Q9UT43 (YFRD_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative phospholipid-transporting ATPase C821.13c
EC=3.6.3.1

Gene names

ORF Names:

SPAC821.13c, SPAC955.01c

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	1562 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + H2O + phospholipid(In) = ADP + phosphate + phospholipid(Out).
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. [View classification]

Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cation transport Inferred from electronic annotation. Source: InterPro phospholipid translocation Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW trans-Golgi network transport vesicle 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 – 1562	1562	Putative phospholipid-transporting ATPase C821.13c		PRO_0000046240
Regions
	Topological domain	1 – 275	275	Extracellular Potential
	Transmembrane	276 – 296	21	Helical; Potential
	Topological domain	297 – 574	278	Cytoplasmic Potential
	Transmembrane	575 – 595	21	Helical; Potential
	Topological domain	596 – 614	19	Extracellular Potential
	Transmembrane	615 – 635	21	Helical; Potential
	Topological domain	636 – 1309	674	Cytoplasmic Potential
	Transmembrane	1310 – 1330	21	Helical; Potential
	Topological domain	1331 – 1332	2	Extracellular Potential
	Transmembrane	1333 – 1353	21	Helical; Potential
	Topological domain	1354 – 1381	28	Cytoplasmic Potential
	Transmembrane	1382 – 1402	21	Helical; Potential
	Topological domain	1403 – 1414	12	Extracellular Potential
	Transmembrane	1415 – 1435	21	Helical; Potential
	Topological domain	1436 – 1443	8	Cytoplasmic Potential
	Transmembrane	1444 – 1464	21	Helical; Potential
	Topological domain	1465 – 1490	26	Extracellular Potential
	Transmembrane	1491 – 1511	21	Helical; Potential
	Topological domain	1512 – 1562	51	Cytoplasmic Potential
	Compositional bias	125 – 132	8	Poly-Lys
	Compositional bias	338 – 346	9	Poly-Arg
Sites
	Active site	684	1	4-aspartylphosphate intermediate By similarity
	Metal binding	1243	1	Magnesium By similarity
	Metal binding	1247	1	Magnesium By similarity
Amino acid modifications
	Modified residue	954	1	Phosphoserine Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9UT43 [UniParc]. Last modified May 30, 2003. Version 2. Checksum: 2B2B138BF8CB5E6E	FASTA	1,562	176,725
	10 20 30 40 50 60 MKSSGIAGDS NGFETNFLNE TTNREEDGAF NWNAADDGTN ERREDIHVRF QDSALPLGID 70 80 90 100 110 120 ENELDEIDIN GDSKKLDSVE VDESHDVNSP SDSRLKSSFK SVLELTANSM VSVLTPSTKT 130 140 150 160 170 180 EQTSKGKGKK KKAHVSFLEG PVEEIPLDDI EPTSPREASP VFNGRPPIPP EFLKSRHKEF 190 200 210 220 230 240 TIPNPLQFIS NFLSNLFSRD TRYLKSSHGR IIIINPYDDS SQIDERTGKP YMQNSIVSSR 250 260 270 280 290 300 YNKYNFVPLQ IIAQFSKTAN CYFLLIAIMQ MIPGWSTTGT YTTIIPLLIF ISIAILREGF 310 320 330 340 350 360 DNYRRYRQDR VENRIQTQVL RHVDVDPPIV EEHSSFFRRR RWRRSRSQES ASRSTIRSTD 370 380 390 400 410 420 EREPERTSED PPQLPPSPSS PSSPALSVKP NIDPQPPLYN STLTTTRSIP ANKPTFFWAS 430 440 450 460 470 480 CDRKDVRVGD