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3.A.3.2.43
SERCA of 1001 aas.  Several 3-D structures are known (e.g., 3W5B).  Molecular dynamics simulations provided evidence for the role of the Mg2+ and K+ bound states in the transport mechanism (Espinoza-Fonseca et al. 2014).  Animal SERCAs are inhibited by three short single TMS membrane proteins, phospholamban (TC# 1.A.50.1), sarcolipin (1.A.50.2) and myoregulin (1.A.50.3), and the inhibitory actions of these peptides on SERCA are counteracted by a peptide called DWORF (Dwarf ORF) (Nelson et al. 2016; Anderson et al. 2015).  Norimatsu et al. 2017 have resolved the first layer of phospholipids surrounding the transmembrane helices. Phospholipids follow the movements of associated residues, causing local distortions and changes in thickness of the bilayer. The entire protein tilts during the reaction cycle, governed primarily by a belt of Trp residues, to minimize energy costs accompanying the large perpendicular movements of the transmembrane helices. A class of Arg residues extend their side chains through the cytoplasm to exploit phospholipids as anchors for conformational switching (Norimatsu et al. 2017).

Accession Number:P04191
Protein Name:Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
Length:1001
Molecular Weight:110459.00
Species:Oryctolagus cuniculus (Rabbit) [9986]
Number of TMSs:8
Location1 / Topology2 / Orientation3: Endoplasmic reticulum membrane1 / Multi-pass membrane protein2
Substrate Mg2+, K+

Cross database links:

Structure:
1IWO   1KJU   1SU4   1T5S   1T5T   1VFP   1WPG   1XP5   2AGV   2BY4   [...more]

External Searches:

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  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MEAAHSKSTE ECLAYFGVSE TTGLTPDQVK RHLEKYGHNE LPAEEGKSLW ELVIEQFEDL 
61:	LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILIA NAIVGVWQER NAENAIEALK 
121:	EYEPEMGKVY RADRKSVQRI KARDIVPGDI VEVAVGDKVP ADIRILSIKS TTLRVDQSIL 
181:	TGESVSVIKH TEPVPDPRAV NQDKKNMLFS GTNIAAGKAL GIVATTGVST EIGKIRDQMA 
241:	ATEQDKTPLQ QKLDEFGEQL SKVISLICVA VWLINIGHFN DPVHGGSWIR GAIYYFKIAV 
301:	ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ 
361:	MSVCKMFIID KVDGDFCSLN EFSITGSTYA PEGEVLKNDK PIRSGQFDGL VELATICALC 
421:	NDSSLDFNET KGVYEKVGEA TETALTTLVE KMNVFNTEVR NLSKVERANA CNSVIRQLMK 
481:	KEFTLEFSRD RKSMSVYCSP AKSSRAAVGN KMFVKGAPEG VIDRCNYVRV GTTRVPMTGP 
541:	VKEKILSVIK EWGTGRDTLR CLALATRDTP PKREEMVLDD SSRFMEYETD LTFVGVVGML 
601:	DPPRKEVMGS IQLCRDAGIR VIMITGDNKG TAIAICRRIG IFGENEEVAD RAYTGREFDD 
661:	LPLAEQREAC RRACCFARVE PSHKSKIVEY LQSYDEITAM TGDGVNDAPA LKKAEIGIAM 
721:	GSGTAVAKTA SEMVLADDNF STIVAAVEEG RAIYNNMKQF IRYLISSNVG EVVCIFLTAA 
781:	LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMDRP PRSPKEPLIS GWLFFRYMAI 
841:	GGYVGAATVG AAAWWFMYAE DGPGVTYHQL THFMQCTEDH PHFEGLDCEI FEAPEPMTMA 
901:	LSVLVTIEMC NALNSLSENQ SLMRMPPWVN IWLLGSICLS MSLHFLILYV DPLPMIFKLK 
961:	ALDLTQWLMV LKISLPVIGL DEILKFIARN YLEDPEDERR K