Reviewed, UniProtKB/Swiss-Prot Q09891 (ATCX_SCHPO)

Names and origin

Protein names

Recommended name:
    Putative phospholipid-transporting ATPase C24B11.12c
    EC=3.6.3.1

Gene names

ORF Names:

SPAC24B11.12c

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	1402 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	ATP + H2O + phospholipid(In) = ADP + phosphate + phospholipid(Out).
Subcellular location	Membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type IV subfamily.

Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane
Ligand	ATP-binding 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 phospholipid transport Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum Inferred from direct assay. Source: GeneDB_SPombe integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipid-translocating ATPase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1402	1402	Putative phospholipid-transporting ATPase C24B11.12c		PRO_0000046239
Regions
	Transmembrane	109 – 129	21	Potential
	Transmembrane	135 – 155	21	Potential
	Transmembrane	457 – 477	21	Potential
	Transmembrane	501 – 521	21	Potential
	Transmembrane	1066 – 1086	21	Potential
	Transmembrane	1101 – 1121	21	Potential
	Transmembrane	1151 – 1171	21	Potential
	Transmembrane	1193 – 1213	21	Potential
	Transmembrane	1218 – 1238	21	Potential
	Transmembrane	1260 – 1280	21	Potential
Sites
	Active site	569	1	4-aspartylphosphate intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q09891-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: E8495A7598B3020B	FASTA	1,402	159,356
	10 20 30 40 50 60 MESVEEKSKQ RRWLPNFKAL RLKVYRLADR LNIPLADAAR VELEEYDGSD PQSLRGLQKL 70 80 90 100 110 120 PRTLYFGLPL PDSELDDTGE AKRWFPRNKI RTAKYTPIDF IPKNIFLQFQ NVANLFFLFL 130 140 150 160 170 180 VILQSISIFG EQVNPGLAAV PLIVVVGITA VKDAIEDFRR TMLDIHLNNT PTLRLSHYQN 190 200 210 220 230 240 PNIRTEYISY FRRFKKRISA LFRVFLAKQE EKKRAKRLND AVPLEDMAGS ESRPSYDSIF 250 260 270 280 290 300 RESFEAKRSF EDSKGKVPLS ALDGTATILQ SRPMDIIDYE AEATGECHFK KTYWKDVRVG 310 320 330 340 350 360 DFVKVMDNDE IPADIVIINS SDPEGICYIE TKNLDGETNL KMRHALTCGK NVVDEASCER 370 380 390 400 410 420 CRFWIESEPP HANLYEYNGA CKSFVHSEAG GSDTSQTVSE PISLDSMLLR GCVLRNTKWV 430 440 450 460 470 480 IGVVVFTGDD TKIMLNSGAP PLKRSRITRN LNWNVYLNFI ILFSMCFVCA VVEGIAWRGH 490 500 510 520 530 540 SRSSYYFEFG SIGGSPAKDG VVTFFTGVIL FQNLVPISLY ISIEIVKTIQ AIFIYFDKDM 550 560 570 580 590 600 YYKKLKYACT PKSWNISDDL GQVEYIFSDK TGTLTQNVME FKKCTINGVA YGEAFTEAMA 610 620 630 640 650 660 GMAKREGKDT EELTLQKQSF IERDRMQMIS QMRNMHDNKY LVDDNLTFIS SQFVHDLAGK 670 680 690 700 710 720 AGEEQSLACY EFFLALALCH SVVADRVGDR IVYKAQSPDE AALVGTARDV GFVFLDQRRD 730 740 750 760 770 780 IMVTRALGET QRFKLMDTIE FSSARKRMSV IVKGPDNRYV LICKGADSII FERLEPNEQV 790 800 810 820 830 840 ELRKTTSEHL RIFALEGLRT LCIAKRELTE EEYYEWKEKY DIAASAIENR EEQIEEVADL 850 860 870 880 890 900 IESHLTLLGG TAIEDRLQEG VPDSIALLAQ AGIKLWVLTG DKMETAINIG FSCNLLDAGM 910 920 930 940 950 960 DMIKFDVDQE VSTPELEVIL ADYLYRYFGL SGSVEELEAA KKDHDTPSGS HALVIDGSVL 970 980 990 1000 1010 1020 KRVLDGPMRT KFLLLCKRCK AVLCCRVSPA QKADVVQLVR ESLEVMTLAI GDGANDVAMI 1030 1040 1050 1060 1070 1080 QKADIGVGIV GEEGRAAAMS ADYAIGQFRF LSKLVLVHGR WDYNRVAEMV NNFFYKSVVW 1090 1100 1110 1120 1130 1140 TFTLFWYQIY NNFDANYLFD YTYVMLFNLI FSSLPVIVMG VYDQDVNADL SLRIPQLYKR 1150 1160 1170 1180 1190 1200 GILQLNSARK IFIGYMLDGF YQSVICFFFS FLVINNVTTA AQNGRDTMAV QDLGVYVAAP 1210 1220 1230 1240 1250 1260 TIMVVDTYVI LNQSNWDVFS IGLWALSCLT FWFWTGVYSQ SLYTYEFYKS ASRIFRTPNF 1270 1280 1290 1300 1310 1320 WAVLCGTIVS CLFPKFLFMT TQKLFWPYDV DIIRESYRTK RLHELDEEEE IENAEQSPDW 1330 1340 1350 1360 1370 1380 ASSTLQVPFN ASSSSLATPK KEPLRLDTNS LTLTSSMPRS FTPSYTPSFL EGSPVFSDEI 1390 1400 LNRGEYMPHR GSISSSEQPL RP

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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAA91777.1.
PIR	S62557. T38339.
RefSeq	NP_592849.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q09891.
Genome annotation databases
GeneID	2541560.
KEGG	spo:SPAC24B11.12c.
NMPDR	fig|4896.1.peg.2819.
Organism-specific databases
GeneDB_Spombe	SPAC24B11.12c.
Phylogenomic databases
eggNOG	fuNOG04167.
HOGENOM	HBG745019.
OMA	AAMSADY.
OrthoDB	EOG9C898R.
PhylomeDB	Q09891.
Enzyme and pathway databases
BRENDA	3.6.3.1. 653.
Gene expression databases
ArrayExpress	Q09891.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR006539. ATPase_P-typ_Plipid-transl. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 1 hit.
Pfam	PF00122. E1-E2_ATPase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
TIGRFAMs	TIGR01652. ATPase-Plipid. 1 hit. TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATCX_SCHPO

Accession

Primary (citable) accession number: Q09891

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	February 9, 2010
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)