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E3 ubiquitin-protein ligase MARCH5 (EC 2.3.2.27) (Membrane-associated RING finger protein 5) (Membrane-associated RING-CH protein V) (MARCH-V) (Mitochondrial ubiquitin ligase) (MITOL) (RING finger protein 153) (RING-type E3 ubiquitin transferase MARCH5)

 MARH5_HUMAN             Reviewed;         278 AA.
Q9NX47;
09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
30-AUG-2017, entry version 151.
RecName: Full=E3 ubiquitin-protein ligase MARCH5;
EC=2.3.2.27;
AltName: Full=Membrane-associated RING finger protein 5;
AltName: Full=Membrane-associated RING-CH protein V;
Short=MARCH-V;
AltName: Full=Mitochondrial ubiquitin ligase;
Short=MITOL;
AltName: Full=RING finger protein 153;
AltName: Full=RING-type E3 ubiquitin transferase MARCH5 {ECO:0000305};
Name=MARCH5; Synonyms=RNF153;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MFN2 AND DNM1L, AND
SUBCELLULAR LOCATION.
PubMed=16936636; DOI=10.1038/sj.embor.7400790;
Nakamura N., Kimura Y., Tokuda M., Honda S., Hirose S.;
"MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to
change mitochondrial morphology.";
EMBO Rep. 7:1019-1022(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
SUBCELLULAR LOCATION.
PubMed=14722266; DOI=10.1128/JVI.78.3.1109-1120.2004;
Bartee E., Mansouri M., Hovey Nerenberg B.T., Gouveia K., Frueh K.;
"Downregulation of major histocompatibility complex class I by human
ubiquitin ligases related to viral immune evasion proteins.";
J. Virol. 78:1109-1120(2004).
[6]
FUNCTION AS AN E3 UBIQUITIN LIGASE FOR FIS1 AND DNM1L AND AS A
REGULATOR OF MITOCHONDRIAL FISSION, AUTOUBIQUITINATION, PTM,
SUBCELLULAR LOCATION, INTERACTION WITH FIS1 AND DNM1L, TISSUE
SPECIFICITY, AND MUTAGENESIS OF CYS-65 AND CYS-68.
PubMed=16874301; DOI=10.1038/sj.emboj.7601249;
Yonashiro R., Ishido S., Kyo S., Fukuda T., Goto E., Matsuki Y.,
Ohmura-Hoshino M., Sada K., Hotta H., Yamamura H., Inatome R.,
Yanagi S.;
"A novel mitochondrial ubiquitin ligase plays a critical role in
mitochondrial dynamics.";
EMBO J. 25:3618-3626(2006).
[7]
FUNCTION AS A REGULATOR OF MITOCHONDRIAL MORPHOLOGY, MUTAGENESIS OF
HIS-43; CYS-65 AND CYS-68, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=17606867; DOI=10.1083/jcb.200611064;
Karbowski M., Neutzner A., Youle R.J.;
"The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1
dependent mitochondrial division.";
J. Cell Biol. 178:71-84(2007).
[8]
FUNCTION AS A REGULATOR OF MITOCHONDRIAL QUALITY CONTROL, AND
SUBCELLULAR LOCATION.
PubMed=19741096; DOI=10.1091/mbc.E09-02-0112;
Yonashiro R., Sugiura A., Miyachi M., Fukuda T., Matsushita N.,
Inatome R., Ogata Y., Suzuki T., Dohmae N., Yanagi S.;
"Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and
attenuates mutant SOD1-induced reactive oxygen species generation.";
Mol. Biol. Cell 20:4524-4530(2009).
[9]
FUNCTION AS AN E3 UBIQUITIN LIGASE FOR MFN1 AND AS A POSITIVE
REGULATOR OF MITOCHONDRIAL FISSION, MUTAGENESIS OF HIS-43, AND
INTERACTION WITH MFN1.
