ID A0A395T6F4_9HYPO Unreviewed; 2909 AA.
AC A0A395T6F4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Mitochondrial distribution and morphology protein 12 {ECO:0000256|HAMAP-Rule:MF_03104};
DE AltName: Full=Mitochondrial inheritance component MDM12 {ECO:0000256|HAMAP-Rule:MF_03104};
GN Name=MDM12 {ECO:0000256|HAMAP-Rule:MF_03104};
GN ORFNames=FLONG3_1473 {ECO:0000313|EMBL:RGP80324.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP80324.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP80324.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP80324.1,
RC ECO:0000313|Proteomes:UP000266234};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- FUNCTION: Component of the ERMES/MDM complex, which serves as a
CC molecular tether to connect the endoplasmic reticulum (ER) and
CC mitochondria. Components of this complex are involved in the control of
CC mitochondrial shape and protein biogenesis, and function in
CC nonvesicular lipid trafficking between the ER and mitochondria. MDM12
CC is required for the interaction of the ER-resident membrane protein
CC MMM1 and the outer mitochondrial membrane-resident beta-barrel protein
CC MDM10. The MDM12-MMM1 subcomplex functions in the major beta-barrel
CC assembly pathway that is responsible for biogenesis of all
CC mitochondrial outer membrane beta-barrel proteins, and acts in a late
CC step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further
CC acts in the TOM40-specific pathway after the action of the MDM12-MMM1
CC complex. Essential for establishing and maintaining the structure of
CC mitochondria and maintenance of mtDNA nucleoids. {ECO:0000256|HAMAP-
CC Rule:MF_03104}.
CC -!- SUBUNIT: Component of the ER-mitochondria encounter structure (ERMES)
CC or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34. A MMM1
CC homodimer associates with one molecule of MDM12 on each side in a
CC pairwise head-to-tail manner, and the SMP-LTD domains of MMM1 and MDM12
CC generate a continuous hydrophobic tunnel for phospholipid trafficking.
CC {ECO:0000256|HAMAP-Rule:MF_03104}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000256|HAMAP-
CC Rule:MF_03104}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_03104}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_03104}.
CC Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03104};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03104};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_03104}. Note=The ERMES/MDM
CC complex localizes to a few discrete foci (around 10 per single cell),
CC that represent mitochondria-endoplasmic reticulum junctions. These foci
CC are often found next to mtDNA nucleoids. {ECO:0000256|HAMAP-
CC Rule:MF_03104}.
CC -!- SIMILARITY: Belongs to the MDM12 family. {ECO:0000256|HAMAP-
CC Rule:MF_03104}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RGP80324.1}.
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DR EMBL; PXOG01000032; RGP80324.1; -; Genomic_DNA.
DR STRING; 694270.A0A395T6F4; -.
DR Proteomes; UP000266234; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032865; C:ERMES complex; IEA:UniProtKB-UniRule.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IEA:UniProtKB-UniRule.
DR CDD; cd03334; Fab1_TCP; 1.
DR CDD; cd17300; PIPKc_PIKfyve; 1.
DR CDD; cd21672; SMP_Mdm12; 1.
DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR Gene3D; 3.50.7.10; GroEL; 1.
DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR HAMAP; MF_03104; Mdm12; 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027532; Mdm12.
DR InterPro; IPR019411; MMM1_dom.
DR InterPro; IPR044769; PIKfyve_PIPKc.
DR InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf.
DR InterPro; IPR002498; PInositol-4-P-4/5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR InterPro; IPR031468; SMP_LBD.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45748; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE-RELATED; 1.
DR PANTHER; PTHR45748:SF7; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE-RELATED; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF10296; MMM1; 1.
DR Pfam; PF01504; PIP5K; 2.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS51847; SMP; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03104};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_03104};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03104};
KW Mitochondrion outer membrane {ECO:0000256|HAMAP-Rule:MF_03104};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Reference proteome {ECO:0000313|Proteomes:UP000266234};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Transport {ECO:0000256|ARBA:ARBA00023055};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 415..474
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 2132..2462
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT DOMAIN 2492..2909
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1603..1676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1689..1846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1894..2044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2149..2168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2550..2605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2668..2690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2705..2755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2830..2851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..595
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1631..1654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1659..1676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1767..1784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1814..1838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1941..1967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1981..2028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2559..2577
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2675..2690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2705..2723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2832..2851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2909 AA; 324518 MW; A10A4C702CD1224D CRC64;
MSPPRAGSVV SESSPVRTRR DSISSITTGQ LAHTLDKIHT SASQSDSLTT FNDFAPPPIA
APTSDNKGIA GDLVQQGFSG LYSRLKEAVG GGSSPKSPLE QTAGEKSEPS SKRASITANH
GSKASISSLS RVDTGASMST TSSQVIQNDG ASTNVSGGTI EPRPQPQSSK PSSISLMSNQ
KASSTNRQSF SKKAPSSIAA DPTIAPITVH RDPSNTTLRT EDSGGAGSSR KSVSSRVDLQ
AHLITAESSS SLFDMKEGKL PPKSKRDDTS SIDESIKSPT SPRSAHHHRT PSLQTLQTRS
LRSPSITSSL LSPDSVRRKP AVIDRISRSK SPGDQNSRDS SLDRGTAEPS HVSTSAHDSV
CHDSFSHNPK PQKMASGDFR IPGTVTSNEE ASEQVNAQLN RMRKQVLSKE FWMKDDTVKE
CFLCQTPFSA FRRKHHCRTC GCIFDSKCTT VISGEKFGVQ GSLRVCKRCL EVITRRFDGS
GSEDSGDEQS FMPRFFGSNH AKSPSNASQS KPKDNESGVA SEGSEDSRPV SRPVTTPMMA
IPATRRLGES RAAAILEIDA PQLSRPGSSR SLKSLSARPH SSAGHKRHHS KHGGFLNRFK
PAPEERAPFR RGVDDESAKK PKFPAFHDDN IIDPELADYM SDESSEDEQM SLFATMTGDL
QPGSLGDDKS ELTPYVNANR KYRHRAGEKS ISGMSFASRT GIDDLPGSLG AYRRPPRRRN
TSNVGGSIHY LPSPRPKSGV YKGPSQSSEM LFALDTPHHS ASQITRSDSL QHKKAPKVEL
NSSSLRHVDK LLHQLLDDAE IPNPPAWQKA LVPILLQATD DVDPDVAKGE DMDIRHYVKL
KRIPGGKPGD TAYISGVVFT KNLALKSMPR RITNPRIMLV TFPIEYQRHQ QHFMSLQPVI
EQEKEFLRVV VQRITNLRPH VLLAEKSISG VALQYLSDSN ISVAYNVKHT VIEAVARCAE
TDIISSLDML ALPVQIGRCS NFEVRTFVNN DYPGRKKSYI FLSGCTPELG CTIALRGANS
TVLSKVKHIM EFMVYVVYNL KLESSLLRDE SIELPEGGES MANSVHLPID SVRSQSVSSA
DHSRDGPAVV VNHPASESEP PSQTTIDSSS IAETDDTGSI SQSGQLAQDR ARLKSLQEQP
EPAAEDQTSQ VPDDVPMPTY YSDMVAKYET KILSASPYVK FTQPYLLMKA REQERRLLYL
RRLRNHDYYE EKGDPEKSDP PRFQLIKPEM VEAIGQKAPR QIMEILRAVH DAEYDKALYN
YQTQTRQWET YIQGNLDLFD PYSHQNIVVL YSVICTETKI PCTEPSLVAI NFYDEQHIDT
GMDPDCTLGQ YIEDLAFTMN QVCTSNGCER RMLEHHRTYV HDQSRITVFV ENLPNTSPMA
ELEGITMWTY CKICKKDTEE RTMSEATYKY SFGKYLELLF WGRGLKMKYM HDCPHDHHRD
HVRYFSLQDA RIRIHWDPID LLEIVVPRAR ITWKVTNDLK LKNEIFARME ERWAKFMTSV
RSRLMCIRID SVLPEKADLC KSEVDRLTAK AKEDLPLIVK RLQDIYVNSK YYEVVPFNSI
VREMLEKAGE WDQAFTKFEA DFLSDKDMRQ LTIMQLKKMF TDNESKESLT SNEGTPSTVD
SEERPSQTFT EEEGKSTQPT EYTDNTSMEA SVASSKPVDN RDVPDDDGKV EIPAEGVIER
VEPLDLACAP LTPSNPPSEY FPAGEVSEDL EDQETPLALD PEQTPKAPSK AFDTISTDPA
EPIPSPIEAL PSPVPSLSER VDQMRREQGQ SSIPTPTSER APSRKAGQAI SPPMVRATSH
PNRGLPRTQS GIGKGLGTKE SKSNSSESTG SDSITTPDGS IRVDKKLSDR LGLRNLKDRG
KATASGIPRF VHKKRESKVS TLAKHFEQLS REFEKERIRD RKKRAASMRQ PRAMLPRTTT
KAIVEVYDDV NEAFEEPSPP TDSVAEREAS KRAGSITSRK SESRQRTDPV SEPLTPAEPP
ASREEQEHGN QNQQHEEDEH HQELQDKEQE EKDEKTEKME KEDNDEHTIA NTSQTFSDDE
ERATDLEHSV PDEYLHDIKE IADSVDASEI PLELPKHQKT SLMKYLTNFW AERGASGWHP
LEYPVNPSDH IFVDSDIIVR EDEPSSVIAL ALNSEDYKGK LRNIRREAQE TMQRESDSGV
DGEPKSLPSE GIDWVSETEL EKSLLRVTGT HLKYQFREGT ATMTCKIFYA EQFDALRKKC
GVAERIVESL SRCLKWDSKG GKTKSVFLKT LDDRLILKSL SPIETSAFLR FAPGYFNIMA
EALFHDLPSV IAKMLGFFQV FIKNPVTGTD IKLDLLITEN LFYDRTATRI FDLKGSMRNR
KIQSTGEQNE VLLDENMVEY IYESPLFARE HSKKLLRASV WNDTLFLARQ NVMDYSLMIA
VDEARKELVV GIIDCIRTYT WDKKLESWIK DRGFAGGGRN RPTVTSPKEY KSRFREAMAR
YILQAPNCWH LFNNPQYPHY YGRASLGKED SMSIELNWET LTSGPDGDAL AERIREFVHD
KFQTVPLPKF IRSVTVHGFD FGTIPPQLEL KDITDPLPDF YEEDLDDDEE DSEEEPSPPP
PPPEPARMRP GQAPWGASTR RGGGLRSDVL RNEMMGHDLG SPFLGTSTPG ILGGSGLGYF
QSHLGTGTHT PLAAVASAHH TNWLSVPGTP AREWGTPSHT RNPSQSSLTS VDNFKASLDP
LQSLREKGSV STLAPTSVEA SRPPTRDTHL GGSAIVDDDE EEGEGEAGRR PREPRVEDVQ
AVFRIRYNGD IRLNLTAEIL LDYPMPSFVG IPLKLNITGL TFDGVGVLAH IRKRVHFCFL
GPDDALAAVG PDDTEEDSKG VAGASKNEHH KPRFGGLLQE IRVESEIGER VGGKQSLKNV
GKVERFVLEQ VRRIFESEFV YPSFWTFLV
//
