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Entry version 80 (29 Sep 2021)
Sequence version 4 (09 Jul 2014)
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Protein

Phospholipid-transporting ATPase IB

Gene

ATP8A2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids (PubMed:19778899, PubMed:24706822, PubMed:31371510, PubMed:26592152).

Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. Reconstituted to liposomes, the ATP8A2:TMEM30A flippase complex predominantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE) (PubMed:19778899, PubMed:24706822, PubMed:31371510, PubMed:26592152).

Phospholipid translocation is not associated with a countertransport of an inorganic ion or other charged substrate from the cytoplasmic side toward the exoplasm in connection with the phosphorylation from ATP (PubMed:31371510).

ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth. Proposed to function in the generation and maintenance of phospholipid asymmetry in photoreceptor disk membranes and neuronal axon membranes. May be involved in vesicle trafficking in neuronal cells. Required for normal visual and auditory function; involved in photoreceptor and inner ear spiral ganglion cell survival.

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 <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

ATPase activity is stimulated by phosphatidylserine (PS) and minimally by phosphatidylethanolamine (PE). ATPase activity is inhibited by N-ethylmaleimide (NEM) and vanadate. Flippase activity is inhibited by NEM and 1,2-dioleoyl-sn-glycero-3-phospho-L-serine (DOPS).1 Publication

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>Sitei331Involved in the recognition of the lipid substrate on the exoplasmic side1 Publication1
Sitei336Involved in the release of the transported lipid into the cytosolic leaflet1 Publication1
<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 sitei3884-aspartylphosphate intermediateCurated1
<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 bindingi781MagnesiumBy similarity1
Metal bindingi785MagnesiumBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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 processLipid transport, Transport
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
7.6.2.1, 908

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000379

<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:
Phospholipid-transporting ATPase IBBy similarity (EC:7.6.2.15 Publications)
Alternative name(s):
ATPase class I type 8A member 2
P4-ATPase flippase complex alpha subunit ATP8A2
<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:ATP8A2By similarity
<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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
<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
  • UP000009136 <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: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_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 – 54CytoplasmicSequence analysisAdd BLAST54
<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>Transmembranei55 – 75HelicalSequence analysisAdd BLAST21
Topological domaini76 – 79Exoplasmic loopSequence analysis4
Transmembranei80 – 100HelicalSequence analysisAdd BLAST21
Topological domaini101 – 276CytoplasmicSequence analysisAdd BLAST176
Transmembranei277 – 297HelicalSequence analysisAdd BLAST21
Topological domaini298 – 324Exoplasmic loopSequence analysisAdd BLAST27
Transmembranei325 – 345HelicalSequence analysisAdd BLAST21
Topological domaini346 – 847CytoplasmicSequence analysisAdd BLAST502
Transmembranei848 – 868HelicalSequence analysisAdd BLAST21
Topological domaini869 – 870Exoplasmic loopSequence analysis2
Transmembranei871 – 891HelicalSequence analysisAdd BLAST21
Topological domaini892 – 919CytoplasmicSequence analysisAdd BLAST28
Transmembranei920 – 940HelicalSequence analysisAdd BLAST21
Topological domaini941 – 957Exoplasmic loopSequence analysisAdd BLAST17
Transmembranei958 – 978HelicalSequence analysisAdd BLAST21
Topological domaini979 – 988CytoplasmicSequence analysis10
Transmembranei989 – 1009HelicalSequence analysisAdd BLAST21
Topological domaini1010 – 1023Exoplasmic loopSequence analysisAdd BLAST14
Transmembranei1024 – 1044HelicalSequence analysisAdd BLAST21
Topological domaini1045 – 1148CytoplasmicSequence analysisAdd BLAST104

