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Protein

Copper-transporting ATPase 1

Gene

Atp7a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells (By similarity).By similarity

Catalytic activityi

ATP + H2O + Cu+(Side 1) = ADP + phosphate + Cu+(Side 2).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei10354-aspartylphosphate intermediateCurated1
Metal bindingi1292MagnesiumPROSITE-ProRule annotation1
Metal bindingi1296MagnesiumPROSITE-ProRule annotation1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • copper-dependent protein binding Source: MGI
  • copper-exporting ATPase activity Source: MGI
  • copper ion binding Source: UniProtKB
  • copper ion transmembrane transporter activity Source: MGI
  • superoxide dismutase copper chaperone activity Source: MGI

GO - Biological processi

  • ATP metabolic process Source: MGI
  • blood vessel development Source: MGI
  • blood vessel remodeling Source: MGI
  • cartilage development Source: MGI
  • catecholamine metabolic process Source: MGI
  • cellular copper ion homeostasis Source: MGI
  • central nervous system neuron development Source: MGI
  • cerebellar Purkinje cell differentiation Source: MGI
  • collagen fibril organization Source: MGI
  • copper ion export Source: MGI
  • copper ion import Source: MGI
  • copper ion transport Source: UniProtKB
  • dendrite morphogenesis Source: MGI
  • detoxification of copper ion Source: MGI
  • dopamine metabolic process Source: MGI
  • elastic fiber assembly Source: MGI
  • elastin biosynthetic process Source: MGI
  • epinephrine metabolic process Source: MGI
  • extracellular matrix organization Source: MGI
  • hair follicle morphogenesis Source: MGI
  • locomotory behavior Source: MGI
  • lung alveolus development Source: MGI
  • mitochondrion organization Source: MGI
  • negative regulation of catalytic activity Source: MGI
  • negative regulation of neuron apoptotic process Source: MGI
  • neuron projection morphogenesis Source: MGI
  • norepinephrine biosynthetic process Source: MGI
  • norepinephrine metabolic process Source: MGI
  • peptidyl-lysine modification Source: MGI
  • pigmentation Source: MGI
  • positive regulation of catalytic activity Source: MGI
  • positive regulation of oxidoreductase activity Source: MGI
  • pyramidal neuron development Source: MGI
  • regulation of gene expression Source: MGI
  • regulation of oxidative phosphorylation Source: MGI
  • release of cytochrome c from mitochondria Source: MGI
  • removal of superoxide radicals Source: MGI
  • serotonin metabolic process Source: MGI
  • skin development Source: MGI
  • T-helper cell differentiation Source: MGI
  • tryptophan metabolic process Source: MGI
  • tyrosine metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Copper transport, Ion transport, Transport

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi3.6.3.4. 3474.
ReactomeiR-MMU-6803544. Ion influx/efflux at host-pathogen interface.
R-MMU-936837. Ion transport by P-type ATPases.

Names & Taxonomyi

Protein namesi
Recommended name:
Copper-transporting ATPase 1 (EC:3.6.3.54)
Alternative name(s):
Copper pump 1
Menkes disease-associated protein homolog
Gene namesi
Name:Atp7a
Synonyms:Mnk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:99400. Atp7a.

Subcellular locationi

  • Golgi apparatustrans-Golgi network membrane By similarity; Multi-pass membrane protein Sequence analysis
  • Cell membrane By similarity; Multi-pass membrane protein Sequence analysis

