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Macrophage erythroblast attacher (Cell proliferation-inducing gene 5 protein) (Erythroblast macrophage protein) (Human lung cancer oncogene 10 protein) (HLC-10)

 MAEA_HUMAN              Reviewed;         396 AA.
Q7L5Y9; O95285; Q5JB54; Q6ZRD6; Q9BQ11; Q9H9V6; Q9H9Z4; Q9NW84;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 1.
20-JUN-2018, entry version 115.
RecName: Full=Macrophage erythroblast attacher;
AltName: Full=Cell proliferation-inducing gene 5 protein;
AltName: Full=Erythroblast macrophage protein;
AltName: Full=Human lung cancer oncogene 10 protein;
Short=HLC-10;
Name=MAEA; Synonyms=EMP; ORFNames=HLC10, PIG5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Kim J.W.;
"Identification of a human cell proliferation gene 5.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
TISSUE=Embryo, and Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 5-396 (ISOFORM 2), REGION, FUNCTION, AND
TISSUE SPECIFICITY.
PubMed=9763581;
Hanspal M., Smockova Y., Uong Q.;
"Molecular identification and functional characterization of a novel
protein that mediates the attachment of erythroblasts to
macrophages.";
Blood 92:2940-2950(1998).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-396 (ISOFORM 1).
Kim J.W.;
"Identification of new human cancer-related gene (HLC-10).";
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-396 (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
FUNCTION, TISSUE SPECIFICITY, SUBUNIT, DEVELOPMENTAL STAGE, AND
SUBCELLULAR LOCATION.
PubMed=16510120; DOI=10.1016/j.bbrc.2006.02.060;
Bala S., Kumar A., Soni S., Sinha S., Hanspal M.;
"Emp is a component of the nuclear matrix of mammalian cells and
undergoes dynamic rearrangements during cell division.";
Biochem. Biophys. Res. Commun. 342:1040-1048(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-28, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: 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
in 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.
{ECO:0000269|PubMed:16510120, ECO:0000269|PubMed:9763581}.
-!- SUBUNIT: Forms a complex with F-actin.
{ECO:0000269|PubMed:16510120}.
-!- SUBCELLULAR LOCATION: Nucleus matrix
{ECO:0000269|PubMed:16510120}. Cell membrane
{ECO:0000269|PubMed:16510120}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:16510120}. Note=Localized as nuclear speckled-
like pattern.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q7L5Y9-1; Sequence=Displayed;
Name=2;
IsoId=Q7L5Y9-2; Sequence=VSP_024786, VSP_024790;
Name=3;
IsoId=Q7L5Y9-3; Sequence=VSP_024786;
Name=4;
IsoId=Q7L5Y9-4; Sequence=VSP_024784, VSP_024788;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q7L5Y9-5; Sequence=VSP_024785, VSP_024789;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16510120,
ECO:0000269|PubMed:9763581}.
-!- DEVELOPMENTAL STAGE: Localized with condensed chromatin at
prophase; Detected in nuclear spindle poles at metaphase and in
the contractile ring during telophase and cytokinesis.
{ECO:0000269|PubMed:16510120}.
-!- SEQUENCE CAUTION:
Sequence=AAC67543.1; Type=Erroneous termination; Positions=397; Note=Translated as stop.; Evidence={ECO:0000305};
Sequence=AAC67543.1; Type=Frameshift; Positions=253, 327; Evidence={ECO:0000305};
Sequence=AAC67543.1; Type=Miscellaneous discrepancy; Note=Sequence differs at N-terminus.; Evidence={ECO:0000305};
Sequence=AAO85220.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AK128302; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY236486; AAP74806.1; -; mRNA.
EMBL; AK001088; BAA91499.1; -; mRNA.
EMBL; AK128302; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK022515; BAB14072.1; -; mRNA.
EMBL; AK022586; BAB14113.1; -; mRNA.
EMBL; BC001225; AAH01225.2; -; mRNA.
EMBL; BC006470; AAH06470.2; -; mRNA.
EMBL; AF084928; AAC67543.1; ALT_SEQ; mRNA.
