Reviewed, UniProtKB/Swiss-Prot Q10185 (ABC2_SCHPO)

Names and origin

Protein names

Recommended name:
    ATP-binding cassette transporter abc2
      Short name=ABC transporter abc2
    EC=3.6.3.44
Alternative name(s):
    Glutathione S-conjugate-transporting ATPase abc2
    ATP-energized glutathione S-conjugate pump abc2

Gene names

Name:	abc2
ORF Names:	SPAC3F10.11c

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	1478 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in detoxification of xenobiotics, and vacuolar sequestration of glutathione S-conjugates. Together with abc4, required for accumulation of a red pigment (ade pigment) in the vacuole of a mutant affected in the adenine biosynthetic pathway.
Catalytic activity	ATP + H(2)O + xenobiotic(In) = ADP + phosphate + xenobiotic(Out).
Subcellular location	Vacuole membrane; Multi-pass membrane proteinPotential.
Miscellaneous	Double disruption mutant, where both abc2 and abc4 are deleted, causes sensitivity to cycloheximide (CHX) and 4-nitroquinoline oxide (4-NQO), and decreased accumulation of monochlorobimane-glutathione (MCIB-GS).
Sequence similarities	Belongs to the ABC transporter family. Conjugate transporter (TC 3.A.1.208) subfamily. [View classification] Contains 2 ABC transmembrane type-1 domains. Contains 2 ABC transporter domains.

Ontologies

Keywords
Biological process	Detoxification Transport
Cellular component	Membrane Vacuole
Domain	Repeat Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	response to toxin Inferred from electronic annotation. Source: UniProtKB-KW vacuolar transport Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	Golgi apparatus Inferred from direct assay. Source: GeneDB_SPombe integral to membrane Inferred from electronic annotation. Source: InterPro vacuolar membrane Ref.2 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro glutathione S-conjugate-exporting ATPase activity Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe xenobiotic-transporting 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 – 1478	1478	ATP-binding cassette transporter abc2		PRO_0000093468
Regions
	Topological domain	1 – 25	25	Vacuolar By similarity
	Transmembrane	26 – 46	21	1 By similarity
	Topological domain	47 – 65	19	Cytoplasmic By similarity
	Transmembrane	66 – 85	20	2 By similarity
	Topological domain	86 – 90	5	Vacuolar By similarity
	Transmembrane	91 – 104	14	3 By similarity
	Topological domain	105 – 116	12	Cytoplasmic By similarity
	Transmembrane	117 – 137	21	4 By similarity
	Topological domain	138 – 154	17	Vacuolar By similarity
	Transmembrane	155 – 175	21	5 By similarity
	Topological domain	176 – 259	84	Cytoplasmic By similarity
	Transmembrane	260 – 280	21	6 By similarity
	Topological domain	281 – 310	30	Vacuolar By similarity
	Transmembrane	311 – 331	21	7 By similarity
	Topological domain	332 – 387	56	Cytoplasmic By similarity
	Transmembrane	388 – 408	21	8 By similarity
	Topological domain	409 – 411	3	Vacuolar By similarity
	Transmembrane	412 – 432	21	9 By similarity
	Topological domain	433 – 495	63	Cytoplasmic By similarity
	Transmembrane	496 – 516	21	10 By similarity
	Topological domain	517 – 539	23	Vacuolar By similarity
	Transmembrane	540 – 560	21	11 By similarity
	Topological domain	561 – 910	350	Cytoplasmic By similarity
	Transmembrane	911 – 931	21	12 By similarity
	Topological domain	932 – 968	37	Vacuolar By similarity
	Transmembrane	969 – 990	22	13 By similarity
	Topological domain	991 – 1033	43	Cytoplasmic By similarity
	Transmembrane	1034 – 1054	21	14 By similarity
	Topological domain	1055	1	Vacuolar By similarity
	Transmembrane	1056 – 1076	21	15 By similarity
	Topological domain	1077 – 1147	71	Cytoplasmic By similarity
	Transmembrane	1148 – 1168	21	16 By similarity
	Topological domain	1169 – 1172	4	Vacuolar By similarity
	Transmembrane	1173 – 1193	21	17 By similarity
	Topological domain	1194 – 1478	285	Cytoplasmic By similarity
	Domain	268 – 557	290	ABC transmembrane type-1 1
	Domain	593 – 821	229	ABC transporter 1
	Domain	918 – 1202	285	ABC transmembrane type-1 2
	Domain	1239 – 1473	235	ABC transporter 2
	Nucleotide binding	631 – 638	8	ATP 1 Potential
	Nucleotide binding	1273 – 1280	8	ATP 2 Potential
Amino acid modifications
	Modified residue	839	1	Phosphoserine
	Modified residue	843	1	Phosphoserine
	Modified residue	863	1	Phosphoserine
	Glycosylation	86	1	N-linked (GlcNAc...) Potential
	Glycosylation	139	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q10185-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 6C59F43105EB7187	FASTA	1,478	166,938
	10 20 30 40 50 60 MVLEQDLDPF VGGNWMNSAY KGFTFLSATW LAPNIYLLIS GCLQYFYEVR KRSHYFHFRR 70 80 90 100 110 120 FWTIWLKSLV IMVLLFTHIY DCYKTNESVW NVLSIITYFL ALFLHVVEQP TLRIPMASLL 130 140 150 160 170 180 MFWLFKFLAS ALVLLLRPNY TMFPMLNVVP SITFFCSLVC LLAEIYVPPA NRVWYPDDAA 190 200 210 220 230 240 ELEETGLRPS RFTYANIFSR ISFGWLSPLM KFGYRNYLTE SDAWSLPPAE RSSNLTIVFE 250 260 270 280 290 300 KNWISHAKKK KSSLYMWGVL FLNHWKLTVV IIVLKLVQDV VAFIQPNLIR KIVIFVSSYS 310 320 330 340 350 360 SEHPQPPQVG FSLAIAMFLT NVVQTALLQQ YFQLGMVLGM RWRSELITAI YRKSLRLSSA 370 380 390 400 410 420 ARQSRSVGDI VNYMSVDTQK VCDLTMFLFV IVSGPFQIVL ALTNLYHLVG YGALSGAFVT 430 440 450 460 470 480 FLLFPCNVVI ASIFKRFQNR QMKNKDARSQ FMTEIINNIR SIKLYAWENI FLQKLLQLRN 490 500 510 520 530 540 TRELRMLKKI GIVNTIGNFT WLFAPILVSA ATFGTFIVLY GKTRVLSVDI VFACLSLFNL 550 560 570 580 590 600 LQFPLTMLPI VVSSVLEASV AISRIYGFLT AGELDSNAVQ RYPANKEPSG VCLEIKKGTF 610 620 630 640 650 660 SWSGPGQNAA EPTLRDIDFV ARRGELCCIV GKVGMGKSSL LEACLGNMQK HSGSVFRCGS 670 680 690 700 710 720 IAYAAQQPWI LNATIQENIL FGLELDPEFY EKTIRACCLL RDFEILADGD QTEVGEKGIS 730 740 750 760 770 780 LSGGQKARIS LARAVYSRSD IYLLDDILSA VDQHVNRDLV RNLLGSKGLL RSRCVILSTN 790 800 810 820 830 840 SLTVLKEASM IYMLRNGKII ESGSFTQLSS SPDSQLFQLL SEFSKKDTAS STGADTPLSR 850 860 870 880 890 900 SQSVITSSTD VTSSASRSSD TVSNYPKATI KGTGRIRKRL TDEDNVKATG QAAEKMERGK 910 920 930 940 950 960 VKWKVYWTYF KACSLFLIFL YFLFIIGGIG MNVGTNVWLK HWSEVNTQLG YNPKPYFYLG 970 980 990 1000 1010 1020 IYTLFGLLSC ALISLSSLTI TVFCAIKSCR YLHDSMVKAV LRAPMSFFET TPTGRILNRF 1030 1040 1050 1060 1070 1080 SSDVYRVDEV ISRVFMFFFR NLFQIVFVLA VICYSSPMFM ILIVPLFFLY RYNQVYYTQT 1090 1100 1110 1120 1130 1140 SRELKRLDSV TRSPLYAHFQ ESLGGLSTIR AYDMEDTFIS ENDIRVDTNH RIWFLYFSSN 1150 1160 1170 1180 1190 1200 RWQAIRVEAI GALVVFSSAF FGVLSAVRGN PNSGLVGLSL SYAVQITQSL TFVVRQSVDV 1210 1220 1230 1240 1250 1260 ETNIVSVERM LEYIGLPSEA PSIIPDHRPP EGWPSHGAIK FDHYSVRYRE NLPLVLNDIS 1270 1280 1290 1300 1310 1320 VNIKPQEKIG IVGRTGAGKS TLTLALFRLI EPTSGDIQLD DINITSIGLH DLRSRLAIIP 1330 1340 1350 1360 1370 1380 QENQAFEGTI RENLDPNANA TDEEIWHALE AASLKQFIQT LDGGLYSRVT EGGANLSSGQ 1390 1400 1410 1420 1430 1440 RQLMCLTRAL LTPTRVLLLD EATAAVDVET DAIVQRTIRE RFNDRTILTI AHRINTVMDS 1450 1460 1470 NRILVLDHGK VVEFDSTKKL LENKASLFYS LAKESGLI