  • Note: Cycles constitutively between the trans-Golgi network (TGN) and the plasma membrane. Predominantly found in the TGN and relocalized to the plasma membrane in response to elevated copper levels.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 644CytoplasmicSequence analysisAdd BLAST644
Transmembranei645 – 666HelicalSequence analysisAdd BLAST22
Topological domaini667 – 705ExtracellularSequence analysisAdd BLAST39
Transmembranei706 – 725HelicalSequence analysisAdd BLAST20
Topological domaini726 – 732CytoplasmicSequence analysis7
Transmembranei733 – 753HelicalSequence analysisAdd BLAST21
Topological domaini754 – 772ExtracellularSequence analysisAdd BLAST19
Transmembranei773 – 793HelicalSequence analysisAdd BLAST21
Topological domaini794 – 926CytoplasmicSequence analysisAdd BLAST133
Transmembranei927 – 950HelicalSequence analysisAdd BLAST24
Topological domaini951 – 980ExtracellularSequence analysisAdd BLAST30
Transmembranei981 – 1002HelicalSequence analysisAdd BLAST22
Topological domaini1003 – 1347CytoplasmicSequence analysisAdd BLAST345
Transmembranei1348 – 1365HelicalSequence analysisAdd BLAST18
Topological domaini1366 – 1376ExtracellularSequence analysisAdd BLAST11
Transmembranei1377 – 1396HelicalSequence analysisAdd BLAST20
Topological domaini1397 – 1491CytoplasmicSequence analysisAdd BLAST95

GO - Cellular componenti

  • basolateral plasma membrane Source: MGI
  • cytoplasmic vesicle Source: MGI
  • Golgi apparatus Source: MGI
  • integral component of membrane Source: MGI
  • integral component of plasma membrane Source: GO_Central
  • late endosome Source: MGI
  • membrane Source: MGI
  • neuronal cell body Source: MGI
  • neuron projection Source: MGI
  • perinuclear region of cytoplasm Source: MGI
  • plasma membrane Source: MGI
  • trans-Golgi network Source: MGI
  • trans-Golgi network transport vesicle Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Defects in Atp7a are associated with mottled, an X-linked recessive condition characterized by mottled pigmentation of the coat, defects in connective tissue and neonatal or fetal death. It is due to a defect in absorption and transport of copper. The mottled mutants exhibit a diversity of phenotypes. Two of these mutants are called brindled and blotchy and their phenotypes resemble classical Menkes disease (MD) and occipital horn syndrome (OHS) in humans, respectively. Other mutants are called dappled, mosaic, tortoiseshell, pewter, etc.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000463121 – 1491Copper-transporting ATPase 1Add BLAST1491

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei152PhosphothreonineBy similarity1
Modified residuei270PhosphoserineBy similarity1
Modified residuei327PhosphothreonineBy similarity1
Modified residuei339PhosphoserineBy similarity1
Modified residuei353PhosphoserineBy similarity1
Modified residuei357PhosphoserineCombined sources1
Modified residuei362PhosphoserineCombined sources1
Glycosylationi677N-linked (GlcNAc...)Sequence analysis1
Glycosylationi966N-linked (GlcNAc...)Sequence analysis1
Modified residuei1203PhosphothreonineBy similarity1
Modified residuei1421PhosphoserineBy similarity1
Modified residuei1423PhosphoserineBy similarity1
Modified residuei1451PhosphoserineBy similarity1
Modified residuei1454PhosphoserineBy similarity1
Modified residuei1457PhosphoserineCombined sources1
Modified residuei1460PhosphoserineBy similarity1
Modified residuei1464PhosphoserineCombined sources1
Modified residuei1467PhosphoserineCombined sources1
Modified residuei1477PhosphoserineCombined sources1

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ64430.
PaxDbiQ64430.
PRIDEiQ64430.

PTM databases

iPTMnetiQ64430.
PhosphoSitePlusiQ64430.

Expressioni

Tissue specificityi

Found in most tissues except liver. In the kidney, it is detected in the proximal and distal tubules.

Developmental stagei

Widespread expressed throughout development.

Gene expression databases

BgeeiENSMUSG00000033792.
CleanExiMM_ATP7A.
ExpressionAtlasiQ64430. baseline and differential.
GenevisibleiQ64430. MM.

