Reviewed, UniProtKB/Swiss-Prot Q9HDW7 (ATC2_SCHPO)

Names and origin

Protein names

Recommended name:
    Calcium-transporting ATPase 2
    EC=3.6.3.8

Gene names

Name:	pmc1
ORF Names:	SPAPB2B4.04c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	1292 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports the calcium to the vacuole and participates in the control of the cytosolic free calcium. Ref.3
Catalytic activity	ATP + H2O + Ca2+(Cis) = ADP + phosphate + Ca2+(Trans).
Subcellular location	Vacuole membrane; Multi-pass membrane protein Ref.3.
Sequence similarities	Belongs to the cation transport ATPase (P-type) family.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Membrane Vacuole
Domain	Transmembrane
Ligand	ATP-binding Calcium Magnesium Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro calcium ion transport Inferred from electronic annotation. Source: UniProtKB-KW cellular calcium ion homeostasis Ref.3 Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	fungal-type vacuole membrane Ref.3 Inferred from direct assay. Source: GeneDB_SPombe integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred by curator. Source: GeneDB_SPombe calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-transporting ATPase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1292	1292	Calcium-transporting ATPase 2		PRO_0000362141
Regions
	Topological domain	1 – 236	236	Cytoplasmic Potential
	Transmembrane	237 – 257	21	Potential
	Topological domain	258 – 273	16	Extracellular Potential
	Transmembrane	274 – 294	21	Potential
	Topological domain	295 – 448	154	Cytoplasmic Potential
	Transmembrane	449 – 469	21	Potential
	Topological domain	470 – 488	19	Extracellular Potential
	Transmembrane	489 – 509	21	Potential
	Topological domain	510 – 938	429	Cytoplasmic Potential
	Transmembrane	939 – 959	21	Potential
	Topological domain	960 – 966	7	Extracellular Potential
	Transmembrane	967 – 987	21	Potential
	Topological domain	988 – 1016	29	Cytoplasmic Potential
	Transmembrane	1017 – 1037	21	Potential
	Topological domain	1038 – 1084	47	Extracellular Potential
	Transmembrane	1085 – 1105	21	Potential
	Topological domain	1106 – 1115	10	Cytoplasmic Potential
	Transmembrane	1116 – 1136	21	Potential
	Topological domain	1137 – 1292	156	Extracellular Potential
	Compositional bias	6 – 9	4	Poly-Asp
	Compositional bias	10 – 105	96	Ser-rich
Sites
	Active site	545	1	4-aspartylphosphate intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9HDW7-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 1499E90144A2B07B	FASTA	1,292	142,235
	10 20 30 40 50 60 MPTYNDDDDS SRPPSVHSER NQKPSSSQFL GVPSSNYNQR ENSSRSGSST ISREPSSSGT 70 80 90 100 110 120 MYPMASRDSM KESYDKNKGT PPDYTSYVSH SDAEPEQASS KSSTSIEDLL HTEYDDAPFA 130 140 150 160 170 180 FSIPLLQRLQ DPKNTSLLHA IHGLKGLCKG LKVDPSTGIS THEPHYADKL QMSDILNDDS 190 200 210 220 230 240 NPKLVVHLDR IRSQDNNPEA KVSHDSDRVK YYGKNVLPEH DSKGLIRLML EAFKDKVLIL 250 260 270 280 290 300 LSIAAVVSLA LGLYQTFGQP PTLDPITGKP EPRVEWVEGV AIMAAIVIVV TVGGVNDWQK 310 320 330 340 350 360 ELQFKKLNAK VSNFDVQVLR DGAVHSTSVF DLVVGDVLFV EAGDVVPVDG VLIESNNLVL 370 380 390 400 410 420 