ID MARH1_HUMAN Reviewed; 289 AA.
AC Q8TCQ1; D3DP29; Q9NWR0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 18-JAN-2017, entry version 125.
DE RecName: Full=E3 ubiquitin-protein ligase MARCH1;
DE EC=2.3.2.27;
DE AltName: Full=Membrane-associated RING finger protein 1;
DE AltName: Full=Membrane-associated RING-CH protein I;
DE Short=MARCH-I;
DE AltName: Full=RING finger protein 171;
DE AltName: Full=RING-type E3 ubiquitin transferase MARCH1 {ECO:0000305};
GN Name=MARCH1; Synonyms=RNF171;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ileal mucosa;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=14722266; DOI=10.1128/JVI.78.3.1109-1120.2004;
RA Bartee E., Mansouri M., Hovey Nerenberg B.T., Gouveia K., Frueh K.;
RT "Downregulation of major histocompatibility complex class I by human
RT ubiquitin ligases related to viral immune evasion proteins.";
RL J. Virol. 78:1109-1120(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=17255932; DOI=10.1038/sj.emboj.7601556;
RA Matsuki Y., Ohmura-Hoshino M., Goto E., Aoki M., Mito-Yoshida M.,
RA Uematsu M., Hasegawa T., Koseki H., Ohara O., Nakayama M., Toyooka K.,
RA Matsuoka K., Hotta H., Yamamoto A., Ishido S.;
RT "Novel regulation of MHC class II function in B cells.";
RL EMBO J. 26:846-854(2007).
RN [6]
RP FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DR BETA, AND INDUCTION BY
RP IL10.
RX PubMed=18389477; DOI=10.1002/eji.200737902;
RA Thibodeau J., Bourgeois-Daigneault M.C., Huppe G., Tremblay J.,
RA Aumont A., Houde M., Bartee E., Brunet A., Gauvreau M.E.,
RA de Gassart A., Gatti E., Baril M., Cloutier M., Bontron S., Fruh K.,
RA Lamarre D., Steimle V.;
RT "Interleukin-10-induced MARCH1 mediates intracellular sequestration of
RT MHC class II in monocytes.";
RL Eur. J. Immunol. 38:1225-1230(2008).
RN [7]
RP FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DR BETA.
RX PubMed=18305173; DOI=10.1073/pnas.0708874105;
RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N.,
RA Pierre P., Gatti E.;
RT "MHC class II stabilization at the surface of human dendritic cells is
RT the result of maturation-dependent MARCH I down-regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008).
RN [8]
RP FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DR ALPHA AND BETA, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19117940; DOI=10.1074/jbc.M805736200;
RA Lapaque N., Jahnke M., Trowsdale J., Kelly A.P.;
RT "The HLA-DRalpha chain is modified by polyubiquitination.";
RL J. Biol. Chem. 284:7007-7016(2009).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
CC of TFRC, CD86, FAS and MHC class II proteins, such as HLA-DR alpha
CC and beta, and promotes their subsequent endocytosis and sorting to
CC lysosomes via multivesicular bodies. By constitutively
CC ubiquitinating MHC class II proteins in immature dendritic cells,
CC down-regulates their cell surface localization thus sequestering
CC them in the intracellular endosomal system.
CC {ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:18305173,
CC ECO:0000269|PubMed:18389477, ECO:0000269|PubMed:19117940}.
CC -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
CC enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
CC conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
CC protein]-L-lysine.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000250|UniProtKB:Q6NZQ8}; Multi-pass membrane
CC protein {ECO:0000255}. Lysosome membrane
CC {ECO:0000269|PubMed:14722266}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000255}. Late endosome membrane
CC {ECO:0000269|PubMed:19117940}; Multi-pass membrane protein
CC {ECO:0000255}. Early endosome membrane
CC {ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:19117940}; Multi-
CC pass membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000269|PubMed:19117940}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TCQ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TCQ1-2; Sequence=VSP_022724, VSP_022725;
CC -!- TISSUE SPECIFICITY: Expressed in antigen presenting cells, APCs,
CC located in lymph nodes and spleen. Also expressed in lung.
CC Expression is high in follicular B-cells, moderate in dendritic
CC cells and low in splenic T-cells. {ECO:0000269|PubMed:14722266,
CC ECO:0000269|PubMed:17255932}.
CC -!- DEVELOPMENTAL STAGE: During maturation of dendritic cells,
CC expression is down-regulated and stabilizes MHC class II proteins
CC accumulate at the plasma membrane.
CC -!- INDUCTION: By IL10/interleukin-10. {ECO:0000269|PubMed:18389477}.
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3
CC ligase activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
CC -!- PTM: Has a short half-life. Instability/short half-life permits
CC rapid changes that allow efficient induction of antigen
CC presentation once antigen presenting cells, APCs, receive
CC maturation signals. Small changes in protein levels significantly
CC alter the cell surface display of MHC class II proteins (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Contains 1 RING-CH-type zinc finger.
CC {ECO:0000255|PROSITE-ProRule:PRU00623}.
DR EMBL; AK000675; BAA91319.1; -; mRNA.
DR EMBL; AL713759; CAD28529.1; -; mRNA.
DR EMBL; CH471056; EAX04835.1; -; Genomic_DNA.
