ATC4_SCHPO
ID ATC4_SCHPO Reviewed; 1211 AA.
AC O14072; Q9USD0; Q9UT01;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Endoplasmic reticulum transmembrane helix translocase {ECO:0000305};
DE EC=7.4.2.- {ECO:0000250|UniProtKB:P39986};
DE AltName: Full=P-type ATPase cta4 {ECO:0000303|PubMed:12058018, ECO:0000303|PubMed:16394583};
DE AltName: Full=P5A-type ATPase cta4 {ECO:0000303|PubMed:22132152};
DE AltName: Full=Sporulation protein essential for vegetative growth 4 {ECO:0000303|PubMed:16394583};
GN Name=cta4 {ECO:0000303|PubMed:12058018, ECO:0000303|PubMed:16394583,
GN ECO:0000303|PubMed:22132152}; Synonyms=sev4 {ECO:0000303|PubMed:16394583};
GN ORFNames=SPAC2E11.07c, SPACUNK4.07c {ECO:0000312|PomBase:SPACUNK4.07c},
GN SPAPYUK71.01 {ECO:0000312|PomBase:SPACUNK4.07c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 617-809, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12058018; DOI=10.1083/jcb.200111012;
RA Okorokova Facanha A.L., Appelgren H., Tabish M., Okorokov L., Ekwall K.;
RT "The endoplasmic reticulum cation P-type ATPase Cta4p is required for
RT control of cell shape and microtubule dynamics.";
RL J. Cell Biol. 157:1029-1039(2002).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLY-615.
RX PubMed=16394583; DOI=10.1266/ggs.80.317;
RA Yoshida S.H., Nakamura T., Shimoda C.;
RT "The cation-transporting P-type ATPase Cta4 is required for assembly of the
RT forespore membrane in fission yeast.";
RL Genes Genet. Syst. 80:317-324(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Fy1180 {ECO:0000303|PubMed:22132152};
RX PubMed=22132152; DOI=10.1371/journal.pone.0027843;
RA Lustoza A.C., Palma L.M., Facanha A.R., Okorokov L.A.,
RA Okorokova-Facanha A.L.;
RT "P(5A)-type ATPase Cta4p is essential for Ca2+ transport in the endoplasmic
RT reticulum of Schizosaccharomyces pombe.";
RL PLoS ONE 6:e27843-e27843(2011).
CC -!- FUNCTION: Endoplasmic reticulum translocase required to remove
CC mitochondrial transmembrane proteins mistargeted to the endoplasmic
CC reticulum. Acts as a dislocase that mediates the ATP-dependent
CC extraction of mislocalized mitochondrial transmembrane proteins from
CC the endoplasmic reticulum membrane. Specifically binds mitochondrial
CC tail-anchored transmembrane proteins: has an atypically large
CC substrate-binding pocket that recognizes and binds moderately
CC hydrophobic transmembranes with short hydrophilic lumenal domains (By
CC similarity). Involved in controlling nuclear calcium ion levels.
CC Required for cytokinesis and stabilizing microtubules
CC (PubMed:12058018). Required for assembly of the forespore membrane
CC (PubMed:16394583). Involved in calcium transport to the endoplasmic
CC reticulum (PubMed:22132152). {ECO:0000250|UniProtKB:P39986,
CC ECO:0000269|PubMed:12058018, ECO:0000269|PubMed:16394583,
CC ECO:0000269|PubMed:22132152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-with a C-terminal TM segment(out) + ATP + H2O =
CC [protein]-with a C-terminal TM segment(in) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:66168, Rhea:RHEA-COMP:16963, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:90782, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P39986};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P39986};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12058018,
CC ECO:0000269|PubMed:16394583, ECO:0000269|PubMed:22132152}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:12058018}.
CC -!- DOMAIN: Contains a large substrate-binding pocket that recognizes
CC alpha-helical transmembranes, which alternately faces the endoplasmic
CC reticulum lumen and cytosol, while remaining accessible to the lipid
CC bilayer through a lateral opening. The translocase alternates between
CC two conformations: inward-open (E1) and outward-open (E2) states.
CC Undergoes a series of conformational changes with ATP-binding,
CC phosphorylation of the Asp active site and subsequent dephosphorylation
CC in a Post-Albers cycle (i.e., E1 -> E1-ATP -> E1P-ADP -> E1P -> E2P ->
CC E2-Pi -> E1). A substrate transmembrane helix with a short,
CC preferentially positively charged lumenal segment binds to the outward-
CC open pocket and the E2P-to-E1 transition flips the transmembrane by a
CC switch from the outward-open to inward-open conformation.
CC {ECO:0000250|UniProtKB:P39986}.
CC -!- DISRUPTION PHENOTYPE: Increased levels of intracellular calcium.
CC Impaired ATP-dependent calcium transport in endoplasmic reticulum (ER)
CC membranes, but up-regulated vacuolar calcium transport. Sensitive to ER
CC stress inducers DTT and tunicamycin, which inhibit the protein
CC disulfide bond formation and N-glycosylation, respectively, and is thus
CC sensitive to accumulation of misfolded proteins in the ER. Stimulated
CC calcineurin phosphatase activity (PubMed:22132152). Cells conjugate to
CC form zygotes at a lower efficiency than wild-type and they do not
CC sporulate (PubMed:16394583). {ECO:0000269|PubMed:16394583,
CC ECO:0000269|PubMed:22132152}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAA20137.1; -; Genomic_DNA.
DR EMBL; AB027853; BAA87157.1; -; Genomic_DNA.
DR PIR; T41702; T41702.
DR RefSeq; NP_593971.1; NM_001019398.2.
DR AlphaFoldDB; O14072; -.
DR SMR; O14072; -.
DR BioGRID; 278845; 2.
DR STRING; 4896.SPACUNK4.07c.1; -.
DR iPTMnet; O14072; -.
DR MaxQB; O14072; -.
DR PaxDb; O14072; -.
DR PRIDE; O14072; -.
DR EnsemblFungi; SPACUNK4.07c.1; SPACUNK4.07c.1:pep; SPACUNK4.07c.
DR GeneID; 2542381; -.
DR KEGG; spo:SPACUNK4.07c; -.
DR PomBase; SPACUNK4.07c; cta4.
DR VEuPathDB; FungiDB:SPACUNK4.07c; -.
DR eggNOG; KOG0209; Eukaryota.
DR HOGENOM; CLU_001828_4_1_1; -.
DR InParanoid; O14072; -.
DR OMA; RFAPKQK; -.
DR PhylomeDB; O14072; -.
DR Reactome; R-SPO-936837; Ion transport by P-type ATPases.
DR PRO; PR:O14072; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:PomBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IMP:PomBase.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0140567; F:transmembrane protein dislocase activity; ISO:PomBase.
DR GO; GO:1903515; P:calcium ion transport from cytosol to endoplasmic reticulum; IMP:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:PomBase.
DR GO; GO:0140569; P:extraction of mislocalized protein from ER membrane; ISS:PomBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006544; P-type_TPase_V.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR TIGRFAMs; TIGR01657; P-ATPase-V; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Endoplasmic reticulum; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Protein transport;
KW Reference proteome; Sporulation; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1211
FT /note="Endoplasmic reticulum transmembrane helix
FT translocase"
FT /id="PRO_0000046350"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..54
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..216
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..1057
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1058..1078
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1079..1100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1101..1121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1122..1136
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1137..1157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1158..1174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1175..1195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1196..1211
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 155..185
FT /note="A-domain; part 1"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT REGION 250..388
FT /note="A-domain; part 2"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT REGION 464..493
FT /note="P-domain; part 1"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT REGION 495..685
FT /note="N-domain"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT REGION 688..845
FT /note="P-domain; part 2"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT REGION 846..955
FT /note="Arm-like"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT REGION 956..971
FT /note="P-domain; part 3"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT ACT_SITE 485
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 485..487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 485
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 587
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 644
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 710
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 824..828
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 824
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT MUTAGEN 615
FT /note="G->E: In sev4-L5; growth defects at high and low
FT temperatures, and sensitivity to high and extremely low
FT concentrations of calcium ions. Conjugates to form zygotes
FT at a lower efficiency than wild-type. Meiotic nuclear
FT divisions proceed normally, but is not forming spores.
FT Incomplete structure alteration of the spindle pole body,
FT and hence forespore membrane formation is severely
FT impaired."
FT /evidence="ECO:0000269|PubMed:16394583"
SQ SEQUENCE 1211 AA; 136261 MW; 6FEE4228CA5A57EC CRC64;
MGSKALITSP DISSGQLYIK LPTFFHLYVW PFALFVYPYI GYVYQNKLYS EEVRYLTYIA
VGTIHALFWL AGEWNTKVYC LMTCRKTDKV EQATHILVTP SKIGESSSVE PITKLVLPDS
QTIQYSFSFQ RKRFIYEPEK GCFANITFPM DEPSTIGTLK KSTGLTNIQS EIFLYRYGKN
CFDIPIPTFG TLFKEHAVAP FFVFQIFCCV LWCLDDYWYF SLFSMFMIIA LECSVVWQRQ
RTLTEFRTMS IKPYEIQVYR NKHWFPISTE DLLPNDVVSV LHNKEDSGLP CDLLLLSGSC
VVNEAMLSGE STPLVKESIE LRPEEAVIDV DELDKNAVLF GGTRVLQVTQ SPFCKLKTPD
NGVPAIVLRT GFETSQGSLV RTMVFSSEKV TANNRESLYF ILFLLVFAIA ASGYVWHVGS
KTERSRYKLM LDCVMIITSV VPSELPMELS MAVNASLGAL SKYYIYCTEP FRIPLSGHLD
ICCFDKTGTL TEEHMVVQGI AGVNRKDPYS LEKLSDASND AILAIATAHT LVLLEQEGET
PKVVGDPMEK ATVENLGWSI EKKNFVSAPE GSVFYKGKVQ IIRNFQFSSA LKRQSSVSNV
RVSGGSFKTF VSVKGAPEVI ATMLREVPKD YEKIYKDYGR KGSRVLALGY KYFKNYIPEN
QVSDLSRESI ESDLVFAGFL IFTSPLKEDA RQTVQMLNNS SHRCMMITGD NPLTAVYVAE
QVGIVEKPTL VLDIKHENEK ILEWKSTDDT INLPMNPHKS LEASLYEKYD LCITGRALSQ
IINPDVIMSI FTHAWVYARV SPSQKEFMIS TLKHNGYITL MCGDGTNDVG ALKQAHVGVA
LLNASEEDML EMQERARNQK LMGVYEKQIQ LAKRFNLPTP PVPPALCHAF PPGPNNPHRE
KTQEGLNKVL EDLETKKASD VQLTEAEKAA ERRANLANKM FDTLANASDD EAPKLKLGDA
SVAAPFTSKL AVVSSITNIV RQGRCTLVAL VQMHKILALN CLITAYSLSV LHLDGIKFGD
TQYTISGMLM SVCFYCVSRA RPLETLSKER PQAGIFNTYI IGSVLGQFAI HIVTLIYITR
VVYLYEDPLE KVDLEETFKP SLLNTAIYLL QLIQQVSTFA INYQGRPFRE ALSENKGMYY
GLLGIAFVAI AGVTEFSPEL NAKLQLVKMA YNFQIQLLAT MVVDYAACWI IEELMKKYFR
DNKPKEIVLR N
