MARHB_RAT
ID MARHB_RAT Reviewed; 398 AA.
AC A6P320;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INTERACTION WITH AP1M1 AND LIN7A, AND MUTAGENESIS OF CYS-169;
RP CYS-182; CYS-184; TYR-367 AND VAL-398.
RC TISSUE=Testis;
RX PubMed=17604280; DOI=10.1074/jbc.m700414200;
RA Morokuma Y., Nakamura N., Kato A., Notoya M., Yamamoto Y., Sakai Y.,
RA Fukuda H., Yamashina S., Hirata Y., Hirose S.;
RT "MARCH-XI, a novel transmembrane ubiquitin ligase implicated in ubiquitin-
RT dependent protein sorting in developing spermatids.";
RL J. Biol. Chem. 282:24806-24815(2007).
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:0000269|PubMed:17604280}.
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:0000269|PubMed:17604280}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:17604280}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17604280}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis. Present in early
CC developing spermatids. Not present in spermatogonia, spermatocytes or
CC somatic cells (i.e. peritubular, Leydig, and Sertoli cells). Present in
CC early round spermatids at step 4, remains until step 11, then it
CC decreases at steps 12-15, and diminishes after step 16 (at protein
CC level). Also expressed at lower level in brain.
CC {ECO:0000269|PubMed:17604280}.
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC activity.
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DR EMBL; AB048841; BAF68985.1; -; mRNA.
DR RefSeq; NP_001095298.1; NM_001101828.1.
DR AlphaFoldDB; A6P320; -.
DR BioGRID; 270867; 3.
DR STRING; 10116.ENSRNOP00000035881; -.
DR PaxDb; A6P320; -.
DR GeneID; 499558; -.
DR KEGG; rno:499558; -.
DR UCSC; RGD:1559945; rat.
DR CTD; 441061; -.
DR RGD; 1559945; March11.
DR eggNOG; KOG1609; Eukaryota.
DR InParanoid; A6P320; -.
DR OrthoDB; 1014283at2759; -.
DR PhylomeDB; A6P320; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:A6P320; -.
DR Proteomes; UP000002494; Unplaced.
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 1: Evidence at protein level;
KW Cytoplasmic vesicle; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..398
FT /note="E3 ubiquitin-protein ligase MARCHF11"
FT /id="PRO_0000339346"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 158..218
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT REGION 1..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 367..370
FT /note="YXXL motif"
FT MOTIF 395..398
FT /note="PDZ-binding"
FT COMPBIAS 17..47
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT MUTAGEN 169
FT /note="C->S: Abolishes ubiquitin ligase activity; when
FT associated with S-182 and S-184."
FT /evidence="ECO:0000269|PubMed:17604280"
FT MUTAGEN 182
FT /note="C->S: Abolishes ubiquitin ligase activity; when
FT associated with S-169 and C-184."
FT /evidence="ECO:0000269|PubMed:17604280"
FT MUTAGEN 184
FT /note="C->S: Abolishes ubiquitin ligase activity; when
FT associated with S-169 and C-182."
FT /evidence="ECO:0000269|PubMed:17604280"
FT MUTAGEN 367
FT /note="Y->A: Abolishes interaction with AP1M1."
FT /evidence="ECO:0000269|PubMed:17604280"
FT MUTAGEN 398
FT /note="Missing: LIN7A."
FT /evidence="ECO:0000269|PubMed:17604280"
SQ SEQUENCE 398 AA; 44085 MW; EB3CC606A44DE800 CRC64;
MSDEGSKRGS RADSLEAEPP LPPPPPPPPP GESSLVPTSP RYRPPLPAPL ERIVGSGEPP
VELAPRRKGE PLPPLPPSRL PGDQEVSAAG DSCEGPRRLP EVKLPEAAAG KGSPAEPEAG
ACREGERRGT GDQPETRSVY SSRSSSSGGS GDQRSGHQHQ HHQPICKICF QGAEQGELLN
PCRCDGSVRY THQLCLLKWI SERGSWTCEL CCYRYHVTAI KMKQPCQWQS ISITLVEKVQ
MIAVILGSLF LIASVTWLLW SAFSPYAVWQ RKDILFQICY GMYGFMDLVC IGLIVHEGAA
VYRVFKRWRA VNLHWDVLNY DKATDIEESS RGESSTSRTL WLPLSALRNR NLVHPTQLTS
PRFQCGYVLL HLFNRMRAHE DVSEDNGSGE VVMRVTSV
