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AP-4 complex subunit epsilon-1 (AP-4 adaptor complex subunit epsilon) (Adaptor-related protein complex 4 subunit epsilon-1) (Epsilon subunit of AP-4) (Epsilon-adaptin)

 AP4E1_MOUSE             Reviewed;        1122 AA.
Q80V94; A2ASB4;
04-APR-2006, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
12-SEP-2018, entry version 116.
RecName: Full=AP-4 complex subunit epsilon-1 {ECO:0000305};
AltName: Full=AP-4 adaptor complex subunit epsilon;
AltName: Full=Adaptor-related protein complex 4 subunit epsilon-1;
AltName: Full=Epsilon subunit of AP-4;
AltName: Full=Epsilon-adaptin;
Name=Ap4e1 {ECO:0000312|MGI:MGI:1336993};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3] {ECO:0000305, ECO:0000312|EMBL:AAH42530.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 590-1122.
STRAIN=FVB/N {ECO:0000312|EMBL:AAH42530.1};
TISSUE=Mammary gland {ECO:0000312|EMBL:AAH42530.1};
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]
INTERACTION WITH GRIA2.
PubMed=18341993; DOI=10.1016/j.neuron.2008.02.012;
Matsuda S., Miura E., Matsuda K., Kakegawa W., Kohda K., Watanabe M.,
Yuzaki M.;
"Accumulation of AMPA receptors in autophagosomes in neuronal axons
lacking adaptor protein AP-4.";
Neuron 57:730-745(2008).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Component of the adaptor protein complex 4 (AP-4).
Adaptor protein complexes are vesicle coat components involved
both in vesicle formation and cargo selection. They control the
vesicular transport of proteins in different trafficking pathways.
AP-4 forms a non clathrin-associated coat on vesicles departing
the trans-Golgi network (TGN) and may be involved in the targeting
of proteins from the trans-Golgi network (TGN) to the endosomal-
lysosomal system. It is also involved in protein sorting to the
basolateral membrane in epithelial cells and the proper asymmetric
localization of somatodendritic proteins in neurons. AP-4 is
involved in the recognition and binding of tyrosine-based sorting
signals found in the cytoplasmic part of cargos, but may also
recognize other types of sorting signal.
{ECO:0000250|UniProtKB:Q9UPM8}.
-!- SUBUNIT: Adaptor protein complex 4 (AP-4) is a heterotetramer
composed of two large adaptins (epsilon-type subunit AP4E1 and
beta-type subunit AP4B1), a medium adaptin (mu-type subunit AP4M1)
and a small adaptin (sigma-type AP4S1). Interacts with TEPSIN (By
similarity). Interacts with GRIA2; probably indirect it mediates
the somatodendritic localization of GRIA2 in neurons
(PubMed:18341993). {ECO:0000250|UniProtKB:Q9UPM8,
ECO:0000269|PubMed:18341993}.
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane {ECO:0000250|UniProtKB:Q9UPM8}; Peripheral membrane
protein {ECO:0000250|UniProtKB:Q9UPM8}.
-!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
{ECO:0000255}.
-!- SEQUENCE CAUTION:
Sequence=AK144636; Type=Frameshift; Positions=303; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK144636; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AL928836; CAM18335.1; -; Genomic_DNA.
EMBL; AL928590; CAM18335.1; JOINED; Genomic_DNA.
EMBL; AL928590; CAM19126.1; -; Genomic_DNA.
EMBL; AL928836; CAM19126.1; JOINED; Genomic_DNA.
EMBL; BC042530; AAH42530.1; -; mRNA.
CCDS; CCDS38231.1; -.
RefSeq; NP_780759.2; NM_175550.3.
UniGene; Mm.134045; -.
ProteinModelPortal; Q80V94; -.
SMR; Q80V94; -.
STRING; 10090.ENSMUSP00000002063; -.
iPTMnet; Q80V94; -.
PhosphoSitePlus; Q80V94; -.
EPD; Q80V94; -.
MaxQB; Q80V94; -.
PaxDb; Q80V94; -.
PeptideAtlas; Q80V94; -.
PRIDE; Q80V94; -.
DNASU; 108011; -.
Ensembl; ENSMUST00000002063; ENSMUSP00000002063; ENSMUSG00000001998.
GeneID; 108011; -.
KEGG; mmu:108011; -.
UCSC; uc008men.1; mouse.
CTD; 23431; -.
