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Protein

ATP-binding cassette transporter abc2

Gene

abc2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in 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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi631 – 6388ATP 1PROSITE-ProRule annotation
Nucleotide bindingi1273 – 12808ATP 2PROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • phytochelatin transmembrane transporter ATPase activity Source: PomBase

GO - Biological processi

  • cellular detoxification of cadmium ion Source: PomBase
  • glutathione transmembrane import into vacuole Source: PomBase
  • phytochelatin 2 import into vacuole Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Detoxification, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-2142850. Hyaluronan biosynthesis and export.
R-SPO-382556. ABC-family proteins mediated transport.

Protein family/group databases

TCDBi3.A.1.208.16. the atp-binding cassette (abc) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-binding cassette transporter abc2 (EC:3.6.3.-)
Short name:
ABC transporter abc2
Alternative name(s):
ATP-energized glutathione S-conjugate pump abc2
Glutathione S-conjugate-transporting ATPase abc2
Gene namesi
Name:abc2
ORF Names:SPAC3F10.11c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

PomBaseiSPAC3F10.11c. abc2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2525VacuolarBy similarityAdd
BLAST
Transmembranei26 – 4621Helical; Name=1PROSITE-ProRule annotationAdd
BLAST
Topological domaini47 – 6519CytoplasmicBy similarityAdd
BLAST
Transmembranei66 – 8520Helical; Name=2PROSITE-ProRule annotationAdd
BLAST
Topological domaini86 – 905VacuolarBy similarity
Transmembranei91 – 10414Helical; Name=3PROSITE-ProRule annotationAdd
BLAST
Topological domaini105 – 11612CytoplasmicBy similarityAdd
BLAST
Transmembranei117 – 13721Helical; Name=4PROSITE-ProRule annotationAdd
BLAST
Topological domaini138 – 15417VacuolarBy similarityAdd
BLAST
Transmembranei155 – 17521Helical; Name=5PROSITE-ProRule annotationAdd
BLAST
Topological domaini176 – 25984CytoplasmicBy similarityAdd
BLAST
Transmembranei260 – 28021Helical; Name=6PROSITE-ProRule annotationAdd
BLAST
Topological domaini281 – 31030VacuolarBy similarityAdd
BLAST
Transmembranei311 – 33121Helical; Name=7PROSITE-ProRule annotationAdd
BLAST
Topological domaini332 – 38756CytoplasmicBy similarityAdd
BLAST
Transmembranei388 – 40821Helical; Name=8PROSITE-ProRule annotationAdd
BLAST
Topological domaini409 – 4113VacuolarBy similarity
Transmembranei412 – 43221Helical; Name=9PROSITE-ProRule annotationAdd
BLAST
Topological domaini433 – 49563CytoplasmicBy similarityAdd
BLAST
Transmembranei496 – 51621Helical; Name=10PROSITE-ProRule annotationAdd
BLAST
Topological domaini517 – 53923VacuolarBy similarityAdd
BLAST
Transmembranei540 – 56021Helical; Name=11PROSITE-ProRule annotationAdd
BLAST
Topological domaini561 – 910350CytoplasmicBy similarityAdd
BLAST
Transmembranei911 – 93121Helical; Name=12PROSITE-ProRule annotationAdd
BLAST
Topological domaini932 – 96837VacuolarBy similarityAdd
BLAST
Transmembranei969 – 99022Helical; Name=13PROSITE-ProRule annotationAdd
BLAST
Topological domaini991 – 103343CytoplasmicBy similarityAdd
BLAST
Transmembranei1034 – 105421Helical; Name=14PROSITE-ProRule annotationAdd
BLAST
Topological domaini1055 – 10551VacuolarBy similarity
Transmembranei1056 – 107621Helical; Name=15PROSITE-ProRule annotationAdd
BLAST
Topological domaini1077 – 114771CytoplasmicBy similarityAdd
BLAST
Transmembranei1148 – 116821Helical; Name=16PROSITE-ProRule annotationAdd
BLAST
Topological domaini1169 – 11724VacuolarBy similarity
Transmembranei1173 – 119321Helical; Name=17PROSITE-ProRule annotationAdd
BLAST
Topological domaini1194 – 1478285CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • fungal-type vacuole membrane Source: PomBase
  • Golgi apparatus Source: PomBase
  • integral component of membrane Source: UniProtKB-KW
  • vacuolar membrane Source: PomBase
  • vacuole Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Disruption phenotypei

