ_TM_dom_sf
IPR008250, ATPase_P-typ_transduc_dom_A_sf
IPR036412, HAD-like_sf
IPR023214, HAD_sf
IPR006544, P-type_TPase_V
IPR001757, P_typ_ATPase
IPR044492, P_typ_ATPase_HD_dom
SFLDiSFLDF00027, p-type_atpase, 1 hit
SUPFAMiSSF56784, SSF56784, 1 hit
SSF81653, SSF81653, 1 hit
SSF81660, SSF81660, 1 hit
SSF81665, SSF81665, 1 hit
TIGRFAMsiTIGR01494, ATPase_P-type, 2 hits
TIGR01657, P-ATPase-V, 1 hit
PROSITEiView protein in PROSITE
PS00154, ATPASE_E1_E2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
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 nameiATC4_SCHPO
<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: O14072
Secondary accession number(s): Q9USD0, Q9UT01
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: September 29, 2021
This is version 168 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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

Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families
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