MARHB_HUMAN
ID MARHB_HUMAN Reviewed; 402 AA.
AC A6NNE9; A7E2S6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 3.
DT 03-AUG-2022, entry version 112.
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 {ECO:0000312|HGNC:HGNC:33609}; Synonyms=MARCH11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 40-402 (ISOFORM 1).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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=A6NNE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6NNE9-2; Sequence=VSP_034147;
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; AC092335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC150513; AAI50514.1; -; mRNA.
DR EMBL; BC150514; AAI50515.1; -; mRNA.
DR EMBL; CR590337; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS47192.1; -. [A6NNE9-1]
DR RefSeq; NP_001096032.1; NM_001102562.1. [A6NNE9-1]
DR AlphaFoldDB; A6NNE9; -.
DR STRING; 9606.ENSP00000333181; -.
DR iPTMnet; A6NNE9; -.
DR PhosphoSitePlus; A6NNE9; -.
DR BioMuta; MARCH11; -.
DR MassIVE; A6NNE9; -.
DR PaxDb; A6NNE9; -.
DR PeptideAtlas; A6NNE9; -.
DR PRIDE; A6NNE9; -.
DR ProteomicsDB; 1603; -. [A6NNE9-1]
DR ProteomicsDB; 1604; -. [A6NNE9-2]
DR Antibodypedia; 3060; 100 antibodies from 14 providers.
DR DNASU; 441061; -.
DR Ensembl; ENST00000332432.9; ENSP00000333181.7; ENSG00000183654.9. [A6NNE9-1]
DR GeneID; 441061; -.
DR KEGG; hsa:441061; -.
DR MANE-Select; ENST00000332432.9; ENSP00000333181.7; NM_001102562.3; NP_001096032.1.
DR UCSC; uc003jfo.3; human. [A6NNE9-1]
DR CTD; 441061; -.
DR DisGeNET; 441061; -.
DR GeneCards; MARCHF11; -.
DR HGNC; HGNC:33609; MARCHF11.
DR HPA; ENSG00000183654; Tissue enriched (testis).
DR MIM; 613338; gene.
DR neXtProt; NX_A6NNE9; -.
DR OpenTargets; ENSG00000183654; -.
DR VEuPathDB; HostDB:ENSG00000183654; -.
DR eggNOG; KOG1609; Eukaryota.
DR GeneTree; ENSGT00940000160025; -.
DR HOGENOM; CLU_045217_2_1_1; -.
DR InParanoid; A6NNE9; -.
DR OMA; NRIRPHE; -.
DR OrthoDB; 1014283at2759; -.
DR PhylomeDB; A6NNE9; -.
DR TreeFam; TF319557; -.
DR PathwayCommons; A6NNE9; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 441061; 6 hits in 1066 CRISPR screens.
DR ChiTaRS; MARCH11; human.
DR GenomeRNAi; 441061; -.
DR Pharos; A6NNE9; Tbio.
DR PRO; PR:A6NNE9; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; A6NNE9; protein.
DR Bgee; ENSG00000183654; Expressed in sperm and 98 other tissues.
DR ExpressionAtlas; A6NNE9; baseline and differential.
DR Genevisible; A6NNE9; HS.
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..402
FT /note="E3 ubiquitin-protein ligase MARCHF11"
FT /id="PRO_0000339344"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 162..222
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT REGION 1..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 371..374
FT /note="YXXL motif"
FT MOTIF 399..402
FT /note="PDZ-binding"
FT COMPBIAS 20..58
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT VAR_SEQ 1..244
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034147"
SQ SEQUENCE 402 AA; 43878 MW; 8040B7DCE9277601 CRC64;
MSFEGGHGGS RCRGAESGDA EPPPQPPPPP PPTPPPGEPA PVPAAPRYLP PLPASPETPE
RAAGPSEPLG EVAPRCRGAD ELPPPPLPLQ PAGQEVAAAG DSGEGPRRLP EAAAAKGGPG
ESEAGAGGER ERRGAGDQPE TRSVCSSRSS SSGGGDQRAG HQHQHHQPIC KICFQGAEQG
ELLNPCRCDG SVRYTHQLCL LKWISERGSW TCELCCYRYH VIAIKMKQPC QWQSISITLV
EKVQMIAVIL GSLFLIASVT WLLWSAFSPY AVWQRKDILF QICYGMYGFM DLVCIGLIVH
EGAAVYRVFK RWRAVNLHWD VLNYDKATDI EESSRGESST SRTLWLPLTA LRNRNLVHPT
QLTSPRFQCG YVLLHLFNRM RPHEDLSEDN SSGEVVMRVT SV