Keywords - Cellular componenti

Cell membrane, Cell projection, Endosome, Golgi apparatus, 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_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>Mutagenesisi60F → A: Enhances substrate affinities. Reduces considerably the Vmax. 1 Publication1
Mutagenesisi84L → A: Does not affect Vmax. Does not affect the apparent affinities for the substrates. Does not affect the phosphorylation rate. 1 Publication1
Mutagenesisi87I → A: Reduces approximately twofold the apparent affinity for PS. Does not affect the apparent affinity for PE. 1 Publication1
Mutagenesisi98E → A: Decreases TMEM30A glycosylation. Does not affect velocity of ATP hydrolyze of P4-ATPase flippase complex. Reduces markedly the flipping activity. 1 Publication1
Mutagenesisi168D → T: Reduces flipping of PS; reduces ATPAse activity by 3-fold. 1 Publication1
Mutagenesisi170E → Q: Slightly reverses flipping of PS, no ATPase activity. Abolishes the transient current establishes in the presence of ATP and the negatively charged lipid substrate phosphatidylserine. 2 Publications1
Mutagenesisi277I → A: Decreases TMEM30A glycosylation. Does not affect velocity of ATP hydrolyze of P4-ATPase flippase complex. 1 Publication1
Mutagenesisi326F → A: Does not affect affinity for PS. 1 Publication1
Mutagenesisi330Y → A: Does not affect affinity for PS. 1 Publication1
Mutagenesisi331N → A: Reduces dramaticaly the maximal velocity (Vmax) to 11% that of the wild type (WT) for PS and 9% for PE. Reduces approximately sixfold the apparent affinity for PS and PE. Reduces strongly ATPase activity. Loss of the PS flipping. Enhances approximately threefold the phosphorylation rate. Reduces highly the apparent affinity for vanadate. 1 Publication1
Mutagenesisi332N → A: Increases the apparent affinity for PS. Reduces approximately twofold the PS flipping rate relative to the WT. Does not affect the phosphorylation rate. 1 Publication1
Mutagenesisi333L → A: Does not affect affinity for PS. Decreases TMEM30A glycosylation. Does not affect velocity of ATP hydrolyze of P4-ATPase flippase complex. Reduces markedly the flipping activity. 2 Publications1
Mutagenesisi334I → A: Increases the apparent affinity for PS. 1 Publication1
Mutagenesisi336I → A: Deacreses flipping activity of 20%. Phosphatidylserine stimulates the ATPase activity to maximum levels of 59% of the wild type level. Phosphatityletanolamine (PE)-stimulated maximum activity is only 16% of wild type. The phosphorylation rates is fourfold reduced. Enhances approximately twofold the apparent affinity for PS. Increases significantly apparent vanadate affinity. Strongly interfers with the electrogenic lipid translocation. 1 Publication1
Mutagenesisi336I → E: Loss of flipping activity. PS- and PE-stimulated activity is very low. Does not affect the phosphorylation rates. Reduces substantialy the apparent affinity for PS. Reduces only slightly vanadate affinuity. 1 Publication1
Mutagenesisi336I → F: Loss of flipping activity. PS- and PE-stimulated activity is very low. The phosphorylation rates is fourfold reduced. Reduces substantialy the apparent affinity for PS. Does not affect vanadate affinity. 1 Publication1
Mutagenesisi336I → M: Loss of flipping activity. PS- and PE-stimulated activity is very low. The phosphorylation rates is twofold reduced. Reduces substantialy the apparent affinity for PS. Reduces markedly reduced vanadate affinity. 1 Publication1
Mutagenesisi336I → Q: Deacreses flipping activity of about 90%. PS- and PE-stimulated activity is very low. The phosphorylation rates is twofold reduced. Reduces markedly reduced vanadate affinity. 1 Publication1
Mutagenesisi336I → S: Deacreses flipping activity of 70%. Phosphatidylserine (PS) stimulates the ATPase activity to maximum levels of 43% of the wild type level. Phosphatityletanolamine (PE)-stimulated maximum activity is only 22% of wild type. The phosphorylation rates is fourfold reduced. Enhances approximately twofold the apparent affinity for PS. Increases significantly apparent vanadate affinity. 1 Publication1
Mutagenesisi337S → A: Reduces significantly affinity for PS. Reduces apparent affinity for PE. 1 Publication1
Mutagenesisi338L → A: Decreases TMEM30A glycosylation. Does not affect velocity of ATP hydrolyze of P4-ATPase flippase complex. 1 Publication1
Mutagenesisi339L → A: Reduces significantly affinity for PS. Does not affect apparent affinity for PE. 1 Publication1
Mutagenesisi339L → F: Does not affect velocity of ATP hydrolyze of P4-ATPase flippase complex. Reduces markedly the flipping activity. 1 Publication1
Mutagenesisi341T → A: Increases the apparent affinity for PS. 1 Publication1
Mutagenesisi343E → Q: Does not affect affinity for PS. 1 Publication1
Mutagenesisi346K → A: Does not affect affinity for PS. 1 Publication1
Mutagenesisi388D → N: Abolishes ATPAse activity. 1 Publication1
Mutagenesisi837K → A: No effect on flipping of PS and ATPase activity. 1 Publication1
Mutagenesisi845K → A: Greatly reduces flipping of PS; reduces affinity PS by 7- and 8-fold; for reduces ATPase activity by 30- and 70-fold; reduces PS-activated dephosphorylation of intermediate; reduces affinity to vanadate. 1 Publication1
Mutagenesisi845K → E: Greatly reduces flipping of PS; reduces affinity PS by 7- and 8-fold; for reduces ATPase activity by 30- and 70-fold. 1 Publication1
Mutagenesisi845K → R: Reduces flipping of PS; reduces affinity PS by 4-fold; reduces ATPase activity by 10-fold. 1 Publication1
Mutagenesisi846N → A: Reduces flipping of PS; reduces affinity PS by 3-fold; reduces ATPase activity by 10-fold. 1 Publication1
Mutagenesisi850Y → A: Decreases TMEM30A glycosylation. Does not affect velocity of ATP hydrolyze of P4-ATPase flippase complex. 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_00004298381 – 1148Phospholipid-transporting ATPase IBAdd BLAST1148

