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Q6ZQ89 (MARH6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase MARCH6
EC=6.3.2.-
Alternative name(s):
Membrane-associated RING finger protein 6
Membrane-associated RING-CH protein VI
Short name=MARCH-VI
Gene names
Name:March6
Synonyms:Kiaa0597
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length909 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase that promotes ubiquitination of DIO2, leading to its degradation. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May cooperate with UBE2G1 By similarity.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with DIO2 By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Domain

The RING-CH-type zinc finger domain is required for E3 ligase activity By similarity.

Post-translational modification

Auto-ubiquitinated, which results in proteasomal degradation By similarity.

Sequence similarities

Belongs to the DOA10/MARCH6 family.

Contains 1 RING-CH-type zinc finger.

Sequence caution

The sequence AAH37454.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein K48-linked ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentintegral to endoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionubiquitin-protein ligase activity

Inferred from electronic annotation. Source: Compara

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6ZQ89-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q6ZQ89-2)

The sequence of this isoform differs from the canonical sequence as follows:
     625-821: PLNFPLRIFL...VISVLLLSLC → LPRWAPSHWQ...SWGFIVHNIC
     822-909: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q6ZQ89-3)

The sequence of this isoform differs from the canonical sequence as follows:
     683-708: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 909909E3 ubiquitin-protein ligase MARCH6
PRO_0000274299

Regions

Topological domain1 – 9191Cytoplasmic Potential
Transmembrane92 – 11221Helical; Potential
Topological domain113 – 14230Extracellular Potential
Transmembrane143 – 16321Helical; Potential
Topological domain164 – 283120Cytoplasmic Potential
Transmembrane284 – 30421Helical; Potential
Topological domain305 – 33632Extracellular Potential
Transmembrane337 – 35721Helical; Potential
Topological domain358 – 37619Cytoplasmic Potential
Transmembrane377 – 39721Helical; Potential
Topological domain398 – 42124Extracellular Potential
Transmembrane422 – 44221Helical; Potential
Topological domain443 – 48038Cytoplasmic Potential
Transmembrane481 – 50121Helical; Potential
Topological domain502 – 51918Extracellular Potential
Transmembrane520 – 54021Helical; Potential
Topological domain541 – 63191Cytoplasmic Potential
Transmembrane632 – 65221Helical; Potential
Topological domain653 – 67725Extracellular Potential
Transmembrane678 – 69821Helical; Potential
Topological domain699 – 72022Cytoplasmic Potential
Transmembrane721 – 74121Helical; Potential
Topological domain742 – 76322Extracellular Potential
Transmembrane764 – 78421Helical; Potential
Topological domain785 – 81430Cytoplasmic Potential
Transmembrane815 – 83521Helical; Potential
Topological domain836 – 84712Extracellular Potential
Transmembrane848 – 86821Helical; Potential
Topological domain869 – 90941Cytoplasmic Potential
Zinc finger1 – 6262RING-CH-type

Natural variations

Alternative sequence625 – 821197PLNFP…LLSLC → LPRWAPSHWQGLLSCVLCPV AFRKMMSSWGFIVHNIC in isoform 2.
VSP_022702
Alternative sequence683 – 70826Missing in isoform 3.
VSP_022704
Alternative sequence822 – 90988Missing in isoform 2.
VSP_022703

Experimental info

Sequence conflict4761H → N in BAC31427. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 6, 2007. Version 2.
Checksum: DC46CB2A34B6F749

FASTA909102,273
        10         20         30         40         50         60 
MDTAEEDICR VCRSEGTPEK PLYHPCVCTG SIKFIHQECL VQWLKHSRKE YCELCKHRFA 

        70         80         90        100        110        120 
FTPIYSPDMP SRLPIQDIFA GLVTSIGTAI RYWFHYTLVA FAWLGVVPLT ACRIYKCLFT 

       130        140        150        160        170        180 
GSVSSLLTLP LDMLSTENLL ADCLQGCFVV TCTLCAFISL VWLREQIVHG GAPIWLEHAA 

       190        200        210        220        230        240 
PPFNAAGHHQ NEAPVGGNGA ENPAADQPAN PAGENAVLGE NPDAQDGQAE EEEEDNEEED 

       250        260        270        280        290        300 
DAGVEDAADA NNGAQDDMNW NALEWDRAAE ELTWERMLGL DGSLVFLEHV FWVVSLNTLF 

