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E3 ubiquitin-protein ligase MARCH1 (EC 2.3.2.27) (Membrane-associated RING finger protein 1) (Membrane-associated RING-CH protein I) (MARCH-I) (RING-type E3 ubiquitin transferase MARCH1)

 MARH1_MOUSE             Reviewed;         289 AA.
Q6NZQ8; Q3U7M8; Q3UVF8; Q8C294; Q8CBA1;
06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 2.
12-SEP-2018, entry version 121.
RecName: Full=E3 ubiquitin-protein ligase MARCH1;
EC=2.3.2.27;
AltName: Full=Membrane-associated RING finger protein 1;
AltName: Full=Membrane-associated RING-CH protein I;
Short=MARCH-I;
AltName: Full=RING-type E3 ubiquitin transferase MARCH1 {ECO:0000305};
Name=March1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
STRAIN=C57BL/6J, and NOD;
TISSUE=Aorta, Bone, Bone marrow, Cerebellum, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[3]
FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DRB.
PubMed=17051151; DOI=10.1038/nature05261;
Shin J.S., Ebersold M., Pypaert M., Delamarre L., Hartley A.,
Mellman I.;
"Surface expression of MHC class II in dendritic cells is controlled
by regulated ubiquitination.";
Nature 444:115-118(2006).
[4]
FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DRB, AND DISRUPTION
PHENOTYPE.
PubMed=17255932; DOI=10.1038/sj.emboj.7601556;
Matsuki Y., Ohmura-Hoshino M., Goto E., Aoki M., Mito-Yoshida M.,
Uematsu M., Hasegawa T., Koseki H., Ohara O., Nakayama M., Toyooka K.,
Matsuoka K., Hotta H., Yamamoto A., Ishido S.;
"Novel regulation of MHC class II function in B cells.";
EMBO J. 26:846-854(2007).
[5]
FUNCTION AS REGULATOR OF ANTIGEN PRESENTATION, PTM, MUTAGENESIS OF
TRP-114; LEU-225 AND TYR-232, AND SUBCELLULAR LOCATION.
PubMed=19880452; DOI=10.4049/jimmunol.0901521;
Jabbour M., Campbell E.M., Fares H., Lybarger L.;
"Discrete domains of MARCH1 mediate its localization, functional
interactions, and posttranscriptional control of expression.";
J. Immunol. 183:6500-6512(2009).
[6]
FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DR AND REGULATOR OF ANTIGEN
PRESENTATION, AND DISRUPTION PHENOTYPE.
PubMed=19917682; DOI=10.4049/jimmunol.0902178;
Ohmura-Hoshino M., Matsuki Y., Mito-Yoshida M., Goto E.,
Aoki-Kawasumi M., Nakayama M., Ohara O., Ishido S.;
"Requirement of MARCH-I-mediated MHC II ubiquitination for the
maintenance of conventional dendritic cells.";
J. Immunol. 183:6893-6897(2009).
-!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
of TFRC, CD86, FAS and MHC class II proteins, such as HLA-DR alpha
and beta, and promotes their subsequent endocytosis and sorting to
lysosomes via multivesicular bodies. By constitutively
ubiquitinating MHC class II proteins in immature dendritic cells,
down-regulates their cell surface localization thus sequestering
them in the intracellular endosomal system.
{ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17255932,
ECO:0000269|PubMed:19880452, ECO:0000269|PubMed:19917682}.
-!- 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.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305};
Multi-pass membrane protein {ECO:0000255}. Late endosome membrane
{ECO:0000269|PubMed:19880452}; Multi-pass membrane protein
{ECO:0000255}. Early endosome membrane
{ECO:0000269|PubMed:19880452}; Multi-pass membrane protein
{ECO:0000255}. Golgi apparatus, trans-Golgi network membrane
{ECO:0000269|PubMed:19880452}; Multi-pass membrane protein
{ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:19880452};
Multi-pass membrane protein {ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q6NZQ8-1; Sequence=Displayed;
Name=2;
IsoId=Q6NZQ8-2; Sequence=VSP_022726;
Name=3;
IsoId=Q6NZQ8-3; Sequence=VSP_022727;
Name=4;
IsoId=Q6NZQ8-4; Sequence=VSP_022726, VSP_022728;
Name=5;
IsoId=Q6NZQ8-5; Sequence=VSP_022728;
-!- DOMAIN: The RING-CH-type zinc finger domain is required for E3
ligase activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
-!- PTM: Has a short half-life. Instability/short half-life permits
rapid changes that allow efficient induction of antigen
presentation once antigen presenting cells, APCs, receive
maturation signals. Small changes in protein levels significantly
alter the cell surface display of MHC class II proteins.
-!- DISRUPTION PHENOTYPE: Shows increase in the cell surface
expression or half-life of MHC class II. Null cells have
accumulated MHC class II and CD86 at the cell surface and a low
antigen-presenting ability for exogenous antigens, in conventional
dendritic cells (PubMed:19917682). Null cells have high antigen-
presenting ability for exogenous antigens in B-cells
(PubMed:17255932). {ECO:0000269|PubMed:17255932,
ECO:0000269|PubMed:19917682}.
-----------------------------------------------------------------------
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EMBL; AK036489; BAC29449.1; -; mRNA.
EMBL; AK089040; BAC40715.1; -; mRNA.
EMBL; AK137337; BAE23311.1; -; mRNA.
EMBL; AK152592; BAE31341.1; -; mRNA.
EMBL; AK163081; BAE37183.1; -; mRNA.
EMBL; BC066008; AAH66008.1; -; mRNA.
CCDS; CCDS22333.1; -. [Q6NZQ8-3]
CCDS; CCDS52560.1; -. [Q6NZQ8-5]
CCDS; CCDS52561.1; -. [Q6NZQ8-4]
CCDS; CCDS80884.1; -. [Q6NZQ8-1]
RefSeq; NP_001159844.1; NM_001166372.1. [Q6NZQ8-5]
RefSeq; NP_001159847.1; NM_001166375.1. [Q6NZQ8-4]
RefSeq; NP_001280713.1; NM_001293784.1. [Q6NZQ8-1]
RefSeq; NP_780397.2; NM_175188.4. [Q6NZQ8-3]
RefSeq; XP_006509821.1; XM_006509758.1. [Q6NZQ8-3]
RefSeq; XP_017168467.1; XM_017312978.1. [Q6NZQ8-3]
UniGene; Mm.380457; -.
ProteinModelPortal; Q6NZQ8; -.
SMR; Q6NZQ8; -.
STRING; 10090.ENSMUSP00000072302; -.
iPTMnet; Q6NZQ8; -.
PhosphoSitePlus; Q6NZQ8; -.
PaxDb; Q6NZQ8; -.
PRIDE; Q6NZQ8; -.
Ensembl; ENSMUST00000039540; ENSMUSP00000044070; ENSMUSG00000036469. [Q6NZQ8-4]
Ensembl; ENSMUST00000072482; ENSMUSP00000072302; ENSMUSG00000036469. [Q6NZQ8-3]
Ensembl; ENSMUST00000098708; ENSMUSP00000096305; ENSMUSG00000036469. [Q6NZQ8-5]
Ensembl; ENSMUST00000110253; ENSMUSP00000105882; ENSMUSG00000036469. [Q6NZQ8-2]
Ensembl; ENSMUST00000110255; ENSMUSP00000105884; ENSMUSG00000036469. [Q6NZQ8-5]
Ensembl; ENSMUST00000110258; ENSMUSP00000105887; ENSMUSG00000036469. [Q6NZQ8-1]
Ensembl; ENSMUST00000110259; ENSMUSP00000105888; ENSMUSG00000036469. [Q6NZQ8-3]
Ensembl; ENSMUST00000178982; ENSMUSP00000136545; ENSMUSG00000036469. [Q6NZQ8-1]
GeneID; 72925; -.
KEGG; mmu:72925; -.
UCSC; uc009lvj.2; mouse. [Q6NZQ8-1]
UCSC; uc009lvk.2; mouse. [Q6NZQ8-5]
UCSC; uc009lvl.2; mouse. [Q6NZQ8-3]
UCSC; uc009lvm.2; mouse. [Q6NZQ8-2]
UCSC; uc009lvn.2; mouse. [Q6NZQ8-4]
CTD; 55016; -.
MGI; MGI:1920175; March1.
eggNOG; KOG1609; Eukaryota.
eggNOG; COG5183; LUCA.
GeneTree; ENSGT00920000148985; -.
HOGENOM; HOG000113483; -.
HOVERGEN; HBG081957; -.
InParanoid; Q6NZQ8; -.
KO; K10656; -.
OMA; RWRAYNR; -.
PhylomeDB; Q6NZQ8; -.
TreeFam; TF319557; -.
UniPathway; UPA00143; -.
ChiTaRS; March1; mouse.
PRO; PR:Q6NZQ8; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000036469; Expressed in 149 organ(s), highest expression level in retina.
CleanEx; MM_MARCH1; -.
ExpressionAtlas; Q6NZQ8; baseline and differential.
Genevisible; Q6NZQ8; MM.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
GO; GO:0042287; F:MHC protein binding; ISS:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0002495; P:antigen processing and presentation of peptide antigen via MHC class II; IMP:UniProtKB.
GO; GO:0006955; P:immune response; IDA:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA: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;
Alternative splicing; Complete proteome; Cytoplasmic vesicle;
Endosome; Golgi apparatus; Immunity; Lysosome; Membrane;
Metal-binding; Reference proteome; Transferase; Transmembrane;
Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 289 E3 ubiquitin-protein ligase MARCH1.
/FTId=PRO_0000274366.
TRANSMEM 155 175 Helical. {ECO:0000255}.
TRANSMEM 197 217 Helical. {ECO:0000255}.
ZN_FING 72 133 RING-CH-type. {ECO:0000255|PROSITE-
ProRule:PRU00623}.
REGION 1 66 Responsible for low stability.
REGION 222 279 Responsible for down-regulation of CD86
and MHC class II cell surface expression.
VAR_SEQ 1 54 MLGWCEAIARNPHRIPNTTRTPETSGDVADASQTSTLNEKS
PGRSASRSSNISK -> MNLTMSNMTSSHICCNFLNMWKKS
KISTMYYLNQDAKLSNLFLQ (in isoform 2 and
isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_022726.
VAR_SEQ 1 37 MLGWCEAIARNPHRIPNTTRTPETSGDVADASQTSTL ->
MPLHQISVIPARETASNGRSSMGRNKEKNKEVE (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022727.
VAR_SEQ 187 190 Missing (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_022728.
MUTAGEN 114 114 W->A: Loss of ubiquitin ligase activity
and loss of down-regulation of CD86 cell
surface expression.
{ECO:0000269|PubMed:19880452}.
MUTAGEN 225 225 L->S: Partial loss of down-regulation of
CD86 cell surface expression. Almost
complete loss of down-regulation of CD86
cell surface expression; when associated
with F-232.
{ECO:0000269|PubMed:19880452}.
MUTAGEN 232 232 Y->F: Almost complete loss of down-
regulation of CD86 cell surface
expression; when associated with S-225.
{ECO:0000269|PubMed:19880452}.
CONFLICT 85 85 C -> Y (in Ref. 1; BAE31341).
{ECO:0000305}.
SEQUENCE 289 AA; 32347 MW; 0DBE9A308D5ED0CE CRC64;
MLGWCEAIAR NPHRIPNTTR TPETSGDVAD ASQTSTLNEK SPGRSASRSS NISKASSPTT
GTAPRSQSRL SVCPSTQDIC RICHCEGDEE SPLITPCRCT GTLRFVHQSC LHQWIKSSDT
RCCELCKYDF IMETKLKPLR KWEKLQMTTS ERRKIFCSVT FHVIAVTCVV WSLYVLIDRT
AEEIKQGNDN GVLEWPFWTK LVVVAIGFTG GLVFMYVQCK VYVQLWRRLK AYNRVIFVQN
CPDTANKLEK NFPCNVNTEI KDAVVVPVPQ TGSNTLPTAE GAPPEVIPV


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