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Entry version 197 (29 Sep 2021)
Sequence version 1 (01 Feb 1995)
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Protein

Endoplasmic reticulum transmembrane helix translocase

Gene

SPF1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's 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 (PubMed:22918956, PubMed:32973005).

Acts as a dislocase that mediates the ATP-dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane (PubMed:32973005).

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 (PubMed:32973005).

2 Publications

Miscellaneous

Present with 1870 molecules/cell in log phase SD medium.1 Publication

Caution

Was initially thought to mediate ion transport such as calcium or manganese (PubMed:12058017, PubMed:24392018). However, different publications have shown that it does not act as an ion transporter (PubMed:22745129, PubMed:32353073, PubMed:32973005). Specifically binds moderately hydrophobic transmembrane with short hydrophilic lumenal domains that misinsert into the endoplasmic reticulum (PubMed:32973005).5 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+2 Publications

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

The ATPase activity is stimulated by phosphatidylinositol 4-phosphate (PI4P).1 Publication

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 sitei4874-aspartylphosphate intermediate4 Publications1
<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 bindingi487Magnesium1 Publication1
Metal bindingi489Magnesium1 Publication1
<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 sitei582ATPBy similarity1
Binding sitei634ATP1 Publication1
Binding sitei699ATP1 Publication1
Metal bindingi816Magnesium1 Publication1

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 bindingi487 – 489ATP1 Publication3
Nucleotide bindingi816 – 820ATP1 Publication5

<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 processProtein transport, Transport
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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

Protein family/group databases

Transport Classification Database

More...
TCDBi
3.A.3.10.3, the p-type atpase (p-atpase) superfamily

<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.-1 Publication)
Alternative name(s):
Complexed with DOR1 protein 11 Publication
Endoplasmic reticulum P5A-ATPase1 Publication
Sensitivity to the P.farinosa killer toxin protein 11 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:SPF11 PublicationImported
Synonyms:COD11 Publication
Ordered Locus Names:YEL031W
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's 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 identifieri559292 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<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
  • UP000002311 <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 V

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000000757, SPF1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YEL031W

<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 – 27Cytoplasmic1 PublicationAdd BLAST27
<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>Transmembranei28 – 43Helical; Name=TMa1 PublicationAdd BLAST16
Topological domaini44 – 56Lumenal1 PublicationAdd BLAST13
Transmembranei57 – 76Helical; Name=TMb1 PublicationAdd BLAST20
Topological domaini77 – 188Cytoplasmic1 PublicationAdd BLAST112
Transmembranei189 – 216Helical; Name=TM11 PublicationAdd BLAST28
Topological domaini217Lumenal1 Publication1
Transmembranei218 – 246Helical; Name=TM21 PublicationAdd BLAST29
Topological domaini247 – 395Cytoplasmic1 PublicationAdd BLAST149
Transmembranei396 – 425Helical; Name=TM31 PublicationAdd BLAST30
Topological domaini426 – 427Lumenal1 Publication2
Transmembranei428 – 442Helical; Name=TM4a1 PublicationAdd BLAST15
Transmembranei446 – 464Helical; Name=TM4b1 PublicationAdd BLAST19
Topological domaini465 – 971Cytoplasmic1 PublicationAdd BLAST507
Transmembranei972 – 1011Helical; Name=TM51 PublicationAdd BLAST40
Topological domaini1012 – 1017Lumenal1 Publication6
Transmembranei1018 – 1035Helical; Name=TM61 PublicationAdd BLAST18
Topological domaini1036 – 1055Cytoplasmic1 PublicationAdd BLAST20
Transmembranei1056 – 1084Helical; Name=TM71 PublicationAdd BLAST29
Topological domaini1085 – 1099Lumenal1 PublicationAdd BLAST15
Transmembranei1100 – 1121Helical; Name=TM81 PublicationAdd BLAST22
Topological domaini1122 – 1133Cytoplasmic1 PublicationAdd BLAST12
Transmembranei1134 – 1151Helical; Name=TM91 PublicationAdd BLAST18
Topological domaini1152 – 1168Lumenal1 PublicationAdd BLAST17
Transmembranei1169 – 1197Helical; Name=TM101 PublicationAdd BLAST29
Topological domaini1198 – 1215Cytoplasmic1 PublicationAdd BLAST18

