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Protein

ATPase 2, plasma membrane-type

Gene

AHA2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The plasma membrane H+ ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H+-symport (PubMed:10748244, PubMed:12920605, PubMed:27013734). The resulting external acidification and/or internal alkinization may mediate growth responses (PubMed:10748244, PubMed:12920605). Involved in maintaining the membrane potential and delta-pH, together forming the plasma membrane protonmotive force (PMF) required for root and hypocotyl elongation and root tropism (PubMed:22214817, PubMed:24492258). Important for root growth and development during different nitrogen regimes (PubMed:25382626). Forms a functional cation-translocating unit with CNGC17 that is activated by PSKR1/BAK1 and possibly other BAK1/RLK complexes (PubMed:26071421).1 Publication6 Publications

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).Curated

Enzyme regulationi

Regulated by an auto-inhibitory C-terminal domain that can be displaced by phosphorylation of Thr-947 and the subsequent binding of 14-3-3 proteins (PubMed:10353834). Negatively regulated by PKS5 (PubMed:17483306). PKS5 phosphorylates Ser-931, inhibiting interaction with the activating 14-3-3 protein (PubMed:17483306). Positively regulated by PSY1R (PubMed:25267325). PSY1R phosphorylates Thr-881, situated in the auto-inhibitory region I of the C-terminal domain, causing pump activation (PubMed:25267325). Negatively regulated by the secreted peptide RALF (PubMed:24458638). After specific binding to FERONIA, RALF causes phosphorylation at Ser-899, mediating the inhibition of proton transport (PubMed:24458638). Activated by lysophospholipids, without the involvement of phosphorylation of Thr-947 (PubMed:25971968). This activation is critically dependent on the single autoinhibitory residue Leu-919 (PubMed:25971968).6 Publications

Kineticsi

  1. KM=1.2 mM for ATP1 Publication
  1. Vmax=0.87 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei3294-aspartylphosphate intermediateBy similarity1
Metal bindingi588MagnesiumBy similarity1
Metal bindingi592MagnesiumBy similarity1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • hydrogen-exporting ATPase activity, phosphorylative mechanism Source: UniProtKB
  • magnesium ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT4G30190-MONOMER.
BRENDAi3.6.3.6. 399.
SABIO-RKP19456.

Protein family/group databases

TCDBi3.A.3.3.9. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
ATPase 2, plasma membrane-type1 Publication (EC:3.6.3.6Curated)
Alternative name(s):
Proton pump 2
Gene namesi
Name:AHA21 Publication
Ordered Locus Names:At4g30190Imported
ORF Names:F9N11.40Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G30190.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 61CytoplasmicSequence analysisAdd BLAST60
Transmembranei62 – 81Helical; Name=1Sequence analysisAdd BLAST20
Topological domaini82 – 93ExtracellularSequence analysisAdd BLAST12
Transmembranei94 – 114Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini115 – 243CytoplasmicSequence analysisAdd BLAST129
Transmembranei244 – 264Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini265 – 273ExtracellularSequence analysis9
Transmembranei274 – 291Helical; Name=4Sequence analysisAdd BLAST18
Topological domaini292 – 643CytoplasmicSequence analysisAdd BLAST352
Transmembranei644 – 665Helical; Name=5Sequence analysisAdd BLAST22
Topological domaini666 – 670ExtracellularSequence analysis5
Transmembranei671 – 693Helical; Name=6Sequence analysisAdd BLAST23
Topological domaini694 – 709CytoplasmicSequence analysisAdd BLAST16
Transmembranei710 – 730Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini731 – 751ExtracellularSequence analysisAdd BLAST21
Transmembranei752 – 772Helical; Name=8Sequence analysisAdd BLAST21
Topological domaini773 – 784CytoplasmicSequence analysisAdd BLAST12
Transmembranei785 – 805Helical; Name=9Sequence analysisAdd BLAST21
Topological domaini806 – 813ExtracellularSequence analysis8
Transmembranei814 – 834Helical; Name=10Sequence analysisAdd BLAST21
Topological domaini835 – 948CytoplasmicSequence analysisAdd BLAST114

