O36028 (ATCZ_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative phospholipid-transporting ATPase C4F10.16c
EC=3.6.3.1

Gene names

ORF Names:

SPAC4F10.16c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1367 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the hydrolysis of ATP coupled with the transport of phospholipids By similarity.
Catalytic activity	ATP + H2O + phospholipid(In) = ADP + phosphate + phospholipid(Out).
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Potential Ref.2.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. [View classification]

Ontologies

Keywords
Biological process	Lipid transport Transport
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cation transport Inferred from electronic annotation. Source: InterPro endocytosis Inferred from sequence or structural similarity. Source: GeneDB_Spombe intracellular protein transport Inferred from sequence or structural similarity. Source: GeneDB_Spombe phospholipid translocation Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from sequence or structural similarity. Source: GeneDB_Spombe
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: InterPro phospholipid-translocating ATPase activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1367	1367	Putative phospholipid-transporting ATPase C4F10.16c		PRO_0000343137
Regions
	Topological domain	1 – 154	154	Cytoplasmic Potential
	Transmembrane	155 – 172	18	Helical; Potential
	Topological domain	173 – 177	5	Lumenal Potential
	Transmembrane	178 – 197	20	Helical; Potential
	Topological domain	198 – 482	285	Cytoplasmic Potential
	Transmembrane	483 – 503	21	Helical; Potential
	Topological domain	504 – 531	28	Lumenal Potential
	Transmembrane	532 – 552	21	Helical; Potential
	Topological domain	553 – 1091	539	Cytoplasmic Potential
	Transmembrane	1092 – 1112	21	Helical; Potential
	Topological domain	1113 – 1124	12	Lumenal Potential
	Transmembrane	1125 – 1145	21	Helical; Potential
	Topological domain	1146 – 1174	29	Cytoplasmic Potential
	Transmembrane	1175 – 1197	23	Helical; Potential
	Topological domain	1198 – 1212	15	Lumenal Potential
	Transmembrane	1213 – 1233	21	Helical; Potential
	Topological domain	1234 – 1240	7	Cytoplasmic Potential
	Transmembrane	1241 – 1261	21	Helical; Potential
	Topological domain	1262 – 1276	15	Lumenal Potential
	Transmembrane	1277 – 1297	21	Helical; Potential
	Topological domain	1298 – 1367	70	Cytoplasmic Potential
Sites
	Active site	600	1	4-aspartylphosphate intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O36028 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 4DCFD8A7479465EB	FASTA	1,367	154,282
	10 20 30 40 50 60 MPSLINFDAI SSLKSSLHGL SICAFNHLHH VPQHNGSLAH EGPTNQTDYS SRHHESQFSQ 70 80 90 100 110 120 EAHAEQRSRD DEEANSFEGS CNNSDQSWTS RVTSKKNEAG TESGDASVRR IYVTSIPEEH 130 140 150 160 170 180 RHLPSQWFPS NKIRTTKYTP VSFIPKNLWN QFKNIANAFF LFVTLLQCIP LFCPEHLGLS 190 200 210 220 230 240 FIPLSVILLT TAIKDGIEDY RRCVLDKKFN NTLTWKLVGF NNANALGEHI GLWRKLKKFI 250 260 270 280 290 300 SHTVADMSYC LKNSGISSGL ATLTVDNISH RHSLESDSAF TLSSVSQDSL EIHEIGNSGP 310 320 330 340 350 360 SNSFSVIQEQ STGSSNAKFE RVCRKSLLVG DIVKVLADEA IPADLLILST ENSNGVCYVE 370 380 390 400 410 420 TKNLDGETNL KDKYALCSTK CCKSEYRCSA ASFWVECEQP HADLYSLNGV VKAPGAVQSP 430 440 450 460 470 480 SESTNGRKIH EEPFSISNVL LCGCTLRNSK WVIGLVLYTG SETRIQKNRG LTPSKRSRIT 490 500 510 520 530 540 RDLNWTIILN FLLLFAMCLF SGVLRSIYSA QNNSARVFEL SKNSNTAPAH GIISIFTSLI 550 560 570 580 590 600 LFQNLVPISL YITMDIVRSI QSYFIFSDRE MYDEKLDCPC SPKSWNISDD LGQIEYIFSD 610 620 630 640 650 660 KTGTLTQNIM SFKKCSINGI RYGKSHNEDT CIKKRRNLNY NENLSCKVDL DKKKMLETLS 670 680 690 700 710 720 LSDSPNPESI TFISSKFVDH LQSNENYIQT EACFEFFKAL ALCHSVVTDV QDETLIYNAQ 730 740 750 760 770 780 SPDEEALVKV ARDFGFTLLN TKNRRYTIRI RGENKNFRVL DIIPFTSTRK RMSVIIRDED 790 800 810 820 830 840 GIIHLICKGA DTVIFPRLSS GQNNIIEKTK KHLASFSSEG FRTLCIARRT IDKQDYLEWK 850 860 870 880 890 900 VNFNEANSAI HERNEKVSKV SEMIEQELEL LGGTAIEDKL QENVPETIAL LAIAGIKLWV 910 920 930 940 950 960 LTGDKVETAI NIGYSCNLLD PNMTIFRIDA NSFGALEEVE AFIRNTLCFN FGYMGTDEEF 970 980 990 1000 1010 1020 RFLLKDHSPP SPKHAIVIDG DALNFVLSEQ VSFLFLMLCK QCKTVLCCRV SPSQKAAVVA 1030 1040 1050 1060 1070 1080 LVKKSLNVVT LAIGDGANDV SMIQEADVGV GIKGVEGQAA SMSADYAIGQ FSFLGRLLLV 1090 1100 1110 1120 1130 1140 HGRWDYKRMS QMISFFFYKN VIWTFILFWY QFYNEFDGNY IFDYTYVMLF NLLFTSLPVI 1150 1160 1170 1180 1190 1200 IAGCFDQDVD ASVSMKNPSL YQRGILGLEW NGKRFWSYML DGIYQSLVCF GVALFVFKFG 1210 1220 1230 1240 1250 1260 DFVSWTGRNI ECIEDIGLFI SSPTIFVINI FILMNQERLN LISLITWMFS IGVFWIWTFI 1270 1280 1290 1300 1310 1320 YSEVGPSYAF HKSASRTCQT FGFWCVTVLT IALCLLPRFS YICLQKLFYP RDIDLLRRRL 1330 1340 1350 1360 CAKSDDETSS SSSFATDIEM CEQCNDPLSS KKNSGIVTSV SFDDSNK