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 residuei5PhosphothreonineBy similarity1

Keywords - PTMi

Phosphoprotein

PTM databases

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
C7EXK4

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in retinal photoreceptor cells and testis.1 Publication

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit (PubMed:21454556, PubMed:26592152).

Interacts with TMEM30A to form a flippase complex (PubMed:21454556).

2 Publications

<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
C7EXK4

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>Regioni1102 – 1126DisorderedSequence analysisAdd BLAST25

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1103 – 1119Polar residuesSequence analysisAdd BLAST17

<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

Database of Orthologous Groups

More...
OrthoDBi
587717at2759

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
IPR006539, P-type_ATPase_IV
IPR032631, P-type_ATPase_N
IPR001757, P_typ_ATPase
IPR032630, P_typ_ATPase_c
IPR044492, P_typ_ATPase_HD_dom

The PANTHER Classification System

More...
PANTHERi
PTHR24092, PTHR24092, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16212, PhoLip_ATPase_C, 1 hit
PF16209, PhoLip_ATPase_N, 1 hit

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
TIGR01652, ATPase-Plipid, 1 hit
TIGR01494, ATPase_P-type, 2 hits

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.

C7EXK4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSRATSVGDQ LDVPARTIYL NQPHLNKFCD NQISTAKYSV VTFLPRFLYE
60 70 80 90 100
QIRRAANAFF LFIALLQQIP DVSPTGRYTT LVPLIIILTI AGIKEIVEDF
110 120 130 140 150
KRHKADNAVN KKKTIVLRNG MWQTIVWKEV AVGDIVKVVN GQYLPADVVL
160 170 180 190 200
LSSSEPQAMC YVETANLDGE TNLKIRQGLS HTADMQTREV LMKLSGTIEC
210 220 230 240 250
EGPNRHLYDF TGNLNLDGKS PVALGPDQIL LRGTQLRNTQ WGFGIVVYTG
260 270 280 290 300
HDTKLMQNST KAPLKRSNVE KVTNVQILVL FGILLVMALV SSVGALYWNG
310 320 330 340 350
SQGGKNWYIK KMDATSDNFG YNLLTFIILY NNLIPISLLV TLEVVKYTQA
360 370 380 390 400
LFINWDTDMY YLGNDTPAMA RTSNLNEELG QVKYLFSDKT GTLTCNIMNF
410 420 430 440 450
KKCSIAGVTY GHFPELTREP SSDDFSRIPP PPSDSCDFDD PRLLKNIEDH
460 470 480 490 500
HPTAPCIQEF LTLLAVCHTV VPERDGDSIV YQASSPDEAA LVKGARKLGF
510 520 530 540 550
VFTARTPYSV IIEAMGQEQT FGILNVLEFS SDRKRMSVIV RTPSGQLRLY
560 570 580 590 600
CKGADNVIFE RLSKDSKYME ETLCHLEYFA TEGLRTLCVA YADLSERDYE
610 620 630 640 650
EWLKVYQEAS TILKDRAQRL EECYEIIEKN LLLLGATAIE DRLQAGVPET
660 670 680 690 700
IATLLKAEIK IWVLTGDKQE TAINIGYSCR LVSQNMALIL LKEDSLDATR
710 720 730 740 750
AAITQHCADL GSLLGKENDA ALIIDGHTLK YALSFEVRRS FLDLALSCKA
760 770 780 790 800
VICCRVSPLQ KSEIVDVVKK RVKAITLAIG DGANDVGMIQ TAHVGVGISG
810 820 830 840 850