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB
  • integral component of plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions, due to the redudancy with AHA1. Aha1 and aha2 double mutants are embryo lethal.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi106N → A, D, K, Q or T: Reduced proton transport. 1 Publication1
Mutagenesisi655R → A or D: No effect on ATP affinity, but reduced proton transport. 1 Publication1
Mutagenesisi655R → K: No effect on ATP affinity and proton transport. 1 Publication1
Mutagenesisi684D → A, V or R: No effect on ATP affinity, but loss of proton transport. 1 Publication1
Mutagenesisi684D → E: No effect on ATP affinity, but reduced proton transport. 1 Publication1
Mutagenesisi684D → N: Insensitive to the inhibitor vanadate and locked in the E1 conformation. No effect on ATP hydrolysis, but loss of proton transport. 2 Publications1
Mutagenesisi881T → A: Decreased phosphorylation by PSY1R. 1 Publication1
Mutagenesisi881T → D: No effect on 14-3-3 protein binding, but increased activity. 1 Publication1
Mutagenesisi904S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi919L → A: Loss of activation by lysophospholipids. 1 Publication1
Mutagenesisi922L → A: Increased activation by lysophospholipids. 1 Publication1
Mutagenesisi924T → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi931S → A: Loss of phosphorylation and increased 14-3-3 protein binding. 1 Publication1
Mutagenesisi931S → D: Loss of interaction with 14-3-3 protein. 1 Publication1
Mutagenesisi942T → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi947T → A: No effect on phosphorylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000462752 – 948ATPase 2, plasma membrane-typeAdd BLAST947

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei881Phosphothreonine1 Publication1
Modified residuei899Phosphoserine1 Publication1
Modified residuei931Phosphoserine; by CIPK111 Publication1
Modified residuei947Phosphothreonine1 Publication1

Post-translational modificationi

Phosphorylation at Thr-881 by PSY1R (PubMed:17651370, PubMed:25267325). This phosphrylation activates proton pumping (PubMed:25267325). Decreased phosphorylation in response to flg22 elicitation (PubMed:17651370).2 Publications
Phosphorylation at Ser-899 is specifically induced by RALF1, thus leading to the inhibition of proton transport (PubMed:24458638). Increased phosphorylation in response to flg22 elicitation (PubMed:17651370).2 Publications
Phosphorylation of Thr-947 induces the binding to 14-3-3 proteins, but phosphorylation of Ser-931 interfers with this binding no matter whether Thr-947 is phosphorylated or not (PubMed:10593986, PubMed:17483306). Decreased phosphorylation in response to flg22 elicitation (PubMed:17651370).3 Publications
Abscisic acid induces dephosphorylation of AHA2 in etiolated seedlings, suppressing ATP hydrolysis and hypocotyl elongation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP19456.
PRIDEiP19456.

PTM databases

iPTMnetiP19456.

Expressioni

Tissue specificityi

Higher levels in roots than in shoots (PubMed:2143186). Expressed in epidermal and root cortex cells, in phloem, xylem and root hairs (PubMed:17483306). Detected in cotyledons, hypocotyls, roots and root hairs (PubMed:25267325).3 Publications

Developmental stagei

Expressed on the surface of developing seeds and up to the early globular stage of embryo development.1 Publication

Inductioni

Up-regulated by low nitrate conditions.1 Publication

Gene expression databases

ExpressionAtlasiP19456. baseline and differential.
GenevisibleiP19456. AT.

Interactioni

Subunit structurei

Binds to 14-3-3 proteins (PubMed:10593986). The binding is induced by phosphorylation of Thr-947 and it activates the H+-ATPase (PubMed:10593986). Interacts (via the R-domain) with PSY1R (via C-terminus) (PubMed:25267325). Part of a functional complex containing PSKR1, BAK1, CNGC17, and AHA (PubMed:26071421). Interacts with CNGC17 and PSKR1 (PubMed:26071421).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CIPK11O229323EBI-2293350,EBI-537638

Protein-protein interaction databases

BioGridi14429. 40 interactors.
IntActiP19456. 4 interactors.
MINTiMINT-112688.
STRINGi3702.AT4G30190.2.