Interactioni

Subunit structurei

Monomer. Interacts with PDZD11 (By similarity). Interacts with ATOX1 and COMMD1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198268. 28 interactors.
IntActiQ64430. 27 interactors.
STRINGi10090.ENSMUSP00000058840.

Structurei

3D structure databases

ProteinModelPortaliQ64430.
SMRiQ64430.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 75HMA 1PROSITE-ProRule annotationAdd BLAST67
Domaini172 – 238HMA 2PROSITE-ProRule annotationAdd BLAST67
Domaini278 – 344HMA 3PROSITE-ProRule annotationAdd BLAST67
Domaini378 – 444HMA 4PROSITE-ProRule annotationAdd BLAST67
Domaini480 – 546HMA 5PROSITE-ProRule annotationAdd BLAST67
Domaini556 – 622HMA 6PROSITE-ProRule annotationAdd BLAST67

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1477 – 1491PDZD11-bindingBy similarityAdd BLAST15

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1478 – 1479Endocytosis signalBy similarity2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi356 – 362Poly-Ser7

Domaini

The C-terminal di-leucine, 1478-Leu-Leu-1479, is an endocytic targeting signal which functions in retrieving recycling from the plasma membrane to the TGN. Mutation of the di-leucine signal results in the accumulation of the protein in the plasma membrane (By similarity).By similarity

Sequence similaritiesi

Contains 6 HMA domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0207. Eukaryota.
COG2217. LUCA.
GeneTreeiENSGT00530000063773.
HOGENOMiHOG000250397.
HOVERGENiHBG050616.
InParanoidiQ64430.
KOiK17686.

