ABC3_SCHPO
ID ABC3_SCHPO Reviewed; 1465 AA.
AC Q9P5N0; Q9UU44;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Vacuolar heme ABC transmembrane exporter abc3 {ECO:0000312|PomBase:SPBC359.05};
GN Name=abc3 {ECO:0000312|PomBase:SPBC359.05};
GN ORFNames=SPBC359.05 {ECO:0000312|PomBase:SPBC359.05};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 207-348, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP SUBCELLULAR LOCATION, AND FUNCTION.
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 [4]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19915076; DOI=10.1128/ec.00262-09;
RA Pouliot B., Jbel M., Mercier A., Labbe S.;
RT "abc3+ encodes an iron-regulated vacuolar ABC-type transporter in
RT Schizosaccharomyces pombe.";
RL Eukaryot. Cell 9:59-73(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-151 AND CYS-152.
RX PubMed=28193844; DOI=10.1074/jbc.m117.776807;
RA Mourer T., Normant V., Labbe S.;
RT "Heme Assimilation in Schizosaccharomyces pombe Requires Cell-surface-
RT anchored Protein Shu1 and Vacuolar Transporter Abc3.";
RL J. Biol. Chem. 292:4898-4912(2017).
CC -!- FUNCTION: Iron-regulated vacuolar transporter that mobilizes stored
CC heme from the vacuole to the cytosol in response to iron deficiency.
CC {ECO:0000269|PubMed:16849797, ECO:0000269|PubMed:19915076,
CC ECO:0000269|PubMed:28193844}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16849797, ECO:0000269|PubMed:19915076,
CC ECO:0000269|PubMed:28193844}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16849797, ECO:0000269|PubMed:19915076,
CC ECO:0000269|PubMed:28193844}.
CC -!- INDUCTION: Induced under conditions of iron deficiency and negatively
CC regulated by iron through fep1. {ECO:0000269|PubMed:19915076}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAB91574.1; -; Genomic_DNA.
DR EMBL; AB027821; BAA87125.1; -; Genomic_DNA.
DR RefSeq; NP_595055.1; NM_001020961.2.
DR AlphaFoldDB; Q9P5N0; -.
DR SMR; Q9P5N0; -.
DR BioGRID; 277453; 6.
DR STRING; 4896.SPBC359.05.1; -.
DR TCDB; 3.A.1.208.28; the atp-binding cassette (abc) superfamily.
DR MaxQB; Q9P5N0; -.
DR PaxDb; Q9P5N0; -.
DR EnsemblFungi; SPBC359.05.1; SPBC359.05.1:pep; SPBC359.05.
DR GeneID; 2540937; -.
DR KEGG; spo:SPBC359.05; -.
DR PomBase; SPBC359.05; abc3.
DR VEuPathDB; FungiDB:SPBC359.05; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q9P5N0; -.
DR OMA; EQESCPD; -.
DR PhylomeDB; Q9P5N0; -.
DR Reactome; R-SPO-189483; Heme degradation.
DR Reactome; R-SPO-382556; ABC-family proteins mediated transport.
DR Reactome; R-SPO-9749641; Aspirin ADME.
DR Reactome; R-SPO-9753281; Paracetamol ADME.
DR Reactome; R-SPO-9754706; Atorvastatin ADME.
DR PRO; PR:Q9P5N0; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IDA:PomBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015439; F:ABC-type heme transporter activity; IMP:PomBase.
DR GO; GO:0015440; F:ABC-type peptide transporter activity; IBA:GO_Central.
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:0020037; F:heme binding; IDA:PomBase.
DR GO; GO:0140357; P:heme export from vacuole to cytoplasm; IMP:PomBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd18580; ABC_6TM_ABCC_D2; 1.
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; IPR044726; ABCC_6TM_D2.
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 1: Evidence at protein level;
KW ATP-binding; Heme; Iron; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Vacuole.
FT CHAIN 1..1465
FT /note="Vacuolar heme ABC transmembrane exporter abc3"
FT /id="PRO_0000093471"
FT TOPO_DOM 1..8
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 30..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 64..69
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 91..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 119..129
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 151..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 257..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 313..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 384..394
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 416..480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 502..511
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 533..899
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 900..920
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 921..939
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 940..960
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 961..1033
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1034..1054
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1055..1465
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 250..539
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 575..804
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 903..1189
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1226..1460
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 805..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 151..152
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:28193844"
FT BINDING 614..621
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1260..1267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 151
FT /note="P->A: Abolishes heme binding and heme export from
FT vacuole; when associated with A-152."
FT /evidence="ECO:0000269|PubMed:28193844"
FT MUTAGEN 152
FT /note="C->A: Abolishes heme binding and heme export from
FT vacuole; when associated with A-151."
FT /evidence="ECO:0000269|PubMed:28193844"
FT CONFLICT 207
FT /note="L -> V (in Ref. 2; BAA87125)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1465 AA; 166613 MW; B15F1579B0895332 CRC64;
MITANKGLSL VLLIPNLFAL VSGGLQYVFD VRRRIFRPHF SQFWTIWMKF FSIALVIITQ
IYVGYKTKNI GWNFFSVVTY CFVLFLQFAE QSTLRVPMAS LLIFWLLKVV TSLLILLFSP
YIAITSMARL LTLITLFCSL VCFISEVYVP PCNRVWYSDD TNEVEEKGIR PSEVRYANIF
SKLSFSWISS FIKFGYTNYL KESDVWLLPP DERSGNLIIG FEDWWIYHSK NKRRSLFLWK
LLFFNHWKLV ALITITKLIQ DVLAFVQPTL IQKTILFISS YTSPNPESPS RGFIIAILVL
VANFLQTLLL QQYNQLIMLL GMRWKTELLA SIYRKSLLLS SSARQNRSIG DIINYMAVDT
QKISDLPIYL FIIVSGPFQI ALALSNLYHL MGYSAFTGVA ASVILFPCNI IVANVYKKFQ
SILMKNKDSR SKLMTEIINN IRSIKLYAWE TPFLQKLLHI RNTKELSMLK KIGFITAIGD
FAWIFTTIIV TTVAFGAFII FHGKTQALTA DIVFPAVSLF NLLQFPLAML PTVISSLLEA
SVSVSRIYEF LIAQELDYNG VQRFPATEIP HEICLEIKSG TFSWSKKTLK QQVTPTLRQI
NFVAKNGELT CIFGKVGAGK SSLLEACMGN MYKNSGSVFQ CGSLAYAAQQ PWIFDATIRE
NILFGSEFDP ELYEKTIHAC CLKRDFEIFT EGDQTEVGQK GASLSGGQKS RISLARAIYS
QADIYLLDDV LSSVDQHVSR DLIKNLFGPE GFLRTHCVVL TTNSLNVLKE ADSIYILSNG
KIVEKGNYEH LFVSTNSELK QQLSEFNDEK DTQPLPEHTT SYPSTQISLA PSIHVEGLET
YSSSERKDSS NKYKSRKRNP IRQKVTEDDK GKCVAQTDEL VQRGKVKWHV YWMYFKSCSI
GLILLYFFFI ISGIMMNVAT NVWLKHWSEE NGKSSSELNP SPYFYLGIYL FFGFLSCAFI
SSSSLTMTVL CGIRSGRYLH DSMLKTILRA PMGFFETTSS GRILNRFSND VYKVDEVVSL
TFMFFFRNSI QVLFILGVIC YSAPLSLLLI VPLFFLYLYN RAYYVRTSRE LKRLDNVTRS
PLYAHVQESL SGLSTIRAYG MQETFVEEND LRIDTNHRVW FMFFSSSRWQ AIRVECIGDL
IIFCTAFYGI LSAIKGSPNP GLVGFSLSYA IQITQGLSFI VQQSVDAENN TVSVERILEY
INVKSEAPEI IPENRPPCEW PTDGAVSFNH YSAKYREDLS FALNNINIEI SPREKIGIVG
RTGAGKSTLA MALFRIIEPT EGKIEIDNED ITKFGLYDLR SRLSIIPQES QIFEGNIREN
LDPNHRLTDK KIWEVLEIAS LKNCISQLED GLYSRVAEGG ANFSSGQRQL ICLARVLLTS
TRILLLDEAT ASVHAETDAI VQQTIRKRFK DRTILTVAHR INTVMDSDRI LVLDHGKVVE
FDATKKLLEN KDSMFYSLAK ESGLI
