ABC2_SCHPO
ID ABC2_SCHPO Reviewed; 1478 AA.
AC Q10185; P78928;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=ATP-binding cassette transporter abc2;
DE Short=ABC transporter abc2;
DE EC=7.-.-.-;
DE AltName: Full=ATP-energized glutathione S-conjugate pump abc2;
DE AltName: Full=Glutathione S-conjugate-transporting ATPase abc2;
GN Name=abc2; ORFNames=SPAC3F10.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1043-1478.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16849797; DOI=10.1099/mic.0.28952-0;
RA Iwaki T., Giga-Hama Y., Takegawa K.;
RT "A survey of all 11 ABC transporters in fission yeast: two novel ABC
RT transporters are required for red pigment accumulation in a
RT Schizosaccharomyces pombe adenine biosynthetic mutant.";
RL Microbiology 152:2309-2321(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-839; SER-843 AND SER-863, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Involved in vacuolar sequestration of glutathione S-
CC conjugates. Together with abc4, required for accumulation of a red
CC pigment (ade pigment) in the vacuole of a mutant affected in the
CC adenine biosynthetic pathway. {ECO:0000269|PubMed:16849797}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking both abc2 and abc4 show sensitivity
CC to cycloheximide (CHX) and 4-nitroquinoline oxide (4-NQO), and
CC decreased accumulation of monochlorobimane-glutathione (MCIB-GS).
CC {ECO:0000269|PubMed:16849797}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAA93309.3; -; Genomic_DNA.
DR EMBL; D89231; BAA13892.1; -; mRNA.
DR PIR; T38712; T38712.
DR RefSeq; NP_593943.3; NM_001019371.3.
DR AlphaFoldDB; Q10185; -.
DR SMR; Q10185; -.
DR BioGRID; 279622; 21.
DR STRING; 4896.SPAC3F10.11c.1; -.
DR TCDB; 3.A.1.208.16; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q10185; -.
DR MaxQB; Q10185; -.
DR PaxDb; Q10185; -.
DR PRIDE; Q10185; -.
DR EnsemblFungi; SPAC3F10.11c.1; SPAC3F10.11c.1:pep; SPAC3F10.11c.
DR GeneID; 2543193; -.
DR KEGG; spo:SPAC3F10.11c; -.
DR PomBase; SPAC3F10.11c; abc2.
DR VEuPathDB; FungiDB:SPAC3F10.11c; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q10185; -.
DR OMA; IRYDFTP; -.
DR PhylomeDB; Q10185; -.
DR Reactome; R-SPO-189483; Heme degradation.
DR Reactome; R-SPO-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR Reactome; R-SPO-382556; ABC-family proteins mediated transport.
DR Reactome; R-SPO-9707564; Cytoprotection by HMOX1.
DR Reactome; R-SPO-9749641; Aspirin ADME.
DR Reactome; R-SPO-9753281; Paracetamol ADME.
DR Reactome; R-SPO-9754706; Atorvastatin ADME.
DR Reactome; R-SPO-9758890; Transport of RCbl within the body.
DR PRO; PR:Q10185; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015440; F:ABC-type peptide transporter activity; IBA:GO_Central.
DR GO; GO:0044604; F:ABC-type phytochelatin transporter activity; IMP:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0098849; P:cellular detoxification of cadmium ion; IMP:PomBase.
DR GO; GO:0071996; P:glutathione transmembrane import into vacuole; IMP:PomBase.