Family and domain databases

CDDicd00371. HMA. 6 hits.
Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006122. HMA_Cu_ion-bd.
IPR006121. HMA_dom.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 6 hits.
[Graphical view]
SUPFAMiSSF55008. SSF55008. 6 hits.
SSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
TIGR00003. TIGR00003. 6 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 6 hits.
PS50846. HMA_2. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q64430-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPSVDANSI TITVEGMTCI SCVRTIEQQI GKVNGVHHIK VSLEEKSATI
60 70 80 90 100
IYDPKLQTPK TLQEAIDDMG FDALLHNANP LPVLTNTVFL TVTAPLTLPW
110 120 130 140 150
DHIQSTLLKT KGVTGVKISP QQRSAVVTII PSVVSASQIV ELVPDLSLDM
160 170 180 190 200
GTQEKKSGAC EEHSTPQAGE VMLKMKVEGM TCHSCTSTIE GKVGKLQGVQ
210 220 230 240 250
RIKVSLDNQE ATIVFQPHLI TAEEIKKQIE AVGFPAFIKK QPKYLKLGAI
260 270 280 290 300
DVERLKNTPV KSSEGSQQKS PSYPSDSTTM FTIEGMHCKS CVSNIESALS
310 320 330 340 350
TLQYVSSIVV SLENRSAIVK YNASLVTPEM LRKAIEAISP GQYRVSIASE
360 370 380 390 400
VESTASSPSS SSLQKMPLNI VSQPLTQEAV ININGMTCNS CVQSIEGVIS
410 420 430 440 450
KKPGVKSIHV SLANSTGTIE FDPLLTSPET LREAIEDMGF DAALPDMKEP
460 470 480 490 500
LVVIAQPSLE TPLLPSSNEL ENVMTSVQNK CYIQVSGMTC ASCVANIERN
510 520 530 540 550
LRREEGIYSV LVALMAGKAE VRYNPAVIQP RVIAEFIREL GFGAMVMENA
560 570 580 590 600
GEGNGILELV VRGMTCASCV HKIESTLTKH KGIFYCSVAL ATNKAHIKYD
610 620 630 640 650
PEIIGPRDII HTIGSLGFEA SLVKKDRSAN HLDHKREIKQ WRGSFLVSLF
660 670 680 690 700
FCIPVMGLMV YMMVMDHHLA TLHHNQNMSN EEMINMHSAM FLERQILPGL
710 720 730 740 750
SIMNLLSLLL CLPVQFCGGW YFYIQAYKAL KHKTANMDVL IVLATTIAFA
760 770 780 790 800
YSLVILLVAM FERAKVNPIT FFDTPPMLFV FIALGRWLEH IAKGKTSEAL
810 820 830 840 850
AKLISLQATE ATIVTLNSEN LLLSEEQVDV ELVQRGDIIK VVPGGKFPVD
860 870 880 890 900
GRVIEGHSMV DESLITGEAM PVAKKPGSTV IAGSINQNGS LLIRATHVGA
910 920 930 940 950
DTTLSQIVKL VEEAQTSKAP IQQFADKLSG YFVPFIVLVS IVTLLVWIII
960 970 980 990 1000
GFQNFEIVET YFPGYNRSIS RTETIIRFAF QASITVLCIA CPCSLGLATP
1010 1020 1030 1040 1050
TAVMVGTGVG AQNGILIKGG EPLEMAHKVK VVVFDKTGTI THGTPVVNQV
1060 1070 1080 1090 1100
KVLVESNKIS RNKILAIVGT AESNSEHPLG AAVTKYCKKE LDTETLGTCT
1110 1120 1130 1140 1150
DFQVVPGCGI SCKVTNIEGL LHKSNLKIEE NNIKNASLVQ IDAINEQSST
1160 1170 1180 1190 1200
SSSMIIDAHL SNAVNTQQYK VLIGNREWMI RNGLVISNDV DESMIEHERR
1210 1220 1230 1240 1250
GRTAVLVTID DELCGLIAIA DTVKPEAELA VHILKSMGLE VVLMTGDNSK
1260 1270 1280 1290 1300
TARSIASQVG ITKVFAEVLP SHKVAKVKQL QEEGKRVAMV GDGINDSPAL
1310 1320 1330 1340 1350
AMANVGIAIG TGTDVAIEAA DVVLIRNDLL DVVASIDLSR KTVKRIRINF
1360 1370 1380 1390 1400
VFALIYNLVG IPIAAGVFLP IGLVLQPWMG SAAMAASSVS VVLSSLFLKL
1410 1420 1430 1440 1450
YRKPTYDNYE LHPRSHTGQR SPSEISVHVG IDDTSRNSPR LGLLDRIVNY
1460 1470 1480 1490
SRASINSLLS DKRSLNSVVT SEPDKHSLLV GDFREDDDTT L
Length:1,491
Mass (Da):161,959
Last modified:July 27, 2011 - v3
Checksum:i2FADCC6806994CA5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti44E → D in AAA57445 (PubMed:8054976).Curated1
Sequence conflicti44E → D in AAB37301 (PubMed:9215672).Curated1
Sequence conflicti103I → V in AAA57445 (PubMed:8054976).Curated1
Sequence conflicti103I → V in AAB37301 (PubMed:9215672).Curated1
Sequence conflicti172M → R in AAA57445 (PubMed:8054976).Curated1
Sequence conflicti172M → R in AAB37301 (PubMed:9215672).Curated1
Sequence conflicti245 – 246LK → PI in AAB08487 (PubMed:8054977).Curated2
Sequence conflicti445P → PA in AAB08487 (PubMed:8054977).Curated1
Sequence conflicti445P → PA in AAB37301 (PubMed:9215672).Curated1
Sequence conflicti470L → P in AAB08487 (PubMed:8054977).Curated1
Sequence conflicti470L → P in BAA22369 (PubMed:9385451).Curated1
Sequence conflicti470L → P in AAB37301 (PubMed:9215672).Curated1
Sequence conflicti515M → T in AAA57445 (PubMed:8054976).Curated1
Sequence conflicti515M → T in AAB37301 (PubMed:9215672).Curated1
Sequence conflicti717C → F in AAB08487 (PubMed:8054977).Curated1
Sequence conflicti770T → A in AAB08487 (PubMed:8054977).Curated1
Sequence conflicti775P → S in AAB08487 (PubMed:8054977).Curated1
Sequence conflicti885I → T in AAB08487 (PubMed:8054977).Curated1
Sequence conflicti1169Y → H in AAB08487 (PubMed:8054977).Curated1
Sequence conflicti1204A → P in AAB08487 (PubMed:8054977).Curated1
Sequence conflicti1204A → P in AAB37301 (PubMed:9215672).Curated1
Sequence conflicti1217I → M in AAA57445 (PubMed:8054976).Curated1
Sequence conflicti1253R → Q in AAA57445 (PubMed:8054976).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti674H → R in MD. 1 Publication1
Natural varianti1381S → P in MD. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03434 mRNA. Translation: AAA57445.1.
U03736 mRNA. Translation: AAB08487.1.
AB007134 mRNA. Translation: BAA22369.1.
U71091 mRNA. Translation: AAB37301.1.
AL672288 Genomic DNA. Translation: CAM16891.1.
CCDSiCCDS41097.1.
PIRiS43793.
RefSeqiNP_033856.3. NM_009726.5.
UniGeneiMm.254297.

