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Protein

Macrophage erythroblast attacher

Gene

Maea

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in erythroblast enucleation and in the development of the mature macrophages. Mediates the attachment of erythroid cell to mature macrophages, in correlation with the presence of MAEA at cell surface of mature macrophages; This MAEA-mediated contact inhibits erythroid cells apoptosis. Participates to erythroblastic island formation, which is the functional unit of definitive erythropoiesis. Associates with F-actin to regulate actin distribution in erythroblasts and macrophages. May contribute to nuclear architecture and cells division events.2 Publications

GO - Molecular functioni

  • actin binding Source: MGI

GO - Biological processi

  • cell adhesion Source: MGI
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cytoskeleton organization Source: MGI
  • enucleate erythrocyte development Source: MGI
  • erythrocyte development Source: MGI
  • erythrocyte maturation Source: UniProtKB-KW
  • negative regulation of myeloid cell apoptotic process Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Erythrocyte maturation

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Macrophage erythroblast attacher
Alternative name(s):
Erythroblast macrophage protein
Gene namesi
Name:Maea
Synonyms:Emp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1891748. Maea.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice die perinatally and exhibit profound alterations in the hematopoietic system. Blood of E14.5-16.5 embryos contained mostly nucleated erythrocytes suggesting a defect in terminal maturation and enucleation of precursor cells. In the fetal liver, large immature erythroblasts predominate, macrophage exhibit an immature morphology and their number is reduced; No erythroblasts are attached to the macrophages suggesting impairment of erythroblastic island formation.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396Macrophage erythroblast attacherPRO_0000284938Add
BLAST

Proteomic databases

EPDiQ4VC33.
MaxQBiQ4VC33.
PaxDbiQ4VC33.
PRIDEiQ4VC33.

PTM databases

iPTMnetiQ4VC33.
PhosphoSiteiQ4VC33.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ4VC33.
CleanExiMM_MAEA.
ExpressionAtlasiQ4VC33. baseline and differential.
GenevisibleiQ4VC33. MM.

Interactioni

Subunit structurei

Forms a complex with F-actin.1 Publication

GO - Molecular functioni

  • actin binding Source: MGI

Protein-protein interaction databases

IntActiQ4VC33. 1 interaction.
STRINGi10090.ENSMUSP00000110093.

Structurei

3D structure databases

ProteinModelPortaliQ4VC33.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini121 – 15333LisHPROSITE-ProRule annotationAdd
BLAST
Domaini159 – 21658CTLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 124124Extracellular and involved in cell to cell contactBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 CTLH domain.PROSITE-ProRule annotation
Contains 1 LisH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0396. Eukaryota.
ENOG410XPGU. LUCA.
GeneTreeiENSGT00720000108841.
HOVERGENiHBG053270.
InParanoidiQ4VC33.
KOiK18624.
OMAiRQETATC.
OrthoDBiEOG722J8H.
PhylomeDBiQ4VC33.
TreeFamiTF314273.

Family and domain databases

InterProiIPR013144. CRA_dom.
IPR024964. CTLH/CRA.
IPR006595. CTLH_C.
IPR006594. LisH.
[Graphical view]
PfamiPF10607. CLTH. 1 hit.
[Graphical view]
SMARTiSM00757. CRA. 1 hit.
SM00668. CTLH. 1 hit.
SM00667. LisH. 1 hit.
[Graphical view]
PROSITEiPS50897. CTLH. 1 hit.
PS50896. LISH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q4VC33-1) [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
MAVQESAAQL SMTLKVQEYP TLKVPYETLN KRFRAAQKNI DRETSHVTMV
60 70 80 90 100
VAELEKTLSS CPAVDSVVSL LDGVVEKLSV LKRKAVESIQ AEDESAKLCK
110 120 130 140 150
RRIEHLKEHS SDQPAAASMW KRKRMDRMMV EHLLRCGYYN TAVKLARQSG
160 170 180 190 200
IEDLVNIEMF LTAKEVEESL ERRETATCLA WCHDNKSRLR KMKSCLEFSL
210 220 230 240 250
RIQEFIELVR QNKRLDAVRH ARKHFSQAEG SQLDEVRQVM GMLAFPPDTH
260 270 280 290 300
ISPYKDLLDP ARWRMLIQQF RYDNYRLHQL GNSSVFTLTL QAGLSAIKTP
310 320 330 340 350
QCYKEDGSSK SPDCPVCSRS LNKLAQPLPM AHCANSRLVC KISGDVMNEN
360 370 380 390
NPPMMLPNGY VYGYNSLLSI RQDDKVVCPR TKEVFHFSQA EKVYIM
Length:396
Mass (Da):45,336
Last modified:July 5, 2005 - v1
Checksum:i686F1E086742B99B
GO
Isoform 2 (identifier: Q4VC33-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     396-396: M → MYAPSCYGHALGQSGGGWEPCPPALTPDPRPQPASTFVSCDQRSVSNDKYS

Show »
Length:446
Mass (Da):50,602
Checksum:i3D84FB9200D658ED
GO

Sequence cautioni

The sequence BAC35873.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti148 – 1481Q → R in BAE31283 (PubMed:16141072).Curated
Sequence conflicti203 – 2031Q → R in BAC28857 (PubMed:16141072).Curated
Sequence conflicti206 – 2061I → V in BAE40928 (PubMed:16141072).Curated
Sequence conflicti326 – 3261Q → R in BAE31283 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei396 – 3961M → MYAPSCYGHALGQSGGGWEP CPPALTPDPRPQPASTFVSC DQRSVSNDKYS in isoform 2. 1 PublicationVSP_024797

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK034859 mRNA. Translation: BAC28857.1.
AK075637 mRNA. Translation: BAC35873.1. Different initiation.
AK145800 mRNA. Translation: BAE26657.1.
AK152523 mRNA. Translation: BAE31283.1.
AK169149 mRNA. Translation: BAE40928.1.
BC039054 mRNA. Translation: AAH39054.1.
BC058687 mRNA. Translation: AAH58687.1.
AF263247 mRNA. Translation: AAF72195.1.
CCDSiCCDS39063.1. [Q4VC33-1]
RefSeqiNP_067475.2. NM_021500.2. [Q4VC33-1]
UniGeneiMm.138617.
Mm.281642.

Genome annotation databases

EnsembliENSMUST00000114449; ENSMUSP00000110093; ENSMUSG00000079562. [Q4VC33-1]
GeneIDi59003.
KEGGimmu:59003.
UCSCiuc008xap.1. mouse. [Q4VC33-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK034859 mRNA. Translation: BAC28857.1.
AK075637 mRNA. Translation: BAC35873.1. Different initiation.
AK145800 mRNA. Translation: BAE26657.1.
AK152523 mRNA. Translation: BAE31283.1.
AK169149 mRNA. Translation: BAE40928.1.
BC039054 mRNA. Translation: AAH39054.1.
BC058687 mRNA. Translation: AAH58687.1.
AF263247 mRNA. Translation: AAF72195.1.
CCDSiCCDS39063.1. [Q4VC33-1]
RefSeqiNP_067475.2. NM_021500.2. [Q4VC33-1]
UniGeneiMm.138617.
Mm.281642.

3D structure databases

ProteinModelPortaliQ4VC33.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ4VC33. 1 interaction.
STRINGi10090.ENSMUSP00000110093.

PTM databases

iPTMnetiQ4VC33.
PhosphoSiteiQ4VC33.

Proteomic databases

EPDiQ4VC33.
MaxQBiQ4VC33.
PaxDbiQ4VC33.
PRIDEiQ4VC33.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000114449; ENSMUSP00000110093; ENSMUSG00000079562. [Q4VC33-1]
GeneIDi59003.
KEGGimmu:59003.
UCSCiuc008xap.1. mouse. [Q4VC33-1]

Organism-specific databases

CTDi10296.
MGIiMGI:1891748. Maea.

Phylogenomic databases

eggNOGiKOG0396. Eukaryota.
ENOG410XPGU. LUCA.
GeneTreeiENSGT00720000108841.
HOVERGENiHBG053270.
InParanoidiQ4VC33.
KOiK18624.
OMAiRQETATC.
OrthoDBiEOG722J8H.
PhylomeDBiQ4VC33.
TreeFamiTF314273.

Miscellaneous databases

ChiTaRSiMaea. mouse.
PROiQ4VC33.
SOURCEiSearch...

Gene expression databases

BgeeiQ4VC33.
CleanExiMM_MAEA.
ExpressionAtlasiQ4VC33. baseline and differential.
GenevisibleiQ4VC33. MM.

Family and domain databases

InterProiIPR013144. CRA_dom.
IPR024964. CTLH/CRA.
IPR006595. CTLH_C.
IPR006594. LisH.
[Graphical view]
PfamiPF10607. CLTH. 1 hit.
[Graphical view]
SMARTiSM00757. CRA. 1 hit.
SM00668. CTLH. 1 hit.
SM00667. LisH. 1 hit.
[Graphical view]
PROSITEiPS50897. CTLH. 1 hit.
PS50896. LISH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Bone marrow, Embryo and Heart.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain and Mammary tumor.
  3. "cDNA sequence and genomic structure of the mouse erythroblast macrophage protein (EMP) gene."
    Dua M., Peters L.L., Hanspal M.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-396 (ISOFORM 2).
  4. "Emp is a component of the nuclear matrix of mammalian cells and undergoes dynamic rearrangements during cell division."
    Bala S., Kumar A., Soni S., Sinha S., Hanspal M.
    Biochem. Biophys. Res. Commun. 342:1040-1048(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "Absence of erythroblast macrophage protein (Emp) leads to failure of erythroblast nuclear extrusion."
    Soni S., Bala S., Gwynn B., Sahr K.E., Peters L.L., Hanspal M.
    J. Biol. Chem. 281:20181-20189(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, SUBUNIT, FUNCTION.
  6. "Changing pattern of the subcellular distribution of erythroblast macrophage protein (Emp) during macrophage differentiation."
    Soni S., Bala S., Kumar A., Hanspal M.
    Blood Cells Mol. Dis. 38:25-31(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Spleen and Testis.

Entry informationi

Entry nameiMAEA_MOUSE
AccessioniPrimary (citable) accession number: Q4VC33
Secondary accession number(s): Q3TFH0
, Q3U7T6, Q5XKE6, Q8BPI3, Q8BSA1, Q9JK49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: July 5, 2005
Last modified: June 8, 2016
This is version 96 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.