DR GO; GO:0036246; P:phytochelatin 2 import into vacuole; IMP:PomBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Detoxification; Glycoprotein; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..1478
FT /note="ATP-binding cassette transporter abc2"
FT /id="PRO_0000093468"
FT TOPO_DOM 1..25
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 26..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 47..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 66..85
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 86..90
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 91..104
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 105..116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 117..137
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 138..154
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 155..175
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 176..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 260..280
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 281..310
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 311..331
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 332..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 388..408
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 409..411
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 412..432
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 433..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 496..516
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 517..539
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 540..560
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 561..910
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 911..931
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 932..968
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 969..990
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 991..1033
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1034..1054
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1055
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 1056..1076
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1077..1147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1148..1168
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1169..1172
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 1173..1193
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1194..1478
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 268..557
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 593..821
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 918..1202
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1239..1473
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 828..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 631..638
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1273..1280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 839
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 843
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 1287
FT /note="F -> L (in Ref. 3; BAA13892)"
FT /evidence="ECO:0000305"
FT CONFLICT 1301..1303
FT /note="DIN -> YIH (in Ref. 3; BAA13892)"
FT /evidence="ECO:0000305"
FT CONFLICT 1311
FT /note="D -> H (in Ref. 3; BAA13892)"
FT /evidence="ECO:0000305"
FT CONFLICT 1467
FT /note="L -> V (in Ref. 3; BAA13892)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1478 AA; 166938 MW; 6C59F43105EB7187 CRC64;
MVLEQDLDPF VGGNWMNSAY KGFTFLSATW LAPNIYLLIS GCLQYFYEVR KRSHYFHFRR
FWTIWLKSLV IMVLLFTHIY DCYKTNESVW NVLSIITYFL ALFLHVVEQP TLRIPMASLL
MFWLFKFLAS ALVLLLRPNY TMFPMLNVVP SITFFCSLVC LLAEIYVPPA NRVWYPDDAA
ELEETGLRPS RFTYANIFSR ISFGWLSPLM KFGYRNYLTE SDAWSLPPAE RSSNLTIVFE
KNWISHAKKK KSSLYMWGVL FLNHWKLTVV IIVLKLVQDV VAFIQPNLIR KIVIFVSSYS
SEHPQPPQVG FSLAIAMFLT NVVQTALLQQ YFQLGMVLGM RWRSELITAI YRKSLRLSSA
ARQSRSVGDI VNYMSVDTQK VCDLTMFLFV IVSGPFQIVL ALTNLYHLVG YGALSGAFVT
FLLFPCNVVI ASIFKRFQNR QMKNKDARSQ FMTEIINNIR SIKLYAWENI FLQKLLQLRN
TRELRMLKKI GIVNTIGNFT WLFAPILVSA ATFGTFIVLY GKTRVLSVDI VFACLSLFNL
LQFPLTMLPI VVSSVLEASV AISRIYGFLT AGELDSNAVQ RYPANKEPSG VCLEIKKGTF
SWSGPGQNAA EPTLRDIDFV ARRGELCCIV GKVGMGKSSL LEACLGNMQK HSGSVFRCGS
IAYAAQQPWI LNATIQENIL FGLELDPEFY EKTIRACCLL RDFEILADGD QTEVGEKGIS
LSGGQKARIS LARAVYSRSD IYLLDDILSA VDQHVNRDLV RNLLGSKGLL RSRCVILSTN
SLTVLKEASM IYMLRNGKII ESGSFTQLSS SPDSQLFQLL SEFSKKDTAS STGADTPLSR
SQSVITSSTD VTSSASRSSD TVSNYPKATI KGTGRIRKRL TDEDNVKATG QAAEKMERGK
VKWKVYWTYF KACSLFLIFL YFLFIIGGIG MNVGTNVWLK HWSEVNTQLG YNPKPYFYLG
IYTLFGLLSC ALISLSSLTI TVFCAIKSCR YLHDSMVKAV LRAPMSFFET TPTGRILNRF
SSDVYRVDEV ISRVFMFFFR NLFQIVFVLA VICYSSPMFM ILIVPLFFLY RYNQVYYTQT
SRELKRLDSV TRSPLYAHFQ ESLGGLSTIR AYDMEDTFIS ENDIRVDTNH RIWFLYFSSN
RWQAIRVEAI GALVVFSSAF FGVLSAVRGN PNSGLVGLSL SYAVQITQSL TFVVRQSVDV
ETNIVSVERM LEYIGLPSEA PSIIPDHRPP EGWPSHGAIK FDHYSVRYRE NLPLVLNDIS
VNIKPQEKIG IVGRTGAGKS TLTLALFRLI EPTSGDIQLD DINITSIGLH DLRSRLAIIP
QENQAFEGTI RENLDPNANA TDEEIWHALE AASLKQFIQT LDGGLYSRVT EGGANLSSGQ
RQLMCLTRAL LTPTRVLLLD EATAAVDVET DAIVQRTIRE RFNDRTILTI AHRINTVMDS
NRILVLDHGK VVEFDSTKKL LENKASLFYS LAKESGLI