Genome annotation databases

EnsembliENSMUST00000113557; ENSMUSP00000109186; ENSMUSG00000033792.
GeneIDi11977.
KEGGimmu:11977.
UCSCiuc012hnn.2. mouse.

Cross-referencesi

Web resourcesi

Protein Spotlight

Heavy metal - Issue 79 of February 2007

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03434 mRNA. Translation: AAA57445.1.
U03736 mRNA. Translation: AAB08487.1.
AB007134 mRNA. Translation: BAA22369.1.
U71091 mRNA. Translation: AAB37301.1.
AL672288 Genomic DNA. Translation: CAM16891.1.
CCDSiCCDS41097.1.
PIRiS43793.
RefSeqiNP_033856.3. NM_009726.5.
UniGeneiMm.254297.

3D structure databases

ProteinModelPortaliQ64430.
SMRiQ64430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198268. 28 interactors.
IntActiQ64430. 27 interactors.
STRINGi10090.ENSMUSP00000058840.

PTM databases

iPTMnetiQ64430.
PhosphoSitePlusiQ64430.

Proteomic databases

MaxQBiQ64430.
PaxDbiQ64430.
PRIDEiQ64430.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000113557; ENSMUSP00000109186; ENSMUSG00000033792.
GeneIDi11977.
KEGGimmu:11977.
UCSCiuc012hnn.2. mouse.

Organism-specific databases

CTDi538.
MGIiMGI:99400. Atp7a.

Phylogenomic databases

eggNOGiKOG0207. Eukaryota.
COG2217. LUCA.
GeneTreeiENSGT00530000063773.
HOGENOMiHOG000250397.
HOVERGENiHBG050616.
InParanoidiQ64430.
KOiK17686.

Enzyme and pathway databases

BRENDAi3.6.3.4. 3474.
ReactomeiR-MMU-6803544. Ion influx/efflux at host-pathogen interface.
R-MMU-936837. Ion transport by P-type ATPases.

Miscellaneous databases

ChiTaRSiAtp7a. mouse.
PROiQ64430.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000033792.
CleanExiMM_ATP7A.
ExpressionAtlasiQ64430. baseline and differential.
GenevisibleiQ64430. MM.

Family and domain databases

CDDicd00371. HMA. 6 hits.
Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006122. HMA_Cu_ion-bd.
IPR006121. HMA_dom.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 6 hits.
[Graphical view]
SUPFAMiSSF55008. SSF55008. 6 hits.
SSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
TIGR00003. TIGR00003. 6 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 6 hits.
PS50846. HMA_2. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATP7A_MOUSE
AccessioniPrimary (citable) accession number: Q64430
Secondary accession number(s): A2AG69
, O35101, P97422, Q64431
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 169 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  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.