MGI; MGI:1336993; Ap4e1.
eggNOG; KOG1062; Eukaryota.
eggNOG; ENOG410XPKK; LUCA.
GeneTree; ENSGT00390000012618; -.
HOGENOM; HOG000231886; -.
HOVERGEN; HBG050522; -.
InParanoid; Q80V94; -.
KO; K12400; -.
OMA; SYKIWKD; -.
OrthoDB; EOG091G010Y; -.
TreeFam; TF332488; -.
Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
PRO; PR:Q80V94; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000001998; Expressed in 233 organ(s), highest expression level in quadriceps femoris.
CleanEx; MM_AP4E1; -.
ExpressionAtlas; Q80V94; baseline and differential.
Genevisible; Q80V94; MM.
GO; GO:0030124; C:AP-4 adaptor complex; ISS:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; TAS:MGI.
GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
GO; GO:0016192; P:vesicle-mediated transport; TAS:MGI.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR017109; AP4_complex_esu.
InterPro; IPR028269; AP4E1_C.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
Pfam; PF01602; Adaptin_N; 1.
Pfam; PF14807; AP4E_app_platf; 1.
PIRSF; PIRSF037097; AP4_complex_epsilon; 1.
SMART; SM01356; AP4E_app_platf; 1.
SUPFAM; SSF48371; SSF48371; 2.
1: Evidence at protein level;
Complete proteome; Golgi apparatus; Membrane; Phosphoprotein;
Protein transport; Reference proteome; Transport.
CHAIN 1 1122 AP-4 complex subunit epsilon-1.
{ECO:0000305}.
/FTId=PRO_0000229749.
REGION 726 1122 Interaction with TEPSIN.
{ECO:0000250|UniProtKB:Q9UPM8}.
MOD_RES 699 699 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UPM8}.
MOD_RES 851 851 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UPM8}.
CONFLICT 338 338 K -> Q (in Ref. 1; AK144636).
{ECO:0000305}.
CONFLICT 379 379 E -> G (in Ref. 1; AK144636).
{ECO:0000305}.
CONFLICT 936 936 D -> E (in Ref. 1; AK144636).
{ECO:0000305}.
CONFLICT 954 954 I -> M (in Ref. 1; AK144636).
{ECO:0000305}.
SEQUENCE 1122 AA; 124845 MW; D5B4E518714DBA3D CRC64;
MSDMVERTLT ALPGLFLQNQ LGGPAASRAP FFSRLGGLIR GVTALSSKHE EEKLIQQELS
SLKATVSAPT TTLKTMKECM VRLIYCEMLG YDASFGYIHA IKLAQQGNLL EKRVGYLAVS
LFLHESHELL LLLVNTVVKD LQSTNLVEVC MALTVVSQIF PREMIPAVLP LIEDKLQHSK
EIIRRKAVLA LYKFYLIAPN QVQHIHTKFR KALCDRDVGV MAASLHIYLR MIKENASGYK
DLTESFVTIL KQVVGGKLPV EFSYHSVPAP WLQIQLLRIL GLLGKDDERT SELMYDVLDE
SLRRAELNHN VTYAILFECV HTIYSIYPKS ELLEKAAKCI GKFVLSPKIN LKYLGLKALT
YVIQQDPSLA LQHQITIIEC LDHPDPIIKR ETLELLYRIT NAQNVVVIVQ KMLEYLHQSK
EEHIIISLVG RIAELAEKYA PDNVWFIQTM NAVFSVGGDV MHPDILSNFL RLLAEGFDDE
TEDQQLRLYA VQSYLTLLDM ENTFYPQRFL QVMSWVLGEY SYLLDKESPE EVITRLYKLL
MSDSISSETK AWLFAAVTKL TPQAHSSPLV EKLIQEFTVS LNTCLRQHAF ELKHLHENTE
LMKSLLQGAQ NCEDIVADAS LSFLDGFVAE GLSQGAAPYK PHHQRQEEQL SQEKVLNFEP
YGLSFSSSGF TGRQSPAGIS LGSDISGNSA ETGLKETSSL KMEGIKKLWG KEGYLPKKES
GTGDKPEASH VPAEGATVEN VDQATTRKDQ AQGHIPSTEE KEKQLLASSL FVGLGPENTV
DLLGKADVVS HKFRRKSKLK VAQSDKTPSA PTAPCSALSL GSDVAGGDED GLSAVDