MDL1_SCHPO
ID MDL1_SCHPO Reviewed; 726 AA.
AC Q9Y7M7;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=ATP-dependent permease MDL1, mitochondrial;
DE AltName: Full=ABC transporter mdl1;
DE Flags: Precursor;
GN Name=mdl1; ORFNames=SPBC9B6.09c;
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 SUBCELLULAR LOCATION.
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Mediates export of peptides generated upon proteolysis of
CC mitochondrial inner membrane proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:16849797}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
CC ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:16849797}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Mitochondrial peptide exporter (TC 3.A.1.212) subfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAB42370.1; -; Genomic_DNA.
DR PIR; T40790; T40790.
DR RefSeq; NP_595751.1; NM_001021651.2.
DR AlphaFoldDB; Q9Y7M7; -.
DR SMR; Q9Y7M7; -.
DR BioGRID; 277798; 4.
DR STRING; 4896.SPBC9B6.09c.1; -.
DR MaxQB; Q9Y7M7; -.
DR PaxDb; Q9Y7M7; -.
DR PRIDE; Q9Y7M7; -.
DR EnsemblFungi; SPBC9B6.09c.1; SPBC9B6.09c.1:pep; SPBC9B6.09c.
DR GeneID; 2541285; -.
DR KEGG; spo:SPBC9B6.09c; -.
DR PomBase; SPBC9B6.09c; mdl1.
DR VEuPathDB; FungiDB:SPBC9B6.09c; -.
DR eggNOG; KOG0058; Eukaryota.
DR HOGENOM; CLU_000604_84_3_1; -.
DR InParanoid; Q9Y7M7; -.
DR OMA; WGTYLVK; -.
DR PhylomeDB; Q9Y7M7; -.
DR Reactome; R-SPO-1369007; Mitochondrial ABC transporters.
DR Reactome; R-SPO-159418; Recycling of bile acids and salts.
DR Reactome; R-SPO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-SPO-382556; ABC-family proteins mediated transport.
DR Reactome; R-SPO-9754706; Atorvastatin ADME.
DR PRO; PR:Q9Y7M7; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0015421; F:ABC-type oligopeptide transporter activity; ISO: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:0090374; P:oligopeptide export from mitochondrion; ISO:PomBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
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 InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..112
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 113..726
FT /note="ATP-dependent permease MDL1, mitochondrial"
FT /id="PRO_0000093470"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 158..447
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 482..719
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 517..524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 668
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 726 AA; 79020 MW; 203473D0B9585BCC CRC64;
MDPIRFGLSR VPFAHCYNKR VIFRANYLVP LTWLKNNVAY KSTNTLLLPT PNAEYYSTSK
LSSQVNVSLN SLSQKASSGS KIYPFKNSFP LPFSRSILPI RSLAFLKLCV RHNSTVPSKD
EQAQDISKIN TNGTLQTPNK KVNVFRLFTL ARGQGWNFFI AGSLLLVSSG VTMSIPYIVG
KILDAGSSGD SSVTHIMGIP SGTFYIGLLG LFFLGSACNF GRIITLRLLS ERIVSRLRAR
LFAKCMSLDG AFFDFHKHGD LISRLTTDSS IVGKSLSMYL SDGLRSSVSA IAGIGMMLYV
SMRLTGYMSL IVPPIALGAF FYGEYVRKLS RTTQDALGDL TRVSEEKLAN VRTTQAFLGE
RQEVNRYNDY IRNLFVLAKR EAFASGIFFG STGFLGNATV IAILALGGRM VAAGDITVGQ
LSSFLLYTVY AGGSIVGLSG CFTDIMKGLG AASRLFELLD AKPKIAPTVG IPVPVTVGKA
ILSFRNVGFA YPTRPSASIF DNLSFDIHPG TNVAIVAPSG GGKSTISQLL LRFYAPSSGK
ILADGVDIST YNVHQWRSHF GLVGQEPVLF SGTIGENIAY GKSNASQEEI EDAAKRANCS
FVLSFPEKWS TQVGTRGLQL SGGQKQRIAI ARALLRNPAF LILDEATSAL DGEAEVMVDK
TIQSLMHNRS MTTITIAHKL ATIRRADQII VVGDGKVLEQ GSFERLSRPG TNFYKLMRWQ
LGKVEP