IIRLTSDQTL PADVIALSSP NPNGAIYIET AALDGETSLK TRLVNSTLRS 490 500 510 520 530 540 LCKDINDLIR LSGTCTVEDP NGDLYNFNGS MKLDSIQGEI PLSNNDVLYR GSNLRNTSEL 550 560 570 580 590 600 FALVIFTGEE SKIRMNAVRN VSVKAPSMQK VTNRIVIFIF ALVVSMAIYC TAAYFVWQKK 610 620 630 640 650 660 VERKLWYLTN SKLSFVPILV SFIILYNTMV PISLYVSMEI IRVFQTFLVQ SDIDLYYPEN 670 680 690 700 710 720 DTRCEVRSSS ILEELGQVTH VFSDKTGTLT DNIMLFRNLS VGGFAWQHVG AENPKLVSTS 730 740 750 760 770 780 QKSDDLDGEA KPPQLENIQG TTIQLLQYVH DNPHTTFSKR VRIFLLNLAI CHTCLPSFDE 790 800 810 820 830 840 ENQIYKYQSI SPDELALVHA AQQLGYIVID RDIDSLTIRL HYPLDPHSHP IAKTYRILNI 850 860 870 880 890 900 IEFTSKRKCM SVIVRMPNGR ICLFCKGADS AIIKRLRLSN LAKRKDKSVT KAEQARKSIE 910 920 930 940 950 960 IDKAIIRNSQ STSRPSLTAS RPSLSRRRND YINNVTSWLD ERREKMGVVR PRASTSILET 970 980 990 1000 1010 1020 RRRPAVGRHS LAGGERLMED KKYLSKQEEA EGSIYESLNH NDAKLFENTF EHVHAFATDG 1030 1040 1050 1060 1070 1080 LRTLMYAHRF IDESEYQSWK LVNDAALNSL SNRQQLLDEA ADLIEKDLEF AGATAIEDKL 1090 1100 1110 1120 1130 1140 QVGVPESINS LFRAGIKFWM LTGDKKETAI NIGHSCGVIK EYSTVVVMGS LDGVEGSDET 1150 1160 1170 1180 1190 1200 VSGGQRLSLD RPPTNDPASL MIHQLISCMN AIHSNSLAHL VIVIDGSTLA DIENDPELFL 1210 1220 1230 1240 1250 1260 LFINTAVEAD SVICCRSSPM QKALMVQKVR NTLEKAVTLA IGDGANDIAM IQEAHVGIGI 1270 1280 1290 1300 1310 1320 AGREGLQAAR SSDFSIGRFK FLIKLLFCHG RWSYVRLSKY ILGTFYKEQF FFLMQAIMQP 1330 1340 1350 1360 1370 1380 FVGYTGQSLY ESWGLTCFNT LFSSLCVIGL GIFEKDLSAS TVIAVPELYQ KGINNEAFNW 1390 1400 1410 1420 1430 1440 RVYFGWCSIA FIQAFLVFYV TYSLFGMKEL NDNNIFAYGQ LIFTAAIFIM NFKLVFIEMQ 1450 1460 1470 1480 1490 1500 YINIISIIVL VLTSLAWFLF NIFISEHYPD KNLYLARSQF LHHFGKNPSW WLTMLFVMVC 1510 1520 1530 1540 1550 1560 ALTIDIVAQM LRRTLRPTDT DIFVEMENDA FVRSRFEQES GEFLQANAPS VDEIEQYLKS RD

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]

"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-954, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB57447.1.
PIR	T41724.
RefSeq	XP_001713045.1. XM_001712993.1.
3D structure databases
ProteinModelPortal	Q9UT43.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC821.13c.1; SPAC821.13c.1:pep; SPAC821.13c.
GeneID	3361515.
KEGG	spo:SPAC821.13c.
Organism-specific databases
GeneDB_Spombe	SPAC821.13c.
Phylogenomic databases
eggNOG	fuNOG04304.
GeneTree	EFGT00050000000755.
HOGENOM	HBG676968.
OMA	AILQMIP.
OrthoDB	EOG47M55Z.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001960-MONOMER.
Gene expression databases
ArrayExpress	Q9UT43.
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. 3 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. 2 hits. TIGR01494. ATPase_P-type. 1 hit.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

YFRD_SCHPO

Accession

Primary (citable) accession number: Q9UT43
Secondary accession number(s): Q9P6S8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2003
Last sequence update:	May 30, 2003
Last modified:	December 14, 2011
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program