Basic Information
Name | ATP-dependent permease MDL2, mitochondrial (Multidrug resistance-like protein 2) |
Uniprot ID | P33311 |
Systematic gene name | YPL270W |
Standard gene name | MDL2 |
Gene names | MDL2 SSH1 YPL270W |
Description from SGD | YPL270W MDL2 SGDID:S000006191, Chr XVI from 30482-32803, Genome Release 64-3-1, Verified ORF, "Mitochondrial inner membrane half-type ABC transporter; required for respiratory growth at high temperature; localizes to vacuole membrane in response to H2O2; similar to human TAP1 and TAP2 implicated in bare lymphocyte syndrome and Wegener-like granulomatosis" |
Protein length | 773 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MLNGRLPLLR LGICRNMLSR PRLAKLPSIR FRSLVTPSSS QLIPLSRLCL
RSPAVGKSLI LQSFRCNSSK TVPETSLPSA SPISKGSARS AHAKEQSKTD
DYKDIIRLFM LAKRDWKLLL TAILLLTISC SIGMSIPKVI GIVLDTLKTS
SGSDFFDLKI PIFSLPLYEF LSFFTVALLI GCAANFGRFI LLRILSERVV
ARLRANVIKK TLHQDAEFFD NHKVGDLISR LGSDAYVVSR SMTQKVSDGV
KALICGVVGV GMMCSLSPQL SILLLFFTPP VLFSASVFGK QIRNTSKDLQ
EATGQLTRVA EEQLSGIKTV QSFVAEGNEL SRYNVAIRDI FQVGKTAAFT
NAKFFTTTSL LGDLSFLTVL AYGSYLVLQS QLSIGDLTAF MLYTEYTGNA
VFGLSTFYSE IMQGAGAASR LFELTDRKPS ISPTVGHKYK PDRGVIEFKD
VSFSYPTRPS VQIFKNLNFK IAPGSSVCIV GPSGRGKSTI ALLLLRYYNP
TTGTITIDNQ DISKLNCKSL RRHIGIVQQE PVLMSGTIRD NITYGLTYTP
TKEEIRSVAK QCFCHNFITK FPNTYDTVIG PHGTLLSGGQ KQRIAIARAL
IKKPTILILD EATSALDVES EGAINYTFGQ LMKSKSMTIV SIAHRLSTIR
RSENVIVLGH DGSVVEMGKF KELYANPTSA LSQLLNEKAA PGPSDQQLQI
EKVIEKEDLN ESKEHDDQKK DDNDDNDNNH DNDSNNQSPE TKDNNSDDIE
KSVEHLLKDA AKEANPIKIT PQP
RSPAVGKSLI LQSFRCNSSK TVPETSLPSA SPISKGSARS AHAKEQSKTD
DYKDIIRLFM LAKRDWKLLL TAILLLTISC SIGMSIPKVI GIVLDTLKTS
SGSDFFDLKI PIFSLPLYEF LSFFTVALLI GCAANFGRFI LLRILSERVV
ARLRANVIKK TLHQDAEFFD NHKVGDLISR LGSDAYVVSR SMTQKVSDGV
KALICGVVGV GMMCSLSPQL SILLLFFTPP VLFSASVFGK QIRNTSKDLQ
EATGQLTRVA EEQLSGIKTV QSFVAEGNEL SRYNVAIRDI FQVGKTAAFT
NAKFFTTTSL LGDLSFLTVL AYGSYLVLQS QLSIGDLTAF MLYTEYTGNA
VFGLSTFYSE IMQGAGAASR LFELTDRKPS ISPTVGHKYK PDRGVIEFKD
VSFSYPTRPS VQIFKNLNFK IAPGSSVCIV GPSGRGKSTI ALLLLRYYNP
TTGTITIDNQ DISKLNCKSL RRHIGIVQQE PVLMSGTIRD NITYGLTYTP
TKEEIRSVAK QCFCHNFITK FPNTYDTVIG PHGTLLSGGQ KQRIAIARAL
IKKPTILILD EATSALDVES EGAINYTFGQ LMKSKSMTIV SIAHRLSTIR
RSENVIVLGH DGSVVEMGKF KELYANPTSA LSQLLNEKAA PGPSDQQLQI
EKVIEKEDLN ESKEHDDQKK DDNDDNDNNH DNDSNNQSPE TKDNNSDDIE
KSVEHLLKDA AKEANPIKIT PQP
Legend
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[90, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[90, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[694, Phos] | Guo X, Niemi NM, Hutchins PD, et al (2017b) Ptc7p dephosphorylates select mitochondrial proteins to enhance metabolic function. Cell Reports 18:307–313. (Publication) (All modifications) |
[694, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |