ABC4_SCHPO
ID ABC4_SCHPO Reviewed; 1469 AA.
AC Q9P7V2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=ATP-binding cassette transporter abc4;
DE Short=ABC transporter abc4;
DE EC=7.6.2.2;
DE AltName: Full=ATP-energized glutathione S-conjugate pump abc4;
DE AltName: Full=Glutathione S-conjugate-transporting ATPase abc4;
GN Name=abc4 {ECO:0000312|EMBL:CAB66463.1}; ORFNames=SPAC30.04c;
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] {ECO:0000312|EMBL:CAB66463.1}
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] {ECO:0000305}
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).
CC -!- FUNCTION: Involved in detoxification of xenobiotics, and vacuolar
CC sequestration of glutathione S-conjugates. Together with abc2, required
CC for accumulation of a red pigment (ade pigment) in the vacuole of a
CC mutant affected in the adenine biosynthetic pathway.
CC {ECO:0000269|PubMed:16849797}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000250|UniProtKB:Q9C8G9};
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000255}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
CC ECO:0000269|PubMed:16849797}.
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; CAB66463.1; -; Genomic_DNA.
DR PIR; T50210; T50210.
DR RefSeq; NP_594558.1; NM_001019987.2.
DR AlphaFoldDB; Q9P7V2; -.
DR SMR; Q9P7V2; -.
DR BioGRID; 279493; 8.
DR STRING; 4896.SPAC30.04c.1; -.
DR MaxQB; Q9P7V2; -.
DR PaxDb; Q9P7V2; -.
DR PRIDE; Q9P7V2; -.
DR EnsemblFungi; SPAC30.04c.1; SPAC30.04c.1:pep; SPAC30.04c.
DR GeneID; 2543059; -.
DR KEGG; spo:SPAC30.04c; -.
DR PomBase; SPAC30.04c; abc4.
DR VEuPathDB; FungiDB:SPAC30.04c; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_6_1; -.
DR InParanoid; Q9P7V2; -.
DR OMA; FMIFTER; -.
DR PhylomeDB; Q9P7V2; -.
DR Reactome; R-SPO-114608; Platelet degranulation.
DR Reactome; R-SPO-382556; ABC-family proteins mediated transport.
DR Reactome; R-SPO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-SPO-9646399; Aggrephagy.
DR Reactome; R-SPO-9748787; Azathioprine ADME.
DR Reactome; R-SPO-9753281; Paracetamol ADME.
DR PRO; PR:Q9P7V2; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000324; C:fungal-type vacuole; IDA: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:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
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:0071996; P:glutathione transmembrane import into vacuole; IMP:PomBase.
DR GO; GO:0036246; P:phytochelatin 2 import into vacuole; IMP:PomBase.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
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; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Detoxification; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..1469
FT /note="ATP-binding cassette transporter abc4"
FT /id="PRO_0000331223"
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 55..74
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 894..914
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 936..956
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1009..1029
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1033..1053
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1065..1085
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1120..1140
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1148..1168
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 296..580
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 611..840
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 897..1176
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1214..1453
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 648..655
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1246..1253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 691
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 815
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 923
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1007
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1469 AA; 164790 MW; EE30BE28F5B9CBDA CRC64;
MENFHHRPFK GGFGVGRVPT SLYYSLSDFS LSAISIFPTH YDQPYLNEAP SWYKYSLESG
LVCLYLYLIY RWITRSFTVK QTVGSEFSGL RKAHGILLWL LSILFLGMTA FMFVNDAFPT
AFSDPPVKIC LLAYSVHLFL LHSLRMIYPR ARPTLYHAAV LLNLLLLPPI FHFYSYPFFF
VDHPPLSSYS PFLWFYFFIT IVGNFIPLFT PRVWYPLFPE DNYQPSAEQV CSMFNFACSY
GYLNPLVLTA KRRVVEVDDT PVIPDYDKNK AWTYRFERMK TPSLFITIHK IFWRQILGMG
VSSFMVSVCQ FLSPIALNRL LKHLESPSSS SVNPLVWIVL LLTGPFLTSL FTQFYLFMST
RYLARSYTTL VQQIYNKVIR SRFVQNKSGD SKVGRSNNLI STDVDDIGEI REFIHIIVRA
PVEIAGSIYL LQKLLGWSAY VGLALTVLTC SVPIVLGPLV AKLTLRANRA TDSRIELMSE
LLQSIRITKF FGWELPMLDR VKQRRQVELN RTWKLLLMEI CIQVLVESLP VFSMFATFVV
FTTIMGQTIT PSIAFTSISL FSFIRTQFSW IAYLMRQIVQ IFVSIGRVSD FLNDPDEVDP
VNTIEDTSQE IGFFNASLTW VSNPSPGDFC LRDLNIVFPR NKLSIVIGPT GSGKSSLISA
LLGELSLNKG SYNLPRSKGV SYVSQVPWLR NATIRDNILF DYPYIEERYK KVIQACGLLT
DLQSFVASDL TEIGEKGVTL SGGQKQRIAL ARAVYSPTSI VLMDDVFSAL DIHTSNWIYK
HCFQSSLMEN RTVILVTHNV HLFMDSAAFI VTVKNGSAFP VTDKSSPLLF LAEQAASASE
AAAPDLAAIP IPNEVDDAEA ADEKDGKLVE EEQRVTGDVV FSEIFSYMKH FGSGFYVAAV
LLFFVTTQAT SILIDLWVAF WTNSSVNSPD VNNNKFLFVY GTMLLAYSLL DFLRTVSYDR
GAWWASRKLH DSMLESVFGT FASWFDKTPT GRIVNRFAKD IRSIDMNLSG WLFFSINCFL
SVAGGILSVS SAMPIFMIPA VIVCLAGYYF GLLYTRAQVG VKRLISIYTS PIFSLLGESI
VGVSVIRAFN RQTIFKQMFS ERLDNLVRLQ STSYNLNRWV AVRTDGISGL VGAIAGLIAL
LQKDLSPGVV GFSLNQAVIF SSSVLLFVRS CNSLQAEMNS YERVLEYSKL PQEPAPTIAG
QVPATWPKEG DIVFNHVSVS YSAAGPTILK DVNLHINPSE KVAVVGRTGS GKSTLGLTLL
RFTHRISGEI YINGRETQSV NLNALRQRIS FIPQDPILFS GTVRSNLDPF DELEDNFLNE
ALKTSGASSM IMAHTDDQKP IHITLDTHVA SEGSNFSQGQ KQVLALARAI VRRSKIIILD
ECTASVDDAM DQKIQKTLRE AFGDATMLCI AHRLKTIVDY DKVMVLDKGV LVEYGPPAVL
YHNNGHFRRM CDGSGITFLP PETRGSKSA