Cells lacking both abc2 and abc4 show sensitivity to cycloheximide (CHX) and 4-nitroquinoline oxide (4-NQO), and decreased accumulation of monochlorobimane-glutathione (MCIB-GS).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14781478ATP-binding cassette transporter abc2PRO_0000093468Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence analysis
Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence analysis
Modified residuei839 – 8391Phosphoserine1 Publication
Modified residuei843 – 8431Phosphoserine1 Publication
Modified residuei863 – 8631Phosphoserine1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ10185.

PTM databases

iPTMnetiQ10185.

Interactioni

Protein-protein interaction databases

BioGridi279622. 20 interactions.
MINTiMINT-4697599.

Structurei

3D structure databases

ProteinModelPortaliQ10185.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini268 – 557290ABC transmembrane type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini593 – 821229ABC transporter 1PROSITE-ProRule annotationAdd
BLAST
Domaini918 – 1202285ABC transmembrane type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini1239 – 1473235ABC transporter 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 ABC transmembrane type-1 domains.PROSITE-ProRule annotation
Contains 2 ABC transporter domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoidiQ10185.
OMAiLENGVIM.
OrthoDBiEOG75XGV5.
PhylomeDBiQ10185.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00664. ABC_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF90123. SSF90123. 2 hits.
PROSITEiPS50929. ABC_TM1F. 2 hits.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q10185-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLEQDLDPF VGGNWMNSAY KGFTFLSATW LAPNIYLLIS GCLQYFYEVR
60 70 80 90 100
KRSHYFHFRR FWTIWLKSLV IMVLLFTHIY DCYKTNESVW NVLSIITYFL
110 120 130 140 150
ALFLHVVEQP TLRIPMASLL MFWLFKFLAS ALVLLLRPNY TMFPMLNVVP
160 170 180 190 200
SITFFCSLVC LLAEIYVPPA NRVWYPDDAA ELEETGLRPS RFTYANIFSR
210 220 230 240 250
ISFGWLSPLM KFGYRNYLTE SDAWSLPPAE RSSNLTIVFE KNWISHAKKK
260 270 280 290 300
KSSLYMWGVL FLNHWKLTVV IIVLKLVQDV VAFIQPNLIR KIVIFVSSYS
310 320 330 340 350
SEHPQPPQVG FSLAIAMFLT NVVQTALLQQ YFQLGMVLGM RWRSELITAI
360 370 380 390 400
YRKSLRLSSA ARQSRSVGDI VNYMSVDTQK VCDLTMFLFV IVSGPFQIVL
410 420 430 440 450
ALTNLYHLVG YGALSGAFVT FLLFPCNVVI ASIFKRFQNR QMKNKDARSQ
460 470 480 490 500
FMTEIINNIR SIKLYAWENI FLQKLLQLRN TRELRMLKKI GIVNTIGNFT
510 520 530 540 550
WLFAPILVSA ATFGTFIVLY GKTRVLSVDI VFACLSLFNL LQFPLTMLPI
560 570 580 590 600
VVSSVLEASV AISRIYGFLT AGELDSNAVQ RYPANKEPSG VCLEIKKGTF
610 620 630 640 650
SWSGPGQNAA EPTLRDIDFV ARRGELCCIV GKVGMGKSSL LEACLGNMQK
660 670 680 690 700
HSGSVFRCGS IAYAAQQPWI LNATIQENIL FGLELDPEFY EKTIRACCLL
710 720 730 740 750
RDFEILADGD QTEVGEKGIS LSGGQKARIS LARAVYSRSD IYLLDDILSA
760 770 780 790 800
VDQHVNRDLV RNLLGSKGLL RSRCVILSTN SLTVLKEASM IYMLRNGKII
810 820 830 840 850
ESGSFTQLSS SPDSQLFQLL SEFSKKDTAS STGADTPLSR SQSVITSSTD
860 870 880 890 900
VTSSASRSSD TVSNYPKATI KGTGRIRKRL TDEDNVKATG QAAEKMERGK
910 920 930 940 950
VKWKVYWTYF KACSLFLIFL YFLFIIGGIG MNVGTNVWLK HWSEVNTQLG
960 970 980 990 1000
YNPKPYFYLG IYTLFGLLSC ALISLSSLTI TVFCAIKSCR YLHDSMVKAV
1010 1020 1030 1040 1050
LRAPMSFFET TPTGRILNRF SSDVYRVDEV ISRVFMFFFR NLFQIVFVLA
1060 1070 1080 1090 1100
VICYSSPMFM ILIVPLFFLY RYNQVYYTQT SRELKRLDSV TRSPLYAHFQ
1110 1120 1130 1140 1150
ESLGGLSTIR AYDMEDTFIS ENDIRVDTNH RIWFLYFSSN RWQAIRVEAI
1160 1170 1180 1190 1200
GALVVFSSAF FGVLSAVRGN PNSGLVGLSL SYAVQITQSL TFVVRQSVDV
1210 1220 1230 1240 1250
ETNIVSVERM LEYIGLPSEA PSIIPDHRPP EGWPSHGAIK FDHYSVRYRE
1260 1270 1280 1290 1300
NLPLVLNDIS VNIKPQEKIG IVGRTGAGKS TLTLALFRLI EPTSGDIQLD
1310 1320 1330 1340 1350
DINITSIGLH DLRSRLAIIP QENQAFEGTI RENLDPNANA TDEEIWHALE
1360 1370 1380 1390 1400
AASLKQFIQT LDGGLYSRVT EGGANLSSGQ RQLMCLTRAL LTPTRVLLLD
1410 1420 1430 1440 1450
EATAAVDVET DAIVQRTIRE RFNDRTILTI AHRINTVMDS NRILVLDHGK
1460 1470
VVEFDSTKKL LENKASLFYS LAKESGLI
Length:1,478
Mass (Da):166,938
Last modified:October 1, 1996 - v1
Checksum:i6C59F43105EB7187
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1287 – 12871F → L in BAA13892 (PubMed:9501991).Curated
Sequence conflicti1301 – 13033DIN → YIH in BAA13892 (PubMed:9501991).Curated
Sequence conflicti1311 – 13111D → H in BAA13892 (PubMed:9501991).Curated
Sequence conflicti1467 – 14671L → V in BAA13892 (PubMed:9501991).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA93309.3.
D89231 mRNA. Translation: BAA13892.1.
PIRiT38712.
RefSeqiNP_593943.3. NM_001019371.3.

