Tag | Content |
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CPLM ID | CPLM-006927 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | P-type cation-transporting ATPase |
Protein Synonyms/Alias | Cadmium resistance protein 2; Cadmium-translocating P-type ATPase; Cd(2+)-exporting ATPase |
Gene Name | PCA1 |
Gene Synonyms/Alias | CAD2; PAY2; YBR295W; YBR2112 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
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964 | AQNVSNTKAVTGKRV | ubiquitination | [1] |
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Reference | [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J. Nat Methods. 2013 Jul;10(7):676-82. [ PMID: 23749301] |
Functional Description | Cadmium transporting P-type ATPase which plays a critical role in cadmium resistance by extruding intracellular cadmium. Capable of high affinity copper ion binding, but not active copper ion transport. May play a role in copper resistance by chelating and sequestering copper ions. |
Sequence Annotation | DOMAIN 411 474 HMA. REGION 250 350 Metal-responding degradation signal. ACT_SITE 903 903 4-aspartylphosphate intermediate (By METAL 421 421 Copper (Potential). METAL 424 424 Copper (Potential). METAL 1107 1107 Magnesium (By similarity). METAL 1111 1111 Magnesium (By similarity). |
Keyword | ATP-binding; Cadmium; Cadmium resistance; Cell membrane; Complete proteome; Copper; Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix; Transport; Ubl conjugation. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1216 AA |
Protein Sequence | MKPEKLFSGL GTSDGEYGVV NSENISIDAM QDNRGECHRR SIEMHANDNL GLVSQRDCTN 60 RPKITPQECL SETEQICHHG ENRTKAGLDV DDAETGGDHT NESRVDECCA EKVNDTETGL 120 DVDSCCGDAQ TGGDHTNESC VDGCCVRDSS VMVEEVTGSC EAVSSKEQLL TSFEVVPSKS 180 EGLQSIHDIR ETTRCNTNSN QHTGKGRLCI ESSDSTLKKR SCKVSRQKIE VSSKPECCNI 240 SCVERIASRS CEKRTFKGST NVGISGSSST DSLSEKFFSE QYSRMYNRYS SILKNLGCIC 300 NYLRTLGKES CCLPKVRFCS GEGASKKTKY SYRNSSGCLT KKKTHGDKER LSNDNGHADF 360 VCSKSCCTKM KDCAVTSTIS GHSSSEISRI VSMEPIENHL NLEAGSTGTE HIVLSVSGMS 420 CTGCESKLKK SFGALKCVHG LKTSLILSQA EFNLDLAQGS VKDVIKHLSK TTEFKYEQIS 480 NHGSTIDVVV PYAAKDFINE EWPQGVTELK IVERNIIRIY FDPKVIGARD LVNEGWSVPV 540 SIAPFSCHPT IEVGRKHLVR VGCTTALSII LTIPILVMAW APQLREKIST ISASMVLATI 600 IQFVIAGPFY LNALKSLIFS RLIEMDLLIV LSTSAAYIFS IVSFGYFVVG RPLSTEQFFE 660 TSSLLVTLIM VGRFVSELAR HRAVKSISVR SLQASSAILV DKTGKETEIN IRLLQYGDIF 720 KVLPDSRIPT DGTVISGSSE VDEALITGES MPVPKKCQSI VVAGSVNGTG TLFVKLSKLP 780 GNNTISTIAT MVDEAKLTKP KIQNIADKIA SYFVPTIIGI TVVTFCVWIA VGIRVEKQSR 840 SDAVIQAIIY AITVLIVSCP CVIGLAVPIV FVIASGVAAK RGVIFKSAES IEVAHNTSHV 900 VFDKTGTLTE GKLTVVHETV RGDRHNSQSL LLGLTEGIKH PVSMAIASYL KEKGVSAQNV 960 SNTKAVTGKR VEGTSYSGLK LQGGNCRWLG HNNDPDVRKA LEQGYSVFCF SVNGSVTAVY 1020 ALEDSLRADA VSTINLLRQR GISLHILSGD DDGAVRSMAA RLGIESSNIR SHATPAEKSE 1080 YIKDIVEGRN CDSSSQSKRP VVVFCGDGTN DAIGLTQATI GVHINEGSEV AKLAADVVML 1140 KPKLNNILTM ITVSQKAMFR VKLNFLWSFT YNLFAILLAA GAFVDFHIPP EYAGLGELVS 1200 ILPVIFVAIL LRYAKI 1216 |
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