DESAMTGETD NIKKVDANTA IERTSPDVEY RKNADPYLIS GTTILEGNGK LLVTAVGVNS 430 440 450 460 470 480 FNGRTTMAMR TEGQATPLQL RLSRVADAIA KLGGAASALL FIVLLIEFLV RLKSNDSSSK 490 500 510 520 530 540 NKGQEFLQIL IVSVTLLVVA VPEGLPLAVT LALAFATNRM QKDNNLVRHL QACETMGTAT 550 560 570 580 590 600 NICSDKTGTL TQNRMTVVAG GFGTDVLFFD HNDETPTNVD QGSDSSKFED AGASAFAFKR 610 620 630 640 650 660 LSPELRDLTL YSIAVNSTCR QLFEDNSDTP RFIGSKTETA LLDMSVKELG LTNVDSMRSS 670 680 690 700 710 720 VDIKQFFSFS SDRKASGAIF EYKDKYYFVV KGMPERVLQQ STSVITNGSL DEVEDMHSHA 730 740 750 760 770 780 DYFKEMITGY AKRSLRTLGL CYRVFDSWPP KDIPTNDEDS SNPLKWEDAF TDMTFLGFFG 790 800 810 820 830 840 IMDPIRPDVP LAVKVCQGAG VTVRMVTGDN IVTAKAIASQ CGIYTEDGIS MEGPEFRSLS 850 860 870 880 890 900 DEKRLEILPK LDVLARSSPL DKQLLIEGLQ KLGNVVAVTG DGTNDAPALK KANVGFSMGK 910 920 930 940 950 960 SGTEVAKEAS DIILMDDNFS SIVKAIAWGR TVNDAVKKFL QFQITVNITA VFLTIISAVA 970 980 990 1000 1010 1020 STDQSSVLTA VQLLWVNLIM DTLAALALAT DPPTPEVLKR KPEKPGASLF TFDMWKMIIC 1030 1040 1050 1060 1070 1080 QSMYQLAVTL VLHFAGNSIF HYPSNTADMN TIVFNTFVWL QLFNEINNRR LDNKLNIFER 1090 1100 1110 1120 1130 1140 INHNFLFIAI FVIVAGIQVI IVFFGGAAFS VKRIDGKGWA ISIVFGVISI PLGALIRCVP 1150 1160 1170 1180 1190 1200 NNFLRKVLPV KTIDTVFSWI LNPRFRSKRR STDHDVESLS LIPYEPTSPN EVIDSIRHSL 1210 1220 1230 1240 1250 1260 GFVQRIRGGR IRHLLNNSKF DKQMEALPER LRPRVKQRFM KIRSPSVSSA TSVALMIPIS 1270 1280 1290 TLVSEASGRL GGHDIWISHN RQALDKKSSN VH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"An inventory of the P-type ATPases in the fission yeast Schizosaccharomyces pombe." Okorokova-Facanha A.L., Okorokov L.A., Ekwall K. Curr. Genet. 43:273-280(2003) [PubMed: 12707717] [Abstract] Cited for: IDENTIFICATION.
[3]	"Schizosaccharomyces pombe Pmr1p is essential for cell wall integrity and is required for polarized cell growth and cytokinesis." Cortes J.C.G., Katoh-Fukui R., Moto K., Ribas J.C., Ishiguro J. Eukaryot. Cell 3:1124-1135(2004) [PubMed: 15470240] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAC21470.1.
RefSeq	NP_593890.1.
3D structure databases
HSSP	HSSP built from PDB template 1WPG based on UniProtKB P04191.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9HDW7.
Genome annotation databases
GeneID	2543477.
GenomeReviews	Gene locus pmc1 in contig CU329670_GR.
KEGG	spo:SPAPB2B4.04c.
NMPDR	fig|4896.1.peg.3860.
Organism-specific databases
GeneDB_Spombe	SPAPB2B4.04c.
Phylogenomic databases
eggNOG	fuNOG06319.
HOGENOM	HBG456486.
OMA	EADESSI.
PhylomeDB	Q9HDW7.
Gene expression databases
ArrayExpress	Q9HDW7.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR006408. ATPase_P-typ_Ca-transp_PMCA. IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR005834. Dehalogen-like_hydro. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 1 hit.
Pfam	PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01517. ATPase-IIB_Ca. 1 hit. TIGR01494. ATPase_P-type. 3 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATC2_SCHPO

Accession

Primary (citable) accession number: Q9HDW7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	March 1, 2001
Last modified:	February 9, 2010
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)