NEGMQATNNS DYAIAQFSYL EKLLLVHGAW SYNRVTKCIL YCFYKNVVLY
860 870 880 890 900
IIELWFAFVN GFSGQILFER WCIGLYNVIF TALPPFTLGI FERSCSQESM
910 920 930 940 950
LRFPQLYKIT QNAEGFNTKV FWGHCINALV HSLILFWFPM KALEHDTVLA
960 970 980 990 1000
NGHATDYLFV GNIVYTYVVV TVCLKAGLET TAWTKFSHLA VWGSMLIWLV
1010 1020 1030 1040 1050
FFGIYSTIWP TIPIAPDMKG QATMVLSSAH FWLGLFLVPT ACLIEDVAWR
1060 1070 1080 1090 1100
AAKHTCKKTL LEEVQELEMK SRVMGRAMLR DSNGKRMNER DRLLKRLSRK
1110 1120 1130 1140
TPPTLFRGSS LQQSMPHGYA FSQEEHGAVT QEEIVRAYDT TKQKSRKK
Length:1,148
Mass (Da):129,037
Last modified:July 9, 2014 - v4
<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:i9D0DC179F8BF62EF
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 ACT46164 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
GQ303567 mRNA Translation: ACT46164.3 Different initiation.

NCBI Reference Sequences

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RefSeqi
NP_001157274.3, NM_001163802.3

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
508723

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
bta:508723

<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
GQ303567 mRNA Translation: ACT46164.3 Different initiation.
RefSeqiNP_001157274.3, NM_001163802.3

3D structure databases

SMRiC7EXK4
ModBaseiSearch...

Chemistry databases

SwissLipidsiSLP:000000379

PTM databases

SwissPalmiC7EXK4

Genome annotation databases

GeneIDi508723
KEGGibta:508723

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
51761

Phylogenomic databases

OrthoDBi587717at2759

Enzyme and pathway databases

BRENDAi7.6.2.1, 908

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
IPR006539, P-type_ATPase_IV
IPR032631, P-type_ATPase_N
IPR001757, P_typ_ATPase
IPR032630, P_typ_ATPase_c
IPR044492, P_typ_ATPase_HD_dom
PANTHERiPTHR24092, PTHR24092, 1 hit
PfamiView protein in Pfam
PF16212, PhoLip_ATPase_C, 1 hit
PF16209, PhoLip_ATPase_N, 1 hit
SFLDiSFLDF00027, p-type_atpase, 1 hit
SUPFAMiSSF56784, SSF56784, 1 hit
SSF81653, SSF81653, 1 hit
SSF81660, SSF81660, 1 hit
SSF81665, SSF81665, 1 hit
TIGRFAMsiTIGR01652, ATPase-Plipid, 1 hit
TIGR01494, ATPase_P-type, 2 hits
PROSITEiView protein in PROSITE
PS00154, ATPASE_E1_E2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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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 nameiAT8A2_BOVIN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: C7EXK4
<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: July 9, 2014
Last sequence update: July 9, 2014
Last modified: September 29, 2021
This is version 80 of the entry and version 4 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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