MARHB_MOUSE
ID MARHB_MOUSE Reviewed; 400 AA.
AC Q8CBH7; B9EIG0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=E3 ubiquitin-protein ligase MARCHF11;
DE EC=2.3.2.27;
DE AltName: Full=Membrane-associated RING finger protein 11;
DE AltName: Full=Membrane-associated RING-CH protein XI;
DE Short=MARCH-XI;
DE AltName: Full=RING-type E3 ubiquitin transferase MARCHF11 {ECO:0000305};
GN Name=Marchf11; Synonyms=March11;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates polyubiquitination
CC of CD4. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-
CC conjugating enzyme in the form of a thioester and then directly
CC transfer the ubiquitin to targeted substrates. May play a role in
CC ubuquitin-dependent protein sorting in developmenting spermatids.
CC {ECO:0000250|UniProtKB:A6P320}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts (YXXL motif) with AP1M1. Interacts (via PDZ-binding
CC motif) with LIN7A. Interacts with unidentified fucose glycoproteins.
CC {ECO:0000250|UniProtKB:A6P320}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:A6P320}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:A6P320}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CBH7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CBH7-2; Sequence=VSP_034148, VSP_034149;
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
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DR EMBL; AK035990; BAC29270.1; -; mRNA.
DR EMBL; AC102845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC139422; AAI39423.1; -; mRNA.
DR EMBL; BC139423; AAI39424.1; -; mRNA.
DR CCDS; CCDS27401.2; -. [Q8CBH7-1]
DR RefSeq; NP_001297703.1; NM_001310774.1.
DR RefSeq; NP_808265.2; NM_177597.6. [Q8CBH7-1]
DR AlphaFoldDB; Q8CBH7; -.
DR SMR; Q8CBH7; -.
DR BioGRID; 229207; 1.
DR STRING; 10090.ENSMUSP00000118729; -.
DR iPTMnet; Q8CBH7; -.
DR PhosphoSitePlus; Q8CBH7; -.
DR PaxDb; Q8CBH7; -.
DR PRIDE; Q8CBH7; -.
DR ProteomicsDB; 252734; -. [Q8CBH7-1]
DR ProteomicsDB; 252735; -. [Q8CBH7-2]
DR Antibodypedia; 3060; 100 antibodies from 14 providers.
DR DNASU; 211147; -.
DR Ensembl; ENSMUST00000126304; ENSMUSP00000153852; ENSMUSG00000022269. [Q8CBH7-2]
DR Ensembl; ENSMUST00000140840; ENSMUSP00000118729; ENSMUSG00000022269. [Q8CBH7-1]
DR GeneID; 211147; -.
DR KEGG; mmu:211147; -.
DR UCSC; uc007vjl.2; mouse. [Q8CBH7-2]
DR UCSC; uc011zrq.1; mouse. [Q8CBH7-1]
DR CTD; 441061; -.
DR MGI; MGI:3608327; Marchf11.
DR VEuPathDB; HostDB:ENSMUSG00000022269; -.
DR eggNOG; KOG1609; Eukaryota.
DR GeneTree; ENSGT00940000160025; -.
DR HOGENOM; CLU_045217_2_1_1; -.
DR InParanoid; Q8CBH7; -.
DR OMA; NRIRPHE; -.
DR OrthoDB; 1014283at2759; -.
DR PhylomeDB; Q8CBH7; -.
DR TreeFam; TF319557; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 211147; 0 hits in 52 CRISPR screens.
DR ChiTaRS; March11; mouse.
DR PRO; PR:Q8CBH7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8CBH7; protein.
DR Bgee; ENSMUSG00000022269; Expressed in seminiferous tubule of testis and 94 other tissues.
DR ExpressionAtlas; Q8CBH7; baseline and differential.
DR Genevisible; Q8CBH7; MM.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR046356; MARCHF4/9/11.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46053; PTHR46053; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasmic vesicle; Membrane; Metal-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..400
FT /note="E3 ubiquitin-protein ligase MARCHF11"
FT /id="PRO_0000339345"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 160..220
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT REGION 1..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 369..372
FT /note="YXXL motif"
FT MOTIF 397..400
FT /note="PDZ-binding"
FT COMPBIAS 17..47
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT VAR_SEQ 230..252
FT /note="WQSISITLVEKVQMIAVILGSLF -> VDTMFTLPGIILLTRVHLNFVLA
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034148"
FT VAR_SEQ 253..400
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034149"
SQ SEQUENCE 400 AA; 44223 MW; A3C5DB5378B3CDC3 CRC64;
MSDEGKKRSS RADSLEAEPP LPPPPPPPPP GESVLVPTSP RYRPPLPAPL ERIVGSGEPP
VELAPRRKGA GEPLPPLPPS LLPGDQEVTA AGDSCEGPRR LPEVKLPEAA TGKGSPGEPE
AGACREGERR GTGDQPETRS VCSSRSSSSG GGSDQRSGHQ HQHHQPICKI CFQGAEQGEL
LNPCRCDGSV RYTHQLCLLK WISERGSWTC ELCCYRYHVT AIKMKQPCQW QSISITLVEK
VQMIAVILGS LFLIASVTWL LWSAFSPYAV WQRKDILFQI CYGMYGFMDL VCIGLIVHEG
AAVYRVFKRW RAVNLHWDVL NYDKATDIEE SSRGESSTSR TLWLPLSALR NRNLVHPTQL
TSPRFQCGYV LLHLFNRMRA HEDVSEDNGS GEVVMRVTSV
