1.R.1.1.1 Membrane Contact Site (MCS). Functions include lipid and ion transport between organelles as well as organelle positioning and division (Wu et al. 2018). Constituents include: Seipin, 398 aas and 2 - 4 TMSs, Q96G97. Protrudin, 411 aas and 4 - 5 TMSs, Q5T4F4. Spastin (SPAST, ADPSP, FSP2, SPG4), 616 aas, 1 N-terminal TMS, Q9UBP0. Vesicle-associated membrane protein-associated protein A, (VAPA, VAP33), 249 aas, 1 C-terninal TMS, a member of TC family 9.B.17), Q9P0L0. Vesicle-associated membane protein associated, VAPB/C (see TC 9.B.17.1.1), 243 aas and 1 C-terminal TMS, O95292. Dynamin 2 (Dyn2, Dnm2) GTPase, 870 aas, 1 TMS, see TC# 8.A.34.1.4, P50570. Mitofusin 2 (Mfn2, CPRP1) GTPase, 757 aas, 0 - 2 TMSs, (see TC# 1.N.6.1.2), O95140. Acyl-CoA binding domain-containing protein 5, ACBD5, 534 aas, 1 C-terminal TMS, Q5T8D3. Mitofusin; Its heptad repeat domain 1 has membrane destabilization function in mitochondrial fusion (Daste et al. 2018). PDZ domain-containing protein 8, PDZD8, of 1154 aas, a molecular tethering protein that connects ER and mitochondria membranes and is a shared component of at least two distinct MCSs (Hirabayashi et al. 2017; Elbaz-Alon et al. 2020). Mfn2 regulates mitochondria and
mitochondria-associated endoplasmic reticulum membrane function in
neurodegeneration induced by repeated sevoflurane exposure (Zhu et al. 2024).
|
Accession Number: | P50570 |
Protein Name: | Dynamin-2 |
Length: | 870 |
Molecular Weight: | 98064.00 |
Species: | Homo sapiens (Human) [9606] |
Number of TMSs: | 1 |
Location1 / Topology2 / Orientation3: |
Cytoplasm1 |
Substrate |
lipid |
---|
1: MGNRGMEELI PLVNKLQDAF SSIGQSCHLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
61: SGIVTRRPLI LQLIFSKTEH AEFLHCKSKK FTDFDEVRQE IEAETDRVTG TNKGISPVPI
121: NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP DIEYQIKDMI LQFISRESSL ILAVTPANMD
181: LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
241: DIEGKKDIRA ALAAERKFFL SHPAYRHMAD RMGTPHLQKT LNQQLTNHIR ESLPALRSKL
301: QSQLLSLEKE VEEYKNFRPD DPTRKTKALL QMVQQFGVDF EKRIEGSGDQ VDTLELSGGA
361: RINRIFHERF PFELVKMEFD EKDLRREISY AIKNIHGVRT GLFTPDLAFE AIVKKQVVKL
421: KEPCLKCVDL VIQELINTVR QCTSKLSSYP RLREETERIV TTYIREREGR TKDQILLLID
481: IEQSYINTNH EDFIGFANAQ QRSTQLNKKR AIPNQGEILV IRRGWLTINN ISLMKGGSKE
541: YWFVLTAESL SWYKDEEEKE KKYMLPLDNL KIRDVEKGFM SNKHVFAIFN TEQRNVYKDL
601: RQIELACDSQ EDVDSWKASF LRAGVYPEKD QAENEDGAQE NTFSMDPQLE RQVETIRNLV
661: DSYVAIINKS IRDLMPKTIM HLMINNTKAF IHHELLAYLY SSADQSSLME ESADQAQRRD
721: DMLRMYHALK EALNIIGDIS TSTVSTPVPP PVDDTWLQSA SSHSPTPQRR PVSSIHPPGR
781: PPAVRGPTPG PPLIPVPVGA AASFSAPPIP SRPGPQSVFA NSDLFPAPPQ IPSRPVRIPP
841: GIPPGVPSRR PPAAPSRPTI IRPAEPSLLD