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Protein

E3 ubiquitin-protein ligase MARCH11

Gene

March11

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase that mediates polyubiquitination of CD4. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May play a role in ubuquitin-dependent protein sorting in developmenting spermatids.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri158 – 21861RING-CH-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase MARCH11 (EC:6.3.2.-)
Alternative name(s):
Membrane-associated RING finger protein 11
Membrane-associated RING-CH protein XI
Short name:
MARCH-XI
Gene namesi
Name:March11
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1559945. March11.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei241 – 26121HelicalSequence analysisAdd
BLAST
Transmembranei274 – 29421HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi169 – 1691C → S: Abolishes ubiquitin ligase activity; when associated with S-182 and S-184. 1 Publication
Mutagenesisi182 – 1821C → S: Abolishes ubiquitin ligase activity; when associated with S-169 and C-184. 1 Publication
Mutagenesisi184 – 1841C → S: Abolishes ubiquitin ligase activity; when associated with S-169 and C-182. 1 Publication
Mutagenesisi367 – 3671Y → A: Abolishes interaction with AP1M1. 1 Publication
Mutagenesisi398 – 3981Missing : LIN7A. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 398398E3 ubiquitin-protein ligase MARCH11PRO_0000339346Add
BLAST

Proteomic databases

PaxDbiA6P320.

Expressioni

Tissue specificityi

Predominantly expressed in testis. Present in early developing spermatids. Not present in spermatogonia, spermatocytes or somatic cells (i.e. peritubular, Leydig, and Sertoli cells). Present in early round spermatids at step 4, remains until step 11, then it decreases at steps 12-15, and diminishes after step 16 (at protein level). Also expressed at lower level in brain.1 Publication

Interactioni

Subunit structurei

Interacts (YXXL motif) with AP1M1. Interacts (via PDZ-binding motif) with LIN7A. Interacts with unidentified fucose glycoproteins.1 Publication

Protein-protein interaction databases

BioGridi270867. 3 interactions.
STRINGi10116.ENSRNOP00000035881.

Structurei

3D structure databases

ProteinModelPortaliA6P320.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi367 – 3704YXXL motif
Motifi395 – 3984PDZ-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi19 – 8163Pro-richAdd
BLAST
Compositional biasi141 – 1477Poly-Ser

Domaini

The RING-CH-type zinc finger domain is required for E3 ligase activity.

Sequence similaritiesi

Contains 1 RING-CH-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri158 – 21861RING-CH-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG1609. Eukaryota.
COG5183. LUCA.
HOGENOMiHOG000113484.
HOVERGENiHBG052412.
InParanoidiA6P320.
KOiK10659.
PhylomeDBiA6P320.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR033275. MARCH-like.
IPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR23012. PTHR23012. 2 hits.
PfamiPF12906. RINGv. 1 hit.
[Graphical view]
SMARTiSM00744. RINGv. 1 hit.
[Graphical view]
PROSITEiPS51292. ZF_RING_CH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A6P320-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDEGSKRGS RADSLEAEPP LPPPPPPPPP GESSLVPTSP RYRPPLPAPL
60 70 80 90 100
ERIVGSGEPP VELAPRRKGE PLPPLPPSRL PGDQEVSAAG DSCEGPRRLP
110 120 130 140 150
EVKLPEAAAG KGSPAEPEAG ACREGERRGT GDQPETRSVY SSRSSSSGGS
160 170 180 190 200
GDQRSGHQHQ HHQPICKICF QGAEQGELLN PCRCDGSVRY THQLCLLKWI
210 220 230 240 250
SERGSWTCEL CCYRYHVTAI KMKQPCQWQS ISITLVEKVQ MIAVILGSLF
260 270 280 290 300
LIASVTWLLW SAFSPYAVWQ RKDILFQICY GMYGFMDLVC IGLIVHEGAA
310 320 330 340 350
VYRVFKRWRA VNLHWDVLNY DKATDIEESS RGESSTSRTL WLPLSALRNR
360 370 380 390
NLVHPTQLTS PRFQCGYVLL HLFNRMRAHE DVSEDNGSGE VVMRVTSV
Length:398
Mass (Da):44,085
Last modified:August 21, 2007 - v1
Checksum:iEB3CC606A44DE800
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB048841 mRNA. Translation: BAF68985.1.
RefSeqiNP_001095298.1. NM_001101828.1.
UniGeneiRn.206431.

Genome annotation databases

GeneIDi499558.
KEGGirno:499558.
UCSCiRGD:1559945. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB048841 mRNA. Translation: BAF68985.1.
RefSeqiNP_001095298.1. NM_001101828.1.
UniGeneiRn.206431.

3D structure databases

ProteinModelPortaliA6P320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi270867. 3 interactions.
STRINGi10116.ENSRNOP00000035881.

Proteomic databases

PaxDbiA6P320.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi499558.
KEGGirno:499558.
UCSCiRGD:1559945. rat.

Organism-specific databases

CTDi441061.
RGDi1559945. March11.

Phylogenomic databases

eggNOGiKOG1609. Eukaryota.
COG5183. LUCA.
HOGENOMiHOG000113484.
HOVERGENiHBG052412.
InParanoidiA6P320.
KOiK10659.
PhylomeDBiA6P320.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiA6P320.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR033275. MARCH-like.
IPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR23012. PTHR23012. 2 hits.
PfamiPF12906. RINGv. 1 hit.
[Graphical view]
SMARTiSM00744. RINGv. 1 hit.
[Graphical view]
PROSITEiPS51292. ZF_RING_CH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "MARCH-XI, a novel transmembrane ubiquitin ligase implicated in ubiquitin-dependent protein sorting in developing spermatids."
    Morokuma Y., Nakamura N., Kato A., Notoya M., Yamamoto Y., Sakai Y., Fukuda H., Yamashina S., Hirata Y., Hirose S.
    J. Biol. Chem. 282:24806-24815(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH AP1M1 AND LIN7A, MUTAGENESIS OF CYS-169; CYS-182; CYS-184; TYR-367 AND VAL-398.
    Tissue: Testis.

Entry informationi

Entry nameiMARHB_RAT
AccessioniPrimary (citable) accession number: A6P320
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: August 21, 2007
Last modified: June 8, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.