MID49_PONAB
ID MID49_PONAB Reviewed; 454 AA.
AC Q5RA76; Q5RC08;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Mitochondrial dynamics protein MID49;
DE AltName: Full=Mitochondrial dynamics protein of 49 kDa homolog;
DE AltName: Full=Mitochondrial elongation factor 2;
DE AltName: Full=Smith-Magenis syndrome chromosomal region candidate gene 7 protein homolog;
GN Name=MIEF2; Synonyms=MID49, SMCR7;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mitochondrial outer membrane protein which regulates
CC mitochondrial organization (By similarity). It is required for
CC mitochondrial fission and promotes the recruitment and association of
CC the fission mediator dynamin-related protein 1 (DNM1L) to the
CC mitochondrial surface independently of the mitochondrial fission FIS1
CC and MFF proteins (By similarity). Regulates DNM1L GTPase activity (By
CC similarity). {ECO:0000250|UniProtKB:Q96C03}.
CC -!- SUBUNIT: Interacts with DNM1L. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC membrane protein. Note=Colocalizes with DNM1L at mitochondrial
CC membrane. Forms foci and rings around mitochondria (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Does not bind ADP or other nucleotides, in contrast to
CC MIEF1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MID49/MID51 family. {ECO:0000305}.
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DR EMBL; CR858474; CAH90702.1; -; mRNA.
DR EMBL; CR859143; CAH91334.1; -; mRNA.
DR RefSeq; NP_001125789.1; NM_001132317.1.
DR AlphaFoldDB; Q5RA76; -.
DR SMR; Q5RA76; -.
DR STRING; 9601.ENSPPYP00000009052; -.
DR GeneID; 100172717; -.
DR KEGG; pon:100172717; -.
DR CTD; 125170; -.
DR eggNOG; ENOG502QPJX; Eukaryota.
DR InParanoid; Q5RA76; -.
DR OrthoDB; 515815at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISS:UniProtKB.
DR InterPro; IPR024810; Mab-21_dom.
DR InterPro; IPR045909; MID49/MID51.
DR PANTHER; PTHR16451; PTHR16451; 1.
DR Pfam; PF03281; Mab-21; 1.
DR SMART; SM01265; Mab-21; 1.
PE 2: Evidence at transcript level;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..454
FT /note="Mitochondrial dynamics protein MID49"
FT /id="PRO_0000310447"
FT TOPO_DOM 1..22
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 76..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 197
FT /note="L -> Q (in Ref. 1; CAH90702)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="R -> H (in Ref. 1; CAH90702)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 454 AA; 49270 MW; 9BF94A0A155E053F CRC64;
MAEFSQKRGK RRGDEGLGSM VDFLLANARL VLGVGGAAVL GIATLAVKRF IDRATSPRDE
DDTKADSWKE LSLLKATPHL QPRPPPAALS QPVLPLAPSS SAPEGPAKSD PEVTPQLSSP
APLCLTLQER LLAFERDRVT IPAAQVALAK QLAGDIALEL QAYFQSKFPE LPFGAFVPGG
PLYDGLQAGA ADHVRLLVPL VLEPGLWSLV PGVDTVARDP RCWAVRRTQL EFCPRGSSPW
DRFLVGGYLS SRVLLELLRK VLAASVNWPA IGSLLGCLIR PSMASEELLL EVQHERLELT
VAVLVAVPGV DADDRLLLAW PLEGLAGNLW LQDLYPVEAA RLRALDDRDA GTRRRLLLLL
CAVCRGCSAL GQLGRGHLTQ VVLRLGEDNV DWTEEALGER FLQALELLIG SLEQASLPCH
FNPSVNLFSN LREEEIDDIG YALYSGLQEP EGLL