Genome annotation databases

EnsemblFungiiSPAC3F10.11c.1; SPAC3F10.11c.1:pep; SPAC3F10.11c.
GeneIDi2543193.
KEGGispo:SPAC3F10.11c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA93309.3.
D89231 mRNA. Translation: BAA13892.1.
PIRiT38712.
RefSeqiNP_593943.3. NM_001019371.3.

3D structure databases

ProteinModelPortaliQ10185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279622. 20 interactions.
MINTiMINT-4697599.

Protein family/group databases

TCDBi3.A.1.208.16. the atp-binding cassette (abc) superfamily.

PTM databases

iPTMnetiQ10185.

Proteomic databases

MaxQBiQ10185.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC3F10.11c.1; SPAC3F10.11c.1:pep; SPAC3F10.11c.
GeneIDi2543193.
KEGGispo:SPAC3F10.11c.

Organism-specific databases

PomBaseiSPAC3F10.11c. abc2.

Phylogenomic databases

InParanoidiQ10185.
OMAiLENGVIM.
OrthoDBiEOG75XGV5.
PhylomeDBiQ10185.

Enzyme and pathway databases

ReactomeiR-SPO-2142850. Hyaluronan biosynthesis and export.
R-SPO-382556. ABC-family proteins mediated transport.

Miscellaneous databases

NextBioi20804216.
PROiQ10185.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00664. ABC_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF90123. SSF90123. 2 hits.
PROSITEiPS50929. ABC_TM1F. 2 hits.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "Comparative functional genomics of the fission yeasts."
    Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
    , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
    Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL.
  3. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1043-1478.
    Strain: PR745.
  4. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-839; SER-843 AND SER-863, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiABC2_SCHPO
AccessioniPrimary (citable) accession number: Q10185
Secondary accession number(s): P78928
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 17, 2016
This is version 128 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.