DR CCDS; CCDS3806.1; -. [Q8TCQ1-2]
DR CCDS; CCDS54814.1; -. [Q8TCQ1-1]
DR RefSeq; NP_001159845.1; NM_001166373.1. [Q8TCQ1-1]
DR RefSeq; NP_060393.1; NM_017923.3. [Q8TCQ1-2]
DR RefSeq; XP_016863823.1; XM_017008334.1. [Q8TCQ1-1]
DR UniGene; Hs.592804; -.
DR UniGene; Hs.608487; -.
DR ProteinModelPortal; Q8TCQ1; -.
DR SMR; Q8TCQ1; -.
DR BioGrid; 120348; 10.
DR STRING; 9606.ENSP00000274056; -.
DR iPTMnet; Q8TCQ1; -.
DR PhosphoSitePlus; Q8TCQ1; -.
DR BioMuta; MARCH1; -.
DR DMDM; 74762613; -.
DR EPD; Q8TCQ1; -.
DR PaxDb; Q8TCQ1; -.
DR PeptideAtlas; Q8TCQ1; -.
DR PRIDE; Q8TCQ1; -.
DR DNASU; 55016; -.
DR Ensembl; ENST00000274056; ENSP00000274056; ENSG00000145416. [Q8TCQ1-1]
DR Ensembl; ENST00000339875; ENSP00000345676; ENSG00000145416. [Q8TCQ1-2]
DR Ensembl; ENST00000503008; ENSP00000427223; ENSG00000145416. [Q8TCQ1-1]
DR GeneID; 55016; -.
DR KEGG; hsa:55016; -.
DR UCSC; uc003iqr.3; human. [Q8TCQ1-1]
DR CTD; 55016; -.
DR DisGeNET; 55016; -.
DR GeneCards; MARCH1; -.
DR HGNC; HGNC:26077; MARCH1.
DR HPA; HPA014600; -.
DR MIM; 613331; gene.
DR neXtProt; NX_Q8TCQ1; -.
DR OpenTargets; ENSG00000145416; -.
DR PharmGKB; PA134986392; -.
DR eggNOG; KOG1609; Eukaryota.
DR eggNOG; COG5183; LUCA.
DR GeneTree; ENSGT00730000110355; -.
DR HOGENOM; HOG000113483; -.
DR HOVERGEN; HBG081957; -.
DR InParanoid; Q8TCQ1; -.
DR KO; K10656; -.
DR OMA; ERRKICC; -.
DR PhylomeDB; Q8TCQ1; -.
DR TreeFam; TF319557; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; MARCH1; human.
DR GenomeRNAi; 55016; -.
DR PRO; PR:Q8TCQ1; -.
DR Proteomes; UP000005640; Chromosome 4.
DR Bgee; ENSG00000145416; -.
DR CleanEx; HS_MARCH1; -.
DR ExpressionAtlas; Q8TCQ1; baseline and differential.
DR Genevisible; Q8TCQ1; HS.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0042287; F:MHC protein binding; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002495; P:antigen processing and presentation of peptide antigen via MHC class II; IDA:UniProtKB.
DR GO; GO:0006955; P:immune response; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR033275; MARCH-like.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23012; PTHR23012; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome;
KW Cytoplasmic vesicle; Endosome; Golgi apparatus; Immunity; Lysosome;
KW Membrane; Metal-binding; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1 289 E3 ubiquitin-protein ligase MARCH1.
FT /FTId=PRO_0000274365.
FT TRANSMEM 155 175 Helical. {ECO:0000255}.
FT TRANSMEM 197 217 Helical. {ECO:0000255}.
FT ZN_FING 72 133 RING-CH-type. {ECO:0000255|PROSITE-
FT ProRule:PRU00623}.
FT REGION 1 66 Responsible for low stability.
FT {ECO:0000250}.
FT REGION 222 279 Responsible for down-regulation of CD86
FT and MHC class II cell surface expression.
FT {ECO:0000250}.
FT VAR_SEQ 1 18 Missing (in isoform 2).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_022724.
FT VAR_SEQ 19 54 TRTPEISGDLADASQTSTLNEKSPGRSASRSSNISK -> M
FT TSSHVCCNFLNMWKKSKISTMYYLNQDAKLSNLFLQ (in
FT isoform 2).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_022725.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 79 127 ismart:RINGv [T]
FT MYHIT 72 133 iprf:ZF_RING_CH [T]
FT MYHIT 80 126 ipfam:RINGv [T]
SQ SEQUENCE 289 AA; 32308 MW; 923E1809AB3D7087 CRC64;
MLGWCEAIAR NPHRIPNNTR TPEISGDLAD ASQTSTLNEK SPGRSASRSS NISKASSPTT
GTAPRSQSRL SVCPSTQDIC RICHCEGDEE SPLITPCRCT GTLRFVHQSC LHQWIKSSDT
RCCELCKYDF IMETKLKPLR KWEKLQMTTS ERRKIFCSVT FHVIAITCVV WSLYVLIDRT
AEEIKQGNDN GVLEWPFWTK LVVVAIGFTG GLVFMYVQCK VYVQLWRRLK AYNRVIFVQN
CPDTAKKLEK NFSCNVNTDI KDAVVVPVPQ TGANSLPSAE GGPPEVVSV
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