Structurei

Secondary structure

1948
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi20 – 26Combined sources7
Helixi36 – 45Combined sources10
Helixi57 – 59Combined sources3
Turni60 – 62Combined sources3
Helixi68 – 83Combined sources16
Turni84 – 88Combined sources5
Helixi90 – 120Combined sources31
Helixi122 – 128Combined sources7
Beta strandi131 – 136Combined sources6
Beta strandi139 – 144Combined sources6
Beta strandi150 – 156Combined sources7
Beta strandi166 – 172Combined sources7
Beta strandi174 – 177Combined sources4
Turni179 – 182Combined sources4
Beta strandi188 – 190Combined sources3
Beta strandi201 – 204Combined sources4
Beta strandi207 – 211Combined sources5
Turni215 – 217Combined sources3
Helixi219 – 223Combined sources5
Helixi235 – 254Combined sources20
Turni255 – 257Combined sources3
Helixi258 – 265Combined sources8
Helixi271 – 273Combined sources3
Helixi274 – 284Combined sources11
Helixi288 – 307Combined sources20
Helixi316 – 322Combined sources7
Beta strandi325 – 329Combined sources5
Helixi330 – 334Combined sources5
Helixi343 – 345Combined sources3
Turni355 – 357Combined sources3
Helixi358 – 364Combined sources7
Beta strandi368 – 370Combined sources3
Helixi373 – 381Combined sources9
Helixi385 – 389Combined sources5
Beta strandi394 – 398Combined sources5
Turni402 – 404Combined sources3
Beta strandi406 – 413Combined sources8
Turni414 – 416Combined sources3
Beta strandi417 – 424Combined sources8
Helixi426 – 429Combined sources4
Turni430 – 434Combined sources5
Helixi437 – 453Combined sources17
Beta strandi456 – 464Combined sources9
Beta strandi478 – 486Combined sources9
Helixi493 – 502Combined sources10
Beta strandi506 – 510Combined sources5
Helixi515 – 525Combined sources11
Helixi534 – 537Combined sources4
Beta strandi538 – 542Combined sources5
Turni546 – 548Combined sources3
Helixi551 – 557Combined sources7
Beta strandi559 – 563Combined sources5
Helixi566 – 578Combined sources13
Beta strandi583 – 587Combined sources5
Helixi590 – 592Combined sources3
Helixi593 – 598Combined sources6
Beta strandi599 – 604Combined sources6
Helixi610 – 615Combined sources6
Beta strandi617 – 622Combined sources6
Helixi625 – 667Combined sources43
Helixi673 – 686Combined sources14
Helixi687 – 692Combined sources6
Helixi706 – 730Combined sources25
Turni731 – 733Combined sources3
Helixi736 – 739Combined sources4
Helixi750 – 773Combined sources24
Turni778 – 780Combined sources3
Helixi785 – 804Combined sources20
Turni808 – 811Combined sources4
Helixi817 – 843Combined sources27

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5KSDX-ray3.50A/B12-844[»]
ProteinModelPortaliP19456.
SMRiP19456.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19456.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni946 – 948Interaction with 14-3-3 proteins3

Domaini

The C-terminus contains a R-domain composed of 2 autoinhibitory regions (863-885 and 904-919).1 Publication

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0205. Eukaryota.
COG0474. LUCA.
HOGENOMiHOG000160005.
InParanoidiP19456.
KOiK01535.
PhylomeDBiP19456.