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

Impaired mitochondrial transmembrane tail-anchored protein localization, characterized by mitochondrial transmembrane tail-anchored protein accumulation at the endoplasmic reticulum (PubMed:22918956). In addition, a wide spectrum of phenotypes is observed, including induction of the endoplasmic reticulum unfolded protein response, defects in lipid and sterol homeostasis, and dysregulated protein N-glycosylation, topogenesis and turnover (PubMed:12058017, PubMed:22918956, PubMed:24392018).3 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>Mutagenesisi487D → N: Loss of ATPase activity. 4 Publications1

<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_00000463491 – 1215Endoplasmic reticulum transmembrane helix translocaseAdd BLAST1215

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 residuei324PhosphoserineCombined sources1
Modified residuei936PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P39986

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

More...
PaxDbi
P39986

PRoteomics IDEntifications database

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PRIDEi
P39986

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P39986

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P39986

<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
36698, 483 interactors

Database of interacting proteins

More...
DIPi
DIP-6637N

Protein interaction database and analysis system

More...
IntActi
P39986, 3 interactors

STRING: functional protein association networks

More...
STRINGi
4932.YEL031W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P39986, protein

<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

11215
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
P39986

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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>Regioni156 – 185A-domain; part 11 PublicationAdd BLAST30
Regioni250 – 390A-domain; part 21 PublicationAdd BLAST141
Regioni466 – 495P-domain; part 11 PublicationAdd BLAST30
Regioni497 – 674N-domain1 PublicationAdd BLAST178
Regioni677 – 837P-domain; part 21 PublicationAdd BLAST161
Regioni838 – 953Arm-like1 PublicationAdd BLAST116
Regioni954 – 969P-domain; part 31 PublicationAdd 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 (PubMed:32973005). The translocase alternates between two conformations: inward-open (E1) and outward-open (E2) states (PubMed:32973005). 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) (PubMed:32973005). 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 (PubMed:32973005).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
KOG0209, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00550000075064

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_001828_4_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P39986

Identification of Orthologs from Complete Genome Data

More...
OMAi
SCIVNEA

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.