EMBL; AY189687; AAO85220.1; ALT_INIT; mRNA.
EMBL; BT006957; AAP35603.1; -; mRNA.
CCDS; CCDS33936.1; -. [Q7L5Y9-1]
CCDS; CCDS33937.1; -. [Q7L5Y9-3]
CCDS; CCDS77887.1; -. [Q7L5Y9-4]
RefSeq; NP_001017405.1; NM_001017405.2. [Q7L5Y9-1]
RefSeq; NP_001284360.1; NM_001297431.1.
RefSeq; NP_005873.2; NM_005882.4. [Q7L5Y9-3]
UniGene; Hs.139896; -.
ProteinModelPortal; Q7L5Y9; -.
SMR; Q7L5Y9; -.
BioGrid; 115584; 68.
CORUM; Q7L5Y9; -.
IntAct; Q7L5Y9; 16.
STRING; 9606.ENSP00000302830; -.
DrugBank; DB05389; WF10.
iPTMnet; Q7L5Y9; -.
PhosphoSitePlus; Q7L5Y9; -.
BioMuta; MAEA; -.
DMDM; 74754297; -.
EPD; Q7L5Y9; -.
MaxQB; Q7L5Y9; -.
PaxDb; Q7L5Y9; -.
PeptideAtlas; Q7L5Y9; -.
PRIDE; Q7L5Y9; -.
ProteomicsDB; 68819; -.
ProteomicsDB; 68820; -. [Q7L5Y9-2]
ProteomicsDB; 68821; -. [Q7L5Y9-3]
ProteomicsDB; 68822; -. [Q7L5Y9-4]
ProteomicsDB; 68823; -. [Q7L5Y9-5]
DNASU; 10296; -.
Ensembl; ENST00000264750; ENSP00000264750; ENSG00000090316. [Q7L5Y9-3]
Ensembl; ENST00000303400; ENSP00000302830; ENSG00000090316. [Q7L5Y9-1]
GeneID; 10296; -.
KEGG; hsa:10296; -.
UCSC; uc003gda.4; human. [Q7L5Y9-1]
CTD; 10296; -.
DisGeNET; 10296; -.
EuPathDB; HostDB:ENSG00000090316.15; -.
GeneCards; MAEA; -.
HGNC; HGNC:13731; MAEA.
HPA; HPA036886; -.
HPA; HPA058185; -.
MIM; 606801; gene.
neXtProt; NX_Q7L5Y9; -.
OpenTargets; ENSG00000090316; -.
PharmGKB; PA30533; -.
eggNOG; KOG0396; Eukaryota.
eggNOG; ENOG410XPGU; LUCA.
GeneTree; ENSGT00720000108841; -.
HOVERGEN; HBG053270; -.
InParanoid; Q7L5Y9; -.
KO; K18624; -.
PhylomeDB; Q7L5Y9; -.
TreeFam; TF314273; -.
ChiTaRS; MAEA; human.
GenomeRNAi; 10296; -.
PRO; PR:Q7L5Y9; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000090316; -.
CleanEx; HS_MAEA; -.
ExpressionAtlas; Q7L5Y9; baseline and differential.
Genevisible; Q7L5Y9; HS.
GO; GO:0005826; C:actomyosin contractile ring; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
GO; GO:0034657; C:GID complex; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005819; C:spindle; IDA:UniProtKB.
GO; GO:0003779; F:actin binding; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007010; P:cytoskeleton organization; IEA:Ensembl.
GO; GO:0048822; P:enucleate erythrocyte development; IEA:Ensembl.
GO; GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:InterPro.
GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IDA:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0016567; P:protein ubiquitination; IEA:GOC.
GO; GO:0007346; P:regulation of mitotic cell cycle; NAS:UniProtKB.
InterPro; IPR013144; CRA_dom.
InterPro; IPR024964; CTLH/CRA.
InterPro; IPR006595; CTLH_C.
InterPro; IPR027714; Fyv10/EMP.
InterPro; IPR006594; LisH.
PANTHER; PTHR12170:SF2; PTHR12170:SF2; 1.
Pfam; PF10607; CLTH; 1.
SMART; SM00757; CRA; 1.
SMART; SM00668; CTLH; 1.
SMART; SM00667; LisH; 1.
PROSITE; PS50897; CTLH; 1.
PROSITE; PS50896; LISH; 1.
1: Evidence at protein level;
Actin-binding; Alternative splicing; Cell cycle; Cell division;
Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton;
Erythrocyte maturation; Membrane; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 396 Macrophage erythroblast attacher.
/FTId=PRO_0000284936.
DOMAIN 121 153 LisH. {ECO:0000255|PROSITE-
ProRule:PRU00126}.
DOMAIN 159 216 CTLH. {ECO:0000255|PROSITE-
ProRule:PRU00058}.
REGION 1 124 Extracellular and involved in cell to
cell contact.
MOD_RES 28 28 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 152 232 EDLVNIEMFLTAKEVEESLERRETATCLAWCHDNKSRLRKM
KSCLEFSLRIQEFIELIRQNKRLDAVRHARKHFSQAEGSQ
-> GTCKKALQPSRREPAGRGAPGHGHAGLPARHAHLPVQG
PSGPCTVADADPAVPVRQLPTTPAGKQFCVHPHPAGWPLSH
QD (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_024784.
VAR_SEQ 153 245 DLVNIEMFLTAKEVEESLERRETATCLAWCHDNKSRLRKMK
SCLEFSLRIQEFIELIRQNKRLDAVRHARKHFSQAEGSQLD
EVRQAMGMLAF -> TCKKALQPSRREPAGRGAPGHGHAGL
PARHAHLPVQGPSGPCTVADADPAVPVRQLPTTPAGKQFCV
HPHPAGRPLSHQDTTVLQGGRQLQEP (in isoform
5). {ECO:0000303|Ref.1}.
/FTId=VSP_024785.
VAR_SEQ 153 193 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:9763581}.
/FTId=VSP_024786.
VAR_SEQ 233 300 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_024788.
VAR_SEQ 246 396 Missing (in isoform 5).
{ECO:0000303|Ref.1}.
/FTId=VSP_024789.
VAR_SEQ 265 265 M -> TCTVAD (in isoform 2).
{ECO:0000303|PubMed:9763581}.
/FTId=VSP_024790.
VARIANT 34 34 R -> C (in dbSNP:rs34082974).
/FTId=VAR_051150.
CONFLICT 32 32 R -> C (in Ref. 1; AAP74806).
{ECO:0000305}.
CONFLICT 56 56 K -> R (in Ref. 4; AAC67543).
{ECO:0000305}.
CONFLICT 101 101 R -> L (in Ref. 4; AAC67543).
{ECO:0000305}.
CONFLICT 123 123 K -> R (in Ref. 2; BAA91499).
{ECO:0000305}.
CONFLICT 313 313 D -> V (in Ref. 4; AAC67543).
{ECO:0000305}.
CONFLICT 327 327 P -> R (in Ref. 4; AAC67543).
{ECO:0000305}.
SEQUENCE 396 AA; 45287 MW; 361FB82BE0240C21 CRC64;
MAVQESAAQL SMTLKVQEYP TLKVPYETLN KRFRAAQKNI DRETSHVTMV VAELEKTLSG
CPAVDSVVSL LDGVVEKLSV LKRKAVESIQ AEDESAKLCK RRIEHLKEHS SDQPAAASVW
KRKRMDRMMV EHLLRCGYYN TAVKLARQSG IEDLVNIEMF LTAKEVEESL ERRETATCLA
WCHDNKSRLR KMKSCLEFSL RIQEFIELIR QNKRLDAVRH ARKHFSQAEG SQLDEVRQAM
GMLAFPPDTH ISPYKDLLDP ARWRMLIQQF RYDNYRLHQL GNNSVFTLTL QAGLSAIKTP
QCYKEDGSSK SPDCPVCSRS LNKLAQPLPM AHCANSRLVC KISGDVMNEN NPPMMLPNGY
VYGYNSLLSI RQDDKVVCPR TKEVFHFSQA EKVYIM


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