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Protein

Probable phospholipid-transporting ATPase C887.12

Gene

SPBC887.12

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids.Curated

Catalytic activityi

ATP + H2O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2).

GO - Molecular functioni

GO - Biological processi

  • phospholipid translocation Source: PomBase
  • post-Golgi vesicle-mediated transport Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-936837. Ion transport by P-type ATPases.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable phospholipid-transporting ATPase C887.12 (EC:3.6.3.1)
Gene namesi
ORF Names:SPBC887.12
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC887.12.
PomBaseiSPBC887.12.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 183183CytoplasmicBy similarityAdd
BLAST
Transmembranei184 – 20421HelicalSequence analysisAdd
BLAST
Topological domaini205 – 2084LumenalBy similarity
Transmembranei209 – 22921HelicalSequence analysisAdd
BLAST
Topological domaini230 – 406177CytoplasmicBy similarityAdd
BLAST
Transmembranei407 – 42721HelicalSequence analysisAdd
BLAST
Topological domaini428 – 45124LumenalBy similarityAdd
BLAST
Transmembranei452 – 47221HelicalSequence analysisAdd
BLAST
Topological domaini473 – 974502CytoplasmicBy similarityAdd
BLAST
Transmembranei975 – 99521HelicalSequence analysisAdd
BLAST
Topological domaini996 – 9983LumenalBy similarity
Transmembranei999 – 101921HelicalSequence analysisAdd
BLAST
Topological domaini1020 – 105132CytoplasmicBy similarityAdd
BLAST
Transmembranei1052 – 107221HelicalSequence analysisAdd
BLAST
Topological domaini1073 – 108614LumenalBy similarityAdd
BLAST
Transmembranei1087 – 110721HelicalSequence analysisAdd
BLAST
Topological domaini1108 – 11158CytoplasmicBy similarity
Transmembranei1116 – 113621HelicalSequence analysisAdd
BLAST
Topological domaini1137 – 114812LumenalBy similarityAdd
BLAST
Transmembranei1149 – 116921HelicalSequence analysisAdd
BLAST
Topological domaini1170 – 125889CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12581258Probable phospholipid-transporting ATPase C887.12PRO_0000314112Add
BLAST

Proteomic databases

MaxQBiO94296.

Interactioni

Protein-protein interaction databases

MINTiMINT-4682969.

Structurei

3D structure databases

ProteinModelPortaliO94296.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000202528.
InParanoidiO94296.
KOiK14802.
OMAiQESARCA.
OrthoDBiEOG7FR7QR.
PhylomeDBiO94296.

Family and domain databases

Gene3Di2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006539. P-type_ATPase_IV.
IPR032631. P-type_ATPase_N.
IPR001757. P_typ_ATPase.
IPR032630. P_typ_ATPase_c.
[Graphical view]
PANTHERiPTHR24092. PTHR24092. 1 hit.
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF16212. PhoLip_ATPase_C. 1 hit.
PF16209. PhoLip_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O94296-1 [UniParc]FASTAAdd to basket

« Hide

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

RGAYGEMR
Length:1,258
Mass (Da):142,379
Last modified:May 1, 1999 - v1
Checksum:i9128B7BFD692B022
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA21897.1.
PIRiT40737.
RefSeqiNP_596486.1. NM_001022406.2.

Genome annotation databases

EnsemblFungiiSPBC887.12.1; SPBC887.12.1:pep; SPBC887.12.
GeneIDi2541239.
KEGGispo:SPBC887.12.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA21897.1.
PIRiT40737.
RefSeqiNP_596486.1. NM_001022406.2.

3D structure databases

ProteinModelPortaliO94296.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4682969.

Proteomic databases

MaxQBiO94296.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC887.12.1; SPBC887.12.1:pep; SPBC887.12.
GeneIDi2541239.
KEGGispo:SPBC887.12.

Organism-specific databases

EuPathDBiFungiDB:SPBC887.12.
PomBaseiSPBC887.12.

Phylogenomic databases

HOGENOMiHOG000202528.
InParanoidiO94296.
KOiK14802.
OMAiQESARCA.
OrthoDBiEOG7FR7QR.
PhylomeDBiO94296.

Enzyme and pathway databases

ReactomeiR-SPO-936837. Ion transport by P-type ATPases.

Miscellaneous databases

PROiO94296.

Family and domain databases

Gene3Di2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006539. P-type_ATPase_IV.
IPR032631. P-type_ATPase_N.
IPR001757. P_typ_ATPase.
IPR032630. P_typ_ATPase_c.
[Graphical view]
PANTHERiPTHR24092. PTHR24092. 1 hit.
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF16212. PhoLip_ATPase_C. 1 hit.
PF16209. PhoLip_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiYOOC_SCHPO
AccessioniPrimary (citable) accession number: O94296
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 1999
Last modified: June 8, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.