Basic Information
| Name | Mitochondrial intermediate peptidase (MIP) (EC 3.4.24.59) |
| Uniprot ID | P35999 |
| Systematic gene name | YKL134C |
| Standard gene name | OCT1 |
| Gene names | OCT1 MIP1 YKL134C |
| Description from SGD | YKL134C OCT1 SGDID:S000001617, Chr XI from 191442-189124, Genome Release 64-3-1, reverse complement, Verified ORF, "Mitochondrial intermediate peptidase; cleaves destabilizing N-terminal residues of a subset of proteins upon import, after their cleavage by mitochondrial processing peptidase (Mas1p-Mas2p); may contribute to mitochondrial iron homeostasis" |
| Protein length | 772 |
| Download | sequence (fasta, from Uniprot), modifications (csv format) |
| Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MLRTIILKAG SNASIPSPSR QNKLLRFFAT AGAVSRTSPG SIKKIFDDNS
YWRNINGQDA NNSKISQYLF KKNKTGLFKN PYLTSPDGLR KFSQVSLQQA
QELLDKMRND FSESGKLTYI MNLDRLSDTL CRVIDLCEFI RSTHPDDAFV
RAAQDCHEQM FEFMNVLNTD VSLCNILKSV LNNPEVSSKL SAEELKVGKI
LLDDFEKSGI YMNPDVREKF IQLSQEISLV GQEFINHTDY PGSNSVKIPC
KDLDNSKVST FLLKQLNKDV KGQNYKVPTF GYAAYALLKS CENEMVRKKL
WTALHSCSDK QVKRLSHLIK LRAILANLMH KTSYAEYQLE GKMAKNPKDV
QDFILTLMNN TIEKTANELK FIAELKAKDL KKPLTTNTDE ILKLVRPWDR
DYYTGKYFQL NPSNSPNAKE ISYYFTLGNV IQGLSDLFQQ IYGIRLEPAI
TDEGETWSPD VRRLNVISEE EGIIGIIYCD LFERNGKTSN PAHFTVCCSR
QIYPSETDFS TIQVGENPDG TYFQLPVISL VCNFSPILIA SKKSLCFLQL
SEVETLFHEM GHAMHSMLGR THMQNISGTR CATDFVELPS ILMEHFAKDI
RILTKIGKHY GTGETIQADM LQRFMKSTNF LQNCETYSQA KMAMLDQSFH
DEKIISDIDN FDVVENYQAL ERRLKVLVDD QSNWCGRFGH LFGYGATYYS
YLFDRTIASK IWYALFEDDP YSRKNGDKFK KHLLKWGGLK DPWKCIADVL
ECPMLEKGGS DAMEFIAQSH KS
YWRNINGQDA NNSKISQYLF KKNKTGLFKN PYLTSPDGLR KFSQVSLQQA
QELLDKMRND FSESGKLTYI MNLDRLSDTL CRVIDLCEFI RSTHPDDAFV
RAAQDCHEQM FEFMNVLNTD VSLCNILKSV LNNPEVSSKL SAEELKVGKI
LLDDFEKSGI YMNPDVREKF IQLSQEISLV GQEFINHTDY PGSNSVKIPC
KDLDNSKVST FLLKQLNKDV KGQNYKVPTF GYAAYALLKS CENEMVRKKL
WTALHSCSDK QVKRLSHLIK LRAILANLMH KTSYAEYQLE GKMAKNPKDV
QDFILTLMNN TIEKTANELK FIAELKAKDL KKPLTTNTDE ILKLVRPWDR
DYYTGKYFQL NPSNSPNAKE ISYYFTLGNV IQGLSDLFQQ IYGIRLEPAI
TDEGETWSPD VRRLNVISEE EGIIGIIYCD LFERNGKTSN PAHFTVCCSR
QIYPSETDFS TIQVGENPDG TYFQLPVISL VCNFSPILIA SKKSLCFLQL
SEVETLFHEM GHAMHSMLGR THMQNISGTR CATDFVELPS ILMEHFAKDI
RILTKIGKHY GTGETIQADM LQRFMKSTNF LQNCETYSQA KMAMLDQSFH
DEKIISDIDN FDVVENYQAL ERRLKVLVDD QSNWCGRFGH LFGYGATYYS
YLFDRTIASK IWYALFEDDP YSRKNGDKFK KHLLKWGGLK DPWKCIADVL
ECPMLEKGGS DAMEFIAQSH KS
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
| [63, 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) |
| [63, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
| [316, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
| [615, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |