Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Moesin/ezrin/radixin homolog 1

Gene

Moe

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in connections of major cytoskeletal structures to the plasma membrane (PubMed:8666669). Together with wgn, involved in control of axon targeting of R8 and R2-R5 photoreceptors, independent of egr (PubMed:23544124).2 Publications

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • cytoskeletal protein binding Source: FlyBase
  • identical protein binding Source: IntAct
  • microtubule binding Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate binding Source: FlyBase

GO - Biological processi

  • actin cytoskeleton organization Source: FlyBase
  • actin filament-based process Source: FlyBase
  • anterior/posterior pattern specification Source: FlyBase
  • assembly of actomyosin apparatus involved in cytokinesis Source: FlyBase
  • cell morphogenesis Source: FlyBase
  • cortical actin cytoskeleton organization Source: FlyBase
  • cortical actin cytoskeleton stabilization Source: FlyBase
  • cortical microtubule organization Source: UniProtKB
  • cytoskeleton organization Source: FlyBase
  • determination of left/right symmetry Source: FlyBase
  • establishment of mitotic spindle orientation Source: FlyBase
  • establishment or maintenance of apical/basal cell polarity Source: FlyBase
  • establishment or maintenance of epithelial cell apical/basal polarity Source: UniProtKB
  • establishment or maintenance of polarity of larval imaginal disc epithelium Source: FlyBase
  • eye photoreceptor cell development Source: FlyBase
  • lumen formation, open tracheal system Source: FlyBase
  • male courtship behavior, veined wing generated song production Source: FlyBase
  • metaphase/anaphase transition of mitotic cell cycle Source: FlyBase
  • microtubule anchoring Source: UniProtKB
  • mitotic spindle organization Source: FlyBase
  • morphogenesis of an epithelium Source: FlyBase
  • olfactory behavior Source: FlyBase
  • oocyte anterior/posterior axis specification Source: FlyBase
  • photoreceptor cell axon guidance Source: FlyBase
  • pole plasm assembly Source: FlyBase
  • pole plasm protein localization Source: FlyBase
  • positive regulation of cell proliferation Source: FlyBase
  • positive regulation of endocytosis Source: FlyBase
  • positive regulation of mitotic spindle elongation Source: UniProtKB
  • protein localization Source: FlyBase
  • regulation of actin cytoskeleton organization Source: FlyBase
  • regulation of cell shape Source: UniProtKB
  • regulation of membrane potential in photoreceptor cell Source: FlyBase
  • rhabdomere development Source: FlyBase
  • rhabdomere membrane biogenesis Source: FlyBase
  • spindle localization Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Neurogenesis

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Moesin/ezrin/radixin homolog 1
Short name:
Ezrin-moesin-radixin 1
Alternative name(s):
Moesin
Short name:
dMoesin
Protein D17
Gene namesi
Name:Moe
Synonyms:EMR1
ORF Names:CG10701
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0011661. Moe.

Subcellular locationi

GO - Cellular componenti

  • adherens junction Source: UniProtKB
  • apical plasma membrane Source: FlyBase
  • cell cortex Source: FlyBase
  • cleavage furrow Source: FlyBase
  • cytoplasm Source: FlyBase
  • cytosol Source: UniProtKB
  • extrinsic component of membrane Source: InterPro
  • mitotic spindle midzone Source: FlyBase
  • nucleus Source: FlyBase
  • plasma membrane Source: UniProtKB
  • subapical complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 578578Moesin/ezrin/radixin homolog 1PRO_0000219425Add
BLAST

Proteomic databases

PRIDEiP46150.

Expressioni

Tissue specificityi

Expressed in apical and basolateral ends of follicular epithelium during oogenesis. In embryonic CNS, expression is seen in the neuropil, developing brain and neuronal cell bodies. In embryonic PNS, expression is seen at the cell membrane. In third instar larvae, eye imaginal disk expression is seen at the membranes of developing photoreceptors posterior to the morphogenetic furrow. In pupal eyes, expression is at the membrane of cone cells, secondary and tertiary pigment cells, bristle precursor cells and rhabdomeres.1 Publication

Gene expression databases

BgeeiP46150.
GenevisibleiP46150. DM.

Interactioni

Subunit structurei

Interacts with wgn (PubMed:23544124). Interacts with Mer and arm at the adherens junction (PubMed:8666669). Interacts with cytoskeletal actin at apical buds of microvilli in the precellularised embryo (PubMed:8666669).2 Publications

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • cytoskeletal protein binding Source: FlyBase
  • identical protein binding Source: IntAct
  • microtubule binding Source: UniProtKB

Protein-protein interaction databases

BioGridi58274. 123 interactions.
DIPiDIP-52150N.
IntActiP46150. 14 interactions.

Structurei

3D structure databases

ProteinModelPortaliP46150.
SMRiP46150. Positions 4-578.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 296296FERMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00830000128251.
InParanoidiP46150.
OMAiMLHAENV.
OrthoDBiEOG7BGHK6.
PhylomeDBiP46150.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
IPR011174. ERM.
IPR011259. ERM_C_dom.
IPR000798. Ez/rad/moesin-like.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR008954. Moesin_tail.
IPR011993. PH_dom-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view]
PIRSFiPIRSF002305. ERM. 1 hit.
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform J (identifier: P46150-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSPKALNVRV TTMDAELEFA IQSTTTGKQL FDQVVKTIGL REVWFFGLQY
60 70 80 90 100
TDSKGDSTWI KLYKKVMNQD VKKENPLQFR FRAKFYPEDV AEELIQDITL
110 120 130 140 150
RLFYLQVKNA ILTDEIYCPP ETSVLLASYA VQARHGDHNK TTHTAGFLAN
160 170 180 190 200
DRLLPQRVID QHKMSKDEWE QSIMTWWQEH RSMLREDAMM EYLKIAQDLE
210 220 230 240 250
MYGVNYFEIR NKKGTDLWLG VDALGLNIYE QDDRLTPKIG FPWSEIRNIS
260 270 280 290 300
FSEKKFIIKP IDKKAPDFMF FAPRVRINKR ILALCMGNHE LYMRRRKPDT
310 320 330 340 350
IDVQQMKAQA REEKNAKQQE REKLQLALAA RERAEKKQQE YEDRLKQMQE
360 370 380 390 400
DMERSQRDLL EAQDMIRRLE EQLKQLQAAK DELELRQKEL QAMLQRLEEA
410 420 430 440 450
KNMEAVEKLK LEEEIMAKQM EVQRIQDEVN AKDEETKRLQ DEVEDARRKQ
460 470 480 490 500
VIAAEAAAAL LAASTTPQHH HVAEDENENE EELTNGDAGG DVSRDLDTDE
510 520 530 540 550
HIKDPIEDRR TLAERNERLH DQLKALKQDL AQSRDETKET ANDKIHRENV
560 570
RQGRDKYKTL REIRKGNTKR RVDQFENM
Length:578
Mass (Da):68,141
Last modified:November 1, 1997 - v2
Checksum:i24FBA67A3CDF3809
GO
Isoform A (identifier: P46150-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-5: SPKA → GVNFLLFFFSIWL
     65-65: K → KPESPAIKTIKYLKRVKKYVDKKTADSNGVNHLETSEEDDDADDMTGSMPFSTW

Note: No experimental confirmation available.
Show »
Length:640
Mass (Da):75,315
Checksum:i2E52FBE24C5A0ACC
GO
Isoform B (identifier: P46150-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-5: SPKA → VVVSDSRVRLPRYGGVSVKRKT
     65-65: K → KPESPAIKTIKYLKRVKKYVDKKTADSNGVNHLETSEEDDDADDMTGSMPFSTW

Note: No experimental confirmation available.
Show »
Length:649
Mass (Da):76,171
Checksum:i2DD64F7386AE244D
GO
Isoform C (identifier: P46150-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.

Note: No experimental confirmation available.
Show »
Length:512
Mass (Da):60,599
Checksum:i68493D42D08078D9
GO
Isoform D (identifier: P46150-2) [UniParc]FASTAAdd to basket

Also known as: E, F, G, H, I

The sequence of this isoform differs from the canonical sequence as follows:
     451-453: Missing.

Show »
Length:575
Mass (Da):67,858
Checksum:iC2C80F476CC1A464
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti217 – 2193LWL → SLV in AAA65059 (Ref. 6) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6666Missing in isoform C. CuratedVSP_035863Add
BLAST
Alternative sequencei2 – 54SPKA → GVNFLLFFFSIWL in isoform A. CuratedVSP_035864
Alternative sequencei2 – 54SPKA → VVVSDSRVRLPRYGGVSVKR KT in isoform B. CuratedVSP_035865
Alternative sequencei65 – 651K → KPESPAIKTIKYLKRVKKYV DKKTADSNGVNHLETSEEDD DADDMTGSMPFSTW in isoform A and isoform B. CuratedVSP_035866
Alternative sequencei451 – 4533Missing in isoform D. 2 PublicationsVSP_007499

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38909 mRNA. Translation: AAB48934.1.
AE014298 Genomic DNA. Translation: AAF46415.2.
AE014298 Genomic DNA. Translation: AAF46416.1.
AE014298 Genomic DNA. Translation: AAF46417.1.
AE014298 Genomic DNA. Translation: AAF46418.1.
AE014298 Genomic DNA. Translation: AAS65294.1.
AE014298 Genomic DNA. Translation: AAS65295.1.
AE014298 Genomic DNA. Translation: AAS65296.1.
AE014298 Genomic DNA. Translation: AAS65297.1.
AE014298 Genomic DNA. Translation: AAS65298.1.
AE014298 Genomic DNA. Translation: AAS65299.1.
AY069855 mRNA. Translation: AAL40000.1.
U23798 mRNA. Translation: AAA65059.1.
U08218 mRNA. Translation: AAA19857.1.
RefSeqiNP_001245584.1. NM_001258655.1. [P46150-1]
NP_525082.2. NM_080343.4. [P46150-2]
NP_727290.1. NM_167168.4. [P46150-4]
NP_727291.1. NM_167169.2. [P46150-3]
NP_727292.1. NM_167170.2. [P46150-5]
NP_996387.1. NM_206664.3. [P46150-1]
NP_996388.1. NM_206665.3. [P46150-2]
NP_996389.1. NM_206666.3. [P46150-2]
NP_996390.1. NM_206667.3. [P46150-2]
NP_996391.1. NM_206668.3. [P46150-2]
NP_996392.1. NM_206669.2. [P46150-2]
UniGeneiDm.6642.

Genome annotation databases

EnsemblMetazoaiFBtr0071278; FBpp0089236; FBgn0011661. [P46150-1]
FBtr0308194; FBpp0300514; FBgn0011661. [P46150-1]
GeneIDi31816.
UCSCiCG10701-RE. d. melanogaster.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38909 mRNA. Translation: AAB48934.1.
AE014298 Genomic DNA. Translation: AAF46415.2.
AE014298 Genomic DNA. Translation: AAF46416.1.
AE014298 Genomic DNA. Translation: AAF46417.1.
AE014298 Genomic DNA. Translation: AAF46418.1.
AE014298 Genomic DNA. Translation: AAS65294.1.
AE014298 Genomic DNA. Translation: AAS65295.1.
AE014298 Genomic DNA. Translation: AAS65296.1.
AE014298 Genomic DNA. Translation: AAS65297.1.
AE014298 Genomic DNA. Translation: AAS65298.1.
AE014298 Genomic DNA. Translation: AAS65299.1.
AY069855 mRNA. Translation: AAL40000.1.
U23798 mRNA. Translation: AAA65059.1.
U08218 mRNA. Translation: AAA19857.1.
RefSeqiNP_001245584.1. NM_001258655.1. [P46150-1]
NP_525082.2. NM_080343.4. [P46150-2]
NP_727290.1. NM_167168.4. [P46150-4]
NP_727291.1. NM_167169.2. [P46150-3]
NP_727292.1. NM_167170.2. [P46150-5]
NP_996387.1. NM_206664.3. [P46150-1]
NP_996388.1. NM_206665.3. [P46150-2]
NP_996389.1. NM_206666.3. [P46150-2]
NP_996390.1. NM_206667.3. [P46150-2]
NP_996391.1. NM_206668.3. [P46150-2]
NP_996392.1. NM_206669.2. [P46150-2]
UniGeneiDm.6642.

3D structure databases

ProteinModelPortaliP46150.
SMRiP46150. Positions 4-578.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58274. 123 interactions.
DIPiDIP-52150N.
IntActiP46150. 14 interactions.

Proteomic databases

PRIDEiP46150.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071278; FBpp0089236; FBgn0011661. [P46150-1]
FBtr0308194; FBpp0300514; FBgn0011661. [P46150-1]
GeneIDi31816.
UCSCiCG10701-RE. d. melanogaster.

Organism-specific databases

CTDi31816.
FlyBaseiFBgn0011661. Moe.

Phylogenomic databases

GeneTreeiENSGT00830000128251.
InParanoidiP46150.
OMAiMLHAENV.
OrthoDBiEOG7BGHK6.
PhylomeDBiP46150.

Miscellaneous databases

ChiTaRSiMoe. fly.
GenomeRNAii31816.
NextBioi775456.
PROiP46150.

Gene expression databases

BgeeiP46150.
GenevisibleiP46150. DM.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
IPR011174. ERM.
IPR011259. ERM_C_dom.
IPR000798. Ez/rad/moesin-like.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR008954. Moesin_tail.
IPR011993. PH_dom-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view]
PIRSFiPIRSF002305. ERM. 1 hit.
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Distinct cellular and subcellular patterns of expression imply distinct functions for the Drosophila homologues of moesin and the neurofibromatosis 2 tumor suppressor, merlin."
    McCartney B.M., Fehon R.G.
    J. Cell Biol. 133:843-852(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM J), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Oregon-R.
    Tissue: Embryo.
  2. Fehon R.G.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 183-184.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
    Strain: Berkeley.
    Tissue: Embryo.
  6. Winge P., Fleming J.T., Gobel V.
    Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 208-296.
    Tissue: Embryo.
  7. "Identification of Drosophila cytoskeletal proteins by induction of abnormal cell shape in fission yeast."
    Edwards K.A., Montague R.A., Shepard S., Edgar B.A., Erikson R.L., Kiehart D.P.
    Proc. Natl. Acad. Sci. U.S.A. 91:4589-4593(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 256-578 (ISOFORM D).
    Tissue: Embryo.
  8. "Wengen, the sole tumour necrosis factor receptor in Drosophila, collaborates with moesin to control photoreceptor axon targeting during development."
    Ruan W., Unsain N., Desbarats J., Fon E.A., Barker P.A.
    PLoS ONE 8:E60091-E60091(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH WGN.

Entry informationi

Entry nameiMOEH_DROME
AccessioniPrimary (citable) accession number: P46150
Secondary accession number(s): A4V458
, P91930, Q24053, Q24435, Q7KVS6, Q7KVS7, Q9W3B4, Q9W3B5, Q9W3B6, Q9W3B7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: May 11, 2016
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.