Annotation for this protein is in progress - please check future releases for more complete information



DP00282: Copper-transporting ATPase 1 [Isoform 4]FASTA viewXML view

General information
DisProt:DP00282
Name:Copper-transporting ATPase 1 [Isoform 4]
Synonym(s):ATP7A_HUMAN
EC 3.6.3.4
Copper pump 1
Menkes disease-associated protein
First appeared in release:Release 3.0 (02/17/2006)
UniProt:Q04656-1
UniGene:Hs.496414
SwissProt: ATP7A_HUMAN
TrEMBL:  
NCBI (GI): 223590241
Source organism:Homo sapiens (Human)
Sequence length:1500
Percent disordered:2%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MDPSMGVNSV TISVEGMTCN SCVWTIEQQI GKVNGVHHIK VSLEEKNATI IYDPKLQTPK - 60
TLQEAIDDMG FDAVIHNPDP LPVLTDTLFL TVTASLTLPW DHIQSTLLKT KGVTDIKIYP - 120
QKRTVAVTII PSIVNANQIK ELVPELSLDT GTLEKKSGAC EDHSMAQAGE VVLKMKVEGM - 180
TCHSCTSTIE GKIGKLQGVQ RIKVSLDNQE ATIVYQPHLI SVEEMKKQIE AMGFPAFVKK - 240
QPKYLKLGAI DVERLKNTPV KSSEGSQQRS PSYTNDSTAT FIIDGMHCKS CVSNIESTLS - 300
ALQYVSSIVV SLENRSAIVK YNASSVTPES LRKAIEAVSP GLYRVSITSE VESTSNSPSS - 360
SSLQKIPLNV VSQPLTQETV INIDGMTCNS CVQSIEGVIS KKPGVKSIRV SLANSNGTVE - 420
YDPLLTSPET LRGAIEDMGF DATLSDTNEP LVVIAQPSSE MPLLTSTNEF YTKGMTPVQD - 480
KEEGKNSSKC YIQVTGMTCA SCVANIERNL RREEGIYSIL VALMAGKAEV RYNPAVIQPP - 540
MIAEFIRELG FGATVIENAD EGDGVLELVV RGMTCASCVH KIESSLTKHR GILYCSVALA - 600
TNKAHIKYDP EIIGPRDIIH TIESLGFEAS LVKKDRSASH LDHKREIRQW RRSFLVSLFF - 660
CIPVMGLMTY MMVMDHHFAT LHHNQNMSKE EMINLHSSMF LERQILPGLS VMNLLSFLLC - 720
VPVQFFGGWY FYIQAYKALK HKTANMDVLI VLATTIAFAY SLIILLVAMY ERAKVNPITF - 780
FDTPPMLFVF IALGRWLEHI AKGKTSEALA KLISLQATEA TIVTLDSDNI LLSEEQVDVE - 840
LVQRGDIIKV VPGGKFPVDG RVIEGHSMVD ESLITGEAMP VAKKPGSTVI AGSINQNGSL - 900
LICATHVGAD TTLSQIVKLV EEAQTSKAPI QQFADKLSGY FVPFIVFVSI ATLLVWIVIG - 960
FLNFEIVETY FPGYNRSISR TETIIRFAFQ ASITVLCIAC PCSLGLATPT AVMVGTGVGA - 1020
QNGILIKGGE PLEMAHKVKV VVFDKTGTIT HGTPVVNQVK VLTESNRISH HKILAIVGTA - 1080
ESNSEHPLGT AITKYCKQEL DTETLGTCID FQVVPGCGIS CKVTNIEGLL HKNNWNIEDN - 1140
NIKNASLVQI DASNEQSSTS SSMIIDAQIS NALNAQQHKV LIGNREWMIR NGLVINNDVN - 1200
DFMTEHERKG RTAVLVAVDD ELCGLIAIAD TVKPEAELAI HILKSMGLEV VLMTGDNSKT - 1260
ARSIASQVGI TKVFAEVLPS HKVAKVKQLQ EEGKRVAMVG DGINDSPALA MANVGIAIGT - 1320
GTDVAIEAAD VVLIRNDLLD VVASIDLSRK TVKRIRINFV FALIYNLVGI PIAAGVFMPI - 1380
GLVLQPWMGS AAMAASSVSV VLSSLFLKLY RKPTYESYEL PARSQIGQKS PSEISVHVGI - 1440
DDTSRNSPKL GLLDRIVNYS RASINSLLSD KRSLNSVVTS EPDKHSLLVG DFREDDDTAL - 1500

Region 1: 164-168 Region 2: 171-180 Region 3: 239-246

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:164 - 168
Length:5
Region sequence:

SMAQA

Modification type: Fragment
Mutant
PDB:  
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
  1. Nuclear magnetic resonance (NMR) (298 K; )

References:
  1. Jones CE, Daly NL, Cobine PA, Craik DJ, Dameron CT. "Structure and metal binding studies of the second copper binding domain of the Menkes ATPase." J Struct Biol. 2003; 143(3): 209-18. PubMed: 14572476

Comments:
A single point mutation of MNKr2 was created with a F72I substitution, as discussed in the Jones et al. article.




Region 2
Type:Disordered
Name:Loop 1
Location:171 - 180
Length:10
Region sequence:

VVLKMKVEGM

Modification type: Monomeric
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes:  
Functional subclasses: Substrate/ligand binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (298 K; )

  2. Nuclear magnetic resonance (NMR) (298 K; pH: 7; 2H2O (v/v) 10 %; DTT (excess); protein 1 mM; sodium phsophate (buffer) 100 mM)

References:
  1. Banci L, Bertini I, Del Conte R, D'Onofrio M, Rosato A. "Solution structure and backbone dynamics of the Cu(I) and apo forms of the second metal-binding domain of the Menkes protein ATP7A." Biochemistry. 2004; 43(12): 3396-403. PubMed: 15035611

  2. Jones CE, Daly NL, Cobine PA, Craik DJ, Dameron CT. "Structure and metal binding studies of the second copper binding domain of the Menkes ATPase." J Struct Biol. 2003; 143(3): 209-18. PubMed: 14572476

Comments:
 



Region 3
Type:Disordered
Name: 
Location:239 - 246
Length:8
Region sequence:

KKQPKYLK

Modification type: Fragment
Mutant
PDB:  
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
  1. Nuclear magnetic resonance (NMR) (298 K; )

References:
  1. Jones CE, Daly NL, Cobine PA, Craik DJ, Dameron CT. "Structure and metal binding studies of the second copper binding domain of the Menkes ATPase." J Struct Biol. 2003; 143(3): 209-18. PubMed: 14572476

Comments:
A single point mutation of MNKr2 was created with a F72I substitution, as discussed in the Jones et al. article.



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