Reviewed, UniProtKB/Swiss-Prot O94296 (YOOC_SCHPO)

Names and origin

Protein names

Recommended name:
    Probable phospholipid-transporting ATPase C887.12
    EC=3.6.3.1

Gene names

ORF Names:

SPBC887.12

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	1258 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids Potential.
Catalytic activity	ATP + H2O + phospholipid(In) = ADP + phosphate + phospholipid(Out).
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus › trans-Golgi network membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type IV subfamily.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Golgi apparatus Membrane
Domain	Transmembrane
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro phospholipid translocation Traceable author statement. Source: GeneDB_SPombe
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred by curator. Source: GeneDB_SPombe 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 – 1258	1258	Probable phospholipid-transporting ATPase C887.12		PRO_0000314112
Regions
	Topological domain	1 – 183	183	Cytoplasmic By similarity
	Transmembrane	184 – 204	21	Potential
	Topological domain	205 – 208	4	Lumenal By similarity
	Transmembrane	209 – 229	21	Potential
	Topological domain	230 – 406	177	Cytoplasmic By similarity
	Transmembrane	407 – 427	21	Potential
	Topological domain	428 – 451	24	Lumenal By similarity
	Transmembrane	452 – 472	21	Potential
	Topological domain	473 – 974	502	Cytoplasmic By similarity
	Transmembrane	975 – 995	21	Potential
	Topological domain	996 – 998	3	Lumenal By similarity
	Transmembrane	999 – 1019	21	Potential
	Topological domain	1020 – 1051	32	Cytoplasmic By similarity
	Transmembrane	1052 – 1072	21	Potential
	Topological domain	1073 – 1086	14	Lumenal By similarity
	Transmembrane	1087 – 1107	21	Potential
	Topological domain	1108 – 1115	8	Cytoplasmic By similarity
	Transmembrane	1116 – 1136	21	Potential
	Topological domain	1137 – 1148	12	Lumenal By similarity
	Transmembrane	1149 – 1169	21	Potential
	Topological domain	1170 – 1258	89	Cytoplasmic By similarity

Sequences

	Sequence		Length	Mass (Da)
	O94296-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 9128B7BFD692B022	FASTA	1,258	142,379
	10 20 30 40 50 60 MARDVDNKQN AKRISRDEDE DEFAGESMVG RTLDNPFLGE DEFEDIFGSE SQYISSSGQN 70 80 90 100 110 120 STNPFLADTR IENSPLGSES KANQLNKQGT NVNHIEIPLR DFNDPTQPES FLPPPKNTFT 130 140 150 160 170 180 SRIKKIKNLF KKEKKQVKPE DLGPRQIILN DYSANHFLHN AVSTCKYSAF TFLPKFLKEQ 190 200 210 220 230 240 FSKYANLFFL FTAVVQQIPG ITPVNRYTTI GPMLIVLSVS GIKEIMEDIK RKKQDQELNE 250 260 270 280 290 300 SPCYVLQGTG FVEKQWKDVV VGDIVKIVSE TFFPADLVLL SSSEPEGLCY IETANLDGET 310 320 330 340 350 360 NLKIKQALPE TAGLLKPVEL GQLSGEVKSE QPNNNLYTFD ATLKLLPSDR ELPLSPDQLL 370 380 390 400 410 420 LRGAQLRNTP WVYGIVVFTG HESKLMKNTT ETPIKRTSVE KQVNSQILFL LCIFVFLCFA 430 440 450 460 470 480 SSLGALIHRS VYGSALSYVK YTSNRAGMFF KGLLTFWILY SNLVPISLFV TFELVRYIQA 490 500 510 520 530 540 QLISSDLDMY NEETDTPAAC RTSSLVEELG QVGYIFSDKT GTLTRNQMEF RQCTIAGVAY 550 560 570 580 590 600 ADVIPEDRQF TSEDLDSDMY IYDFDTLKEN LKHSENASLI HQFLLVLSIC HTVIPEYDES 610 620 630 640 650 660 TNSIKYQASS PDEGALVKGA ASIGYKFLAR KPHLVTVSIF GKDESYELLH ICEFNSTRKR 670 680 690 700 710 720 MSIVFRCPDG KIRLYVKGAD TVIMERLASD NPYLQTTIHH LEDYATVGLR TLCIAMREVP 730 740 750 760 770 780 EDEYQRWSTV FETAASSLVD RAQKLMDAAE EIEKDLILLG ATAIEDRLQD GVPDTISTLQ 790 800 810 820 830 840 TAGIKIWVLT GDRQETAINI GMSCKLIDED MGLVIVNEET KEATAESVMA KLSSIYRNEA 850 860 870 880 890 900 TTGNVESMAL VIDGVSLTYA LDFSLERRFF ELASLCRAVI CCRVSPLQKA LIVKMVKRNT 910 920 930 940 950 960 GEVLLAIGDG ANDVPMIQAA HVGVGISGME GLQAVRSSDF SISQFCYLKK LLLVHGSWCY 970 980 990 1000 1010 1020 QRLSKLILYS FYKNIALYMT QFWYAFCNAF SGQVIFESWS ISLYNVLFTV LPPVVIGIFD 1030 1040 1050 1060 1070 1080 QFVSAGQLFQ YPQLYQLGQR SEFFNLKRFW SWITNGFYHS LLLFLCSIAV FYYDGPNKDG 1090 1100 1110 1120 1130 1140 LASGHWVWGT TLYAAILATV LGKAALISNH WTQYTVIATL GSFLLWIVFM PIYAVAAPAI 1150 1160 1170 1180 1190 1200 GFSKEYYGII PHLYGNLKFW ASLLVLPTIA LMRDFVWKYS SRMYYPEEYH YVQEIQKYNV 1210 1220 1230 1240 1250 TDYRPRIVGF HKAIRKIRQM QRMRKQRGYA FSQGEEDQSR ILDAYDTTHT RGAYGEMR

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]

"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329671 Genomic DNA. Translation: CAA21897.1.
PIR	T40737.
RefSeq	NP_596486.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2541239.
KEGG	spo:SPBC887.12.
NMPDR	fig|4896.1.peg.2352.
Organism-specific databases
GeneDB_Spombe	SPBC887.12.
Phylogenomic databases
OMA	O94296. RDFVWKY.
Enzyme and pathway databases
BRENDA	3.6.3.1. 653.
Gene expression databases
ArrayExpress	O94296.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-reg. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_phosphor_site. IPR006539. ATPase_P-typ_Plipid-transl. IPR005834. Dehalogen-like_hydro. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 1 hit.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
TIGRFAMs	TIGR01652. ATPase-Plipid. 1 hit. TIGR01494. ATPase_P-type. 4 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

YOOC_SCHPO

Accession

Primary (citable) accession number: O94296

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)