       310        320        330        340        350        360 
ILVFAFCPYH IGHFSLVGLG FEEHVQASHF EGLITTIVGY ILLAITLIIC HALATLVKFH 

       370        380        390        400        410        420 
RSRRLLGVCY IVVKVSLLVV VEIGVFPLIC GWWLDICSLE MFDATLKDRE LSFQSAPGTT 

       430        440        450        460        470        480 
MFLHWLVGMV YVFYFASFIL LLREVLRPGV LWFLRNLNDP DFNPVQEMIH LPIYRHLRRF 

       490        500        510        520        530        540 
ILSVIVFGSI VLLMLWLPIR IIKSLLPNFL PYNVMLYSDA PVSELSLELL LLQVVLPALL 

       550        560        570        580        590        600 
EQGHTRQWLK GLVRAWTVTA GYLLDLHSYL LGDQEENENS ANQQVNNNQP ARNNNAVPAG 

       610        620        630        640        650        660 
EGLHAAHQAI LQQGGPVGFQ PYRRPLNFPL RIFLLIVFMC ITLLIASLIC LTLPVFAGRW 

       670        680        690        700        710        720 
LMSFWTGTAK IHELYTAACG LYVCWLTIRA VTVLVAWMPQ GRRVIFQKVK EWSLMIMKTL 

       730        740        750        760        770        780 
IVAVLLAGVV PLLLGLLFEL VIVAPLRVPL DQTPLFYPWQ DWALGVLHAK IIAAITLMGP 

       790        800        810        820        830        840 
QWWLKTVIEQ VYANGIRNID LHYIIRKLAA PVISVLLLSL CVPYVIASGA VPLLGVTAEM 

       850        860        870        880        890        900 
QNLVHRRIYP FLLMVVVLMG ILSFQVRQFK RLYEHIKNDK YLVGQRLVNY ERKSGKQGPS 


TPPPVSSQE

« Hide

Isoform 2 [UniParc].

Checksum: C73C562C44B0DAF4
Show »

FASTA66174,274
Isoform 3 [UniParc].

Checksum: 5DB1C80612C77827
Show »

FASTA88399,219

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 476-909 (ISOFORM 1).
Strain: C57BL/6J and NOD.
Tissue: Cerebellum and Spleen.
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 348-883 (ISOFORM 3).
Tissue: Brain.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 383-909 (ISOFORM 1).
Strain: Czech II and FVB/N.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK042980 mRNA. Translation: BAC31427.1.
AK089827 mRNA. Translation: BAC40971.1.
AK129169 Transcribed RNA. Translation: BAC97979.1.
BC037454 mRNA. Translation: AAH37454.1. Different initiation.
BC048816 mRNA. Translation: AAH48816.1.
BC059190 mRNA. Translation: AAH59190.2.
IPIIPI00222351.
IPI00403537.
IPI00828730.
RefSeqNP_766194.2. NM_172606.2.
UniGeneMm.272185.

3D structure databases

ProteinModelPortalQ6ZQ89.
SMRQ6ZQ89. Positions 4-59.
ModBaseSearch...

PTM databases

PhosphoSiteQ6ZQ89.

Proteomic databases

PaxDbQ6ZQ89.
PRIDEQ6ZQ89.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000090227; ENSMUSP00000087694; ENSMUSG00000039100.
GeneID223455.
KEGGmmu:223455.
UCSCuc007vkh.1. mouse.

Organism-specific databases

CTD10299.
MGIMGI:2442773. March6.
RougeSearch...

Phylogenomic databases

eggNOGCOG5183.
GeneTreeENSGT00500000044902.
HOGENOMHOG000286005.
HOVERGENHBG080753.
InParanoidQ6ZQ89.
KOK10661.
OMADNLLADC.
OrthoDBEOG4WM4T3.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ6ZQ89.
BgeeQ6ZQ89.
CleanExMM_MARCH6.
GenevestigatorQ6ZQ89.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF12906. RINGv. 1 hit.
[Graphical view]
SMARTSM00744. RINGv. 1 hit.
[Graphical view]
PROSITEPS51292. ZF_RING_CH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMARCH6. mouse.
NextBio376726.
SOURCESearch...

Entry information

Entry nameMARH6_MOUSE
AccessionPrimary (citable) accession number: Q6ZQ89
Secondary accession number(s): Q6PCS1 expand/collapse secondary AC list , Q80V02, Q80VC7, Q8BJA0, Q8BXX6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: February 6, 2007
Last modified: May 1, 2013
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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