References

	« Hide 'large scale' referencesShow 'large scale' 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]	"A survey of all 11 ABC transporters in fission yeast: two novel ABC transporters are required for red pigment accumulation in a Schizosaccharomyces pombe adenine biosynthetic mutant." Iwaki T., Giga-Hama Y., Takegawa K. Microbiology 152:2309-2321(2006) [PubMed: 16849797] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION MUTANT.
[3]	"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-839; SER-843 AND SER-863, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAA93309.1.
PIR	T38712.
RefSeq	NP_593943.2.
3D structure databases
HSSP	HSSP built from PDB template 1MT0 based on UniProtKB P08716.
ModBase	Search...
Genome annotation databases
GeneID	2543193.
KEGG	spo:SPAC3F10.11c.
NMPDR	fig|4896.1.peg.3913.
Organism-specific databases
GeneDB_Spombe	SPAC3F10.11c.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001584-MON.
Gene expression databases
ArrayExpress	Q10185.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase_core. IPR011527. ABC_TM_1. IPR001140. ABC_TM_transpt. IPR003439. ABC_transporter-like. [Graphical view]
Pfam	PF00664. ABC_membrane. 2 hits. PF00005. ABC_tran. 2 hits. [Graphical view]
ProDom	PD000006. ABC_transporter. 2 hits. [Graphical view] [Entries sharing at least one domain]
SMART	SM00382. AAA. 2 hits. [Graphical view]
PROSITE	PS50929. ABC_TM1F. 2 hits. PS00211. ABC_TRANSPORTER_1. 1 hit. PS50893. ABC_TRANSPORTER_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ABC2_SCHPO

Accession

Primary (citable) accession number: Q10185

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 25, 2008
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)