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: 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: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB11719.1.
PIR	T38820.
RefSeq	NP_594759.1. NM_001020186.1.
3D structure databases
ProteinModelPortal	O36028.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC4F10.16c.1; SPAC4F10.16c.1:pep; SPAC4F10.16c.
GeneID	2543523.
KEGG	spo:SPAC4F10.16c.
NMPDR	fig|4896.1.peg.4729.
Organism-specific databases
GeneDB_Spombe	SPAC4F10.16c.
Phylogenomic databases
eggNOG	fuNOG04167.
GeneTree	EFGT00050000000755.
HOGENOM	HBG745019.
OMA	ANSAIHE.
OrthoDB	EOG44BF99.
Gene expression databases
ArrayExpress	O36028.
Family and domain databases
InterPro	IPR023306. ATPase_cation_domN. IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR006539. ATPase_P-typ_Plipid-transl. IPR023214. HAD-like_dom. [Graphical view]
Gene3D	G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 3 hits. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 2 hits. G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KO	K01530.
Pfam	PF00122. E1-E2_ATPase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SUPFAM	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01652. ATPase-Plipid. 1 hit. TIGR01494. ATPase_P-type. 1 hit.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATCZ_SCHPO

Accession

Primary (citable) accession number: O36028

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	January 1, 1998
Last modified:	December 14, 2011
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program