PubMed=20103533; DOI=10.1242/jcs.061481;
Park Y.Y., Lee S., Karbowski M., Neutzner A., Youle R.J., Cho H.;
"Loss of MARCH5 mitochondrial E3 ubiquitin ligase induces cellular
senescence through dynamin-related protein 1 and mitofusin 1.";
J. Cell Sci. 123:619-626(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Mitochondrial E3 ubiquitin-protein ligase that plays a
crucial role in the control of mitochondrial morphology by acting
as a positive regulator of mitochondrial fission. May play a role
in the prevention of cell senescence acting as a regulator of
mitochondrial quality control. Promotes ubiquitination of FIS1,
DNM1L and MFN1. {ECO:0000269|PubMed:16874301,
ECO:0000269|PubMed:17606867, ECO:0000269|PubMed:19741096,
ECO:0000269|PubMed:20103533}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Monomer and homodimer. Interacts with MFN1, MFN2, DNM1L
and FIS1. {ECO:0000269|PubMed:16874301,
ECO:0000269|PubMed:16936636, ECO:0000269|PubMed:17606867,
ECO:0000269|PubMed:20103533}.
-!- INTERACTION:
O43583:DENR; NbExp=2; IntAct=EBI-2341610, EBI-716083;
Q969F0:FATE1; NbExp=3; IntAct=EBI-2341610, EBI-743099;
P0CG48:UBC; NbExp=2; IntAct=EBI-2341610, EBI-3390054;
Q96B02:UBE2W; NbExp=4; IntAct=EBI-2341610, EBI-716589;
Q96FI0:UBE2W; NbExp=3; IntAct=EBI-2341610, EBI-10285774;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
{ECO:0000269|PubMed:16874301}; Multi-pass membrane protein
{ECO:0000255}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:14722266}; Multi-pass membrane protein
{ECO:0000255}. Note=Authors show that the protein can be detected
in endoplasmic reticulum (PubMed:14722266). Authors
(PubMed:16874301) show its presence only in mitochondria
(PubMed:16874301). {ECO:0000269|PubMed:14722266,
ECO:0000269|PubMed:16874301}.
-!- TISSUE SPECIFICITY: Expressed in brain, heart, liver, lung,
spleen, stomach, testis, skeletal and muscle.
{ECO:0000269|PubMed:16874301}.
-!- DOMAIN: The RING-CH-type zinc finger domain is required for E3
ligase activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
-!- PTM: Autoubiquitinated leading to degradation (short half-life).
{ECO:0000269|PubMed:16874301}.
-!- MISCELLANEOUS: By binding to and ubiquitinating two ALS1 variants
of SOD1 (mSOD1 variants Arg-86 and Ala-94) it attenuates their
cytotoxicity.
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EMBL; AB191202; BAF02285.1; -; mRNA.
EMBL; AK000452; BAA91173.1; -; mRNA.
EMBL; AL158040; CAI13639.1; -; Genomic_DNA.
EMBL; AL161652; CAI13639.1; JOINED; Genomic_DNA.
EMBL; AL161652; CAI15361.1; -; Genomic_DNA.
EMBL; AL158040; CAI15361.1; JOINED; Genomic_DNA.
EMBL; BC015480; AAH15480.1; -; mRNA.
CCDS; CCDS7420.1; -.
RefSeq; NP_060294.1; NM_017824.4.
UniGene; Hs.573490; -.
ProteinModelPortal; Q9NX47; -.
SMR; Q9NX47; -.
BioGrid; 120105; 33.
IntAct; Q9NX47; 15.
MINT; MINT-2844053; -.
STRING; 9606.ENSP00000351813; -.
iPTMnet; Q9NX47; -.
PhosphoSitePlus; Q9NX47; -.
BioMuta; MARCH5; -.
DMDM; 74762759; -.
EPD; Q9NX47; -.
MaxQB; Q9NX47; -.
PaxDb; Q9NX47; -.
PeptideAtlas; Q9NX47; -.
PRIDE; Q9NX47; -.
Ensembl; ENST00000358935; ENSP00000351813; ENSG00000198060.
GeneID; 54708; -.
KEGG; hsa:54708; -.
UCSC; uc001khx.1; human.
CTD; 54708; -.
DisGeNET; 54708; -.
GeneCards; MARCH5; -.
HGNC; HGNC:26025; MARCH5.
HPA; HPA056596; -.
MIM; 610637; gene.
neXtProt; NX_Q9NX47; -.
OpenTargets; ENSG00000198060; -.
PharmGKB; PA128394672; -.
eggNOG; KOG3053; Eukaryota.
eggNOG; ENOG410XSJW; LUCA.
GeneTree; ENSGT00390000009948; -.
HOGENOM; HOG000247040; -.
HOVERGEN; HBG059795; -.
InParanoid; Q9NX47; -.
KO; K10660; -.
OMA; KQYGRRK; -.
OrthoDB; EOG091G0G4K; -.
PhylomeDB; Q9NX47; -.
TreeFam; TF316219; -.
UniPathway; UPA00143; -.
ChiTaRS; MARCH5; human.
GeneWiki; MARCH5; -.
GenomeRNAi; 54708; -.
PRO; PR:Q9NX47; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000198060; -.
CleanEx; HS_MARCH5; -.
Genevisible; Q9NX47; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0090344; P:negative regulation of cell aging; IMP:UniProtKB.
GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:UniProtKB.
GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
GO; GO:0070585; P:protein localization to mitochondrion; IMP:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0090140; P:regulation of mitochondrial fission; IMP:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR033275; MARCH-like.
InterPro; IPR011016; Znf_RING-CH.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR23012; PTHR23012; 1.
Pfam; PF12906; RINGv; 1.
SMART; SM00744; RINGv; 1.
PROSITE; PS51292; ZF_RING_CH; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Membrane; Metal-binding;
Mitochondrion; Mitochondrion outer membrane; Reference proteome;
Transferase; Transmembrane; Transmembrane helix; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 278 E3 ubiquitin-protein ligase MARCH5.
/FTId=PRO_0000271769.
TRANSMEM 99 119 Helical. {ECO:0000255}.
TRANSMEM 139 159 Helical. {ECO:0000255}.
TRANSMEM 209 229 Helical. {ECO:0000255}.
TRANSMEM 238 258 Helical. {ECO:0000255}.
ZN_FING 6 75 RING-CH-type. {ECO:0000255|PROSITE-
ProRule:PRU00623}.
MUTAGEN 43 43 H->W: Loss of ubiquitin ligase activity,
formation of highly interconnected
mitochondria, change in mitochondria
morphology that in turns triggers
senescence, and perinuclear accumulation.
{ECO:0000269|PubMed:17606867,
ECO:0000269|PubMed:20103533}.
MUTAGEN 65 65 C->S: Loss of E3 ubiquitin ligase
activity. Formation of highly
interconnected mitochondria and
perinuclear accumulation; when associated
with S-68. {ECO:0000269|PubMed:16874301,
ECO:0000269|PubMed:17606867}.
MUTAGEN 68 68 C->S: Loss of E3 ubiquitin ligase
activity. Formation of highly
interconnected mitochondria and
perinuclear accumulation; when associated
with S-65. {ECO:0000269|PubMed:16874301,
ECO:0000269|PubMed:17606867}.
SEQUENCE 278 AA; 31232 MW; CB00A408E228A9EE CRC64;
MPDQALQQML DRSCWVCFAT DEDDRTAEWV RPCRCRGSTK WVHQACLQRW VDEKQRGNST
ARVACPQCNA EYLIVFPKLG PVVYVLDLAD RLISKACPFA AAGIMVGSIY WTAVTYGAVT
VMQVVGHKEG LDVMERADPL FLLIGLPTIP VMLILGKMIR WEDYVLRLWR KYSNKLQILN
SIFPGIGCPV PRIPAEANPL ADHVSATRIL CGALVFPTIA TIVGKLMFSS VNSNLQRTIL
GGIAFVAIKG AFKVYFKQQQ YLRQAHRKIL NYPEQEEA


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EIAAB07154 Checkpoint with forkhead and RING finger domains protein,CHFR,E3 ubiquitin-protein ligase CHFR,Homo sapiens,Human,RING finger protein 196,RNF196
EIAAB34425 E3 ubiquitin-protein ligase RFWD3,Homo sapiens,Human,RFWD3,RING finger and WD repeat domain-containing protein 3,RING finger protein 201,RNF201
EIAAB34369 E3 ubiquitin-protein ligase rififylin,FYVE-RING finger protein Sakura,Rat,Rattus norvegicus,Rffl,RING finger and FYVE-like domain-containing protein 1
EIAAB35481 Dorfin,Double ring-finger protein,E3 ubiquitin-protein ligase RNF19A,Homo sapiens,Human,p38,RING finger protein 19A,RNF19,RNF19A
EIAAB45296 Ac2-121,E3 ubiquitin-protein ligase UHRF1,Liver regeneration-related protein LRRG126,Rat,Rattus norvegicus,Ubiquitin-like PHD and RING finger domain-containing protein 1,Ubiquitin-like-containing PHD


 

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