P39986-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTKKSFVSSP IVRDSTLLVP KSLIAKPYVL PFFPLYATFA QLYFQQYDRY
60 70 80 90 100
IKGPEWTFVY LGTLVSLNIL VMLMPAWNVK IKAKFNYSTT KNVNEATHIL
110 120 130 140 150
IYTTPNNGSD GIVEIQRVTE AGSLQTFFQF QKKRFLWHEN EQVFSSPKFL
160 170 180 190 200
VDESPKIGDF QKCKGHSGDL THLKRLYGEN SFDIPIPTFM ELFKEHAVAP
210 220 230 240 250
LFVFQVFCVA LWLLDEFWYY SLFNLFMIIS MEAAAVFQRL TALKEFRTMG
260 270 280 290 300
IKPYTINVFR NKKWVALQTN ELLPMDLVSI TRTAEESAIP CDLILLDGSA
310 320 330 340 350
IVNEAMLSGE STPLLKESIK LRPSEDNLQL DGVDKIAVLH GGTKALQVTP
360 370 380 390 400
PEHKSDIPPP PDGGALAIVT KTGFETSQGS LVRVMIYSAE RVSVDNKEAL
410 420 430 440 450
MFILFLLIFA VIASWYVWVE GTKMGRIQSK LILDCILIIT SVVPPELPME
460 470 480 490 500
LTMAVNSSLA ALAKFYVYCT EPFRIPFAGR IDVCCFDKTG TLTGEDLVFE
510 520 530 540 550
GLAGISADSE NIRHLYSAAE APESTILVIG AAHALVKLED GDIVGDPMEK
560 570 580 590 600
ATLKAVGWAV ERKNSNYREG TGKLDIIRRF QFSSALKRSA SIASHNDALF
610 620 630 640 650
AAVKGAPETI RERLSDIPKN YDEIYKSFTR SGSRVLALAS KSLPKMSQSK
660 670 680 690 700
IDDLNRDDVE SELTFNGFLI FHCPLKDDAI ETIKMLNESS HRSIMITGDN
710 720 730 740 750
PLTAVHVAKE VGIVFGETLI LDRAGKSDDN QLLFRDVEET VSIPFDPSKD
760 770 780 790 800
TFDHSKLFDR YDIAVTGYAL NALEGHSQLR DLLRHTWVYA RVSPSQKEFL
810 820 830 840 850
LNTLKDMGYQ TLMCGDGTND VGALKQAHVG IALLNGTEEG LKKLGEQRRL
860 870 880 890 900
EGMKMMYIKQ TEFMARWNQP QPPVPEPIAH LFPPGPKNPH YLKALESKGT
910 920 930 940 950
VITPEIRKAV EEANSKPVEV IKPNGLSEKK PADLASLLLN SAGDAQGDEA
960 970 980 990 1000
PALKLGDASC AAPFTSKLAN VSAVTNIIRQ GRCALVNTIQ MYKILALNCL
1010 1020 1030 1040 1050
ISAYSLSIIY MAGVKFGDGQ ATVSGLLLSV CFLSISRGKP LEKLSKQRPQ
1060 1070 1080 1090 1100
SGIFNVYIMG SILSQFAVHI ATLVYITTEI YKLEPREPQV DLEKEFAPSL
1110 1120 1130 1140 1150
LNTGIFIIQL VQQVSTFAVN YQGEPFRENI RSNKGMYYGL LGVTGLALAS
1160 1170 1180 1190 1200
ATEFLPELNE AMKFVPMTDD FKIKLTLTLL LDFFGSWGVE HFFKFFFMDD
1210
KPSDISVQQV KIASK
Length:1,215
Mass (Da):135,269
Last modified:February 1, 1995 - 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:i7A9960D34B91B5AE
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U18530 Genomic DNA Translation: AAB64508.1
BK006939 Genomic DNA Translation: DAA07622.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S50428

NCBI Reference Sequences

More...
RefSeqi
NP_010883.3, NM_001178846.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YEL031W_mRNA; YEL031W; YEL031W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
856681

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YEL031W

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Protein Spotlight

Wrong place - Issue 234 of March 2021

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18530 Genomic DNA Translation: AAB64508.1
BK006939 Genomic DNA Translation: DAA07622.1
PIRiS50428
RefSeqiNP_010883.3, NM_001178846.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6XMPelectron microscopy3.50A1-1215[»]
6XMQelectron microscopy3.70A1-1215[»]
6XMSelectron microscopy3.40A1-1215[»]
6XMTelectron microscopy3.30A1-1215[»]
6XMUelectron microscopy3.30A1-1215[»]
SMRiP39986
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi36698, 483 interactors
DIPiDIP-6637N
IntActiP39986, 3 interactors
STRINGi4932.YEL031W

Protein family/group databases

TCDBi3.A.3.10.3, the p-type atpase (p-atpase) superfamily

PTM databases

CarbonylDBiP39986
iPTMnetiP39986

Proteomic databases

MaxQBiP39986
PaxDbiP39986
PRIDEiP39986

Genome annotation databases

EnsemblFungiiYEL031W_mRNA; YEL031W; YEL031W
GeneIDi856681
KEGGisce:YEL031W

Organism-specific databases

SGDiS000000757, SPF1
VEuPathDBiFungiDB:YEL031W

Phylogenomic databases

eggNOGiKOG0209, Eukaryota
GeneTreeiENSGT00550000075064
HOGENOMiCLU_001828_4_1_1
InParanoidiP39986
OMAiSCIVNEA

Enzyme and pathway databases

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

Miscellaneous databases

Protein Ontology

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PROi
PR:P39986
RNActiP39986, protein

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

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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 nameiSPF1_YEAST
<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: P39986
Secondary accession number(s): D3DLL8
<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: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 29, 2021
This is version 197 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

3D-structure, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
  5. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
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