Family and domain databases

Gene3Di1.20.1110.10. 3 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006534. P-type_ATPase_IIIA.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01647. ATPase-IIIA_H. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: P19456-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSSLEDIKNE TVDLEKIPIE EVFQQLKCSR EGLTTQEGED RIQIFGPNKL
60 70 80 90 100
EEKKESKLLK FLGFMWNPLS WVMEMAAIMA IALANGDGRP PDWQDFVGII
110 120 130 140 150
CLLVINSTIS FIEENNAGNA AAALMAGLAP KTKVLRDGKW SEQEAAILVP
160 170 180 190 200
GDIVSIKLGD IIPADARLLE GDPLKVDQSA LTGESLPVTK HPGQEVFSGS
210 220 230 240 250
TCKQGEIEAV VIATGVHTFF GKAAHLVDST NQVGHFQKVL TAIGNFCICS
260 270 280 290 300
IAIGMVIEII VMYPIQRRKY RDGIDNLLVL LIGGIPIAMP TVLSVTMAIG
310 320 330 340 350
SHRLSQQGAI TKRMTAIEEM AGMDVLCSDK TGTLTLNKLS VDKNLVEVFC
360 370 380 390 400
KGVEKDQVLL FAAMASRVEN QDAIDAAMVG MLADPKEARA GIREVHFLPF
410 420 430 440 450
NPVDKRTALT YIDGSGNWHR VSKGAPEQIL ELAKASNDLS KKVLSIIDKY
460 470 480 490 500
AERGLRSLAV ARQVVPEKTK ESPGAPWEFV GLLPLFDPPR HDSAETIRRA
510 520 530 540 550
LNLGVNVKMI TGDQLAIGKE TGRRLGMGTN MYPSSALLGT HKDANLASIP
560 570 580 590 600
VEELIEKADG FAGVFPEHKY EIVKKLQERK HIVGMTGDGV NDAPALKKAD
610 620 630 640 650
IGIAVADATD AARGASDIVL TEPGLSVIIS AVLTSRAIFQ RMKNYTIYAV
660 670 680 690 700
SITIRIVFGF MLIALIWEFD FSAFMVLIIA ILNDGTIMTI SKDRVKPSPT
710 720 730 740 750
PDSWKLKEIF ATGVVLGGYQ AIMTVIFFWA AHKTDFFSDT FGVRSIRDNN
760 770 780 790 800
HELMGAVYLQ VSIISQALIF VTRSRSWSFV ERPGALLMIA FLIAQLIATL
810 820 830 840 850
IAVYANWEFA KIRGIGWGWA GVIWLYSIVT YFPLDVFKFA IRYILSGKAW
860 870 880 890 900
LNLFENKTAF TMKKDYGKEE REAQWALAQR TLHGLQPKEA VNIFPEKGSY
910 920 930 940
RELSEIAEQA KRRAEIARLR ELHTLKGHVE SVVKLKGLDI ETPSHYTV
Length:948
Mass (Da):104,401
Last modified:January 23, 2007 - v2
Checksum:i431F4021E99A3CEC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05570 Genomic DNA. Translation: AAA32751.1.
AL109796 Genomic DNA. Translation: CAB52463.1.
AL161576 Genomic DNA. Translation: CAB81012.1.
CP002687 Genomic DNA. Translation: AEE85731.1.
AY035075 mRNA. Translation: AAK59580.1.
BT000781 mRNA. Translation: AAN31920.1.
BT001969 mRNA. Translation: AAN71968.1.
PIRiA37116. PXMUP2.
RefSeqiNP_194748.1. NM_119165.4. [P19456-1]
UniGeneiAt.23014.

Genome annotation databases

EnsemblPlantsiAT4G30190.1; AT4G30190.1; AT4G30190. [P19456-1]
GeneIDi829142.
GrameneiAT4G30190.1; AT4G30190.1; AT4G30190.
KEGGiath:AT4G30190.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05570 Genomic DNA. Translation: AAA32751.1.
AL109796 Genomic DNA. Translation: CAB52463.1.
AL161576 Genomic DNA. Translation: CAB81012.1.
CP002687 Genomic DNA. Translation: AEE85731.1.
AY035075 mRNA. Translation: AAK59580.1.
BT000781 mRNA. Translation: AAN31920.1.
BT001969 mRNA. Translation: AAN71968.1.
PIRiA37116. PXMUP2.
RefSeqiNP_194748.1. NM_119165.4. [P19456-1]
UniGeneiAt.23014.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5KSDX-ray3.50A/B12-844[»]
ProteinModelPortaliP19456.
SMRiP19456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14429. 40 interactors.
IntActiP19456. 4 interactors.
MINTiMINT-112688.
STRINGi3702.AT4G30190.2.

Protein family/group databases

TCDBi3.A.3.3.9. the p-type atpase (p-atpase) superfamily.

PTM databases

iPTMnetiP19456.

Proteomic databases

PaxDbiP19456.
PRIDEiP19456.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G30190.1; AT4G30190.1; AT4G30190. [P19456-1]
GeneIDi829142.
GrameneiAT4G30190.1; AT4G30190.1; AT4G30190.
KEGGiath:AT4G30190.

Organism-specific databases

TAIRiAT4G30190.

Phylogenomic databases

eggNOGiKOG0205. Eukaryota.
COG0474. LUCA.
HOGENOMiHOG000160005.
InParanoidiP19456.
KOiK01535.
PhylomeDBiP19456.

Enzyme and pathway databases

BioCyciARA:AT4G30190-MONOMER.
BRENDAi3.6.3.6. 399.
SABIO-RKP19456.

Miscellaneous databases

EvolutionaryTraceiP19456.
PROiP19456.

Gene expression databases

ExpressionAtlasiP19456. baseline and differential.
GenevisibleiP19456. AT.

Family and domain databases

Gene3Di1.20.1110.10. 3 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006534. P-type_ATPase_IIIA.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01647. ATPase-IIIA_H. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPMA2_ARATH
AccessioniPrimary (citable) accession number: P19456
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The catalytic mechanism involves at least four different enzyme conformational states named E1, E1P, E2P, and E2, with the E1P-E2P transition accompanying the transfer of ion across the membrane. E1P and E2P are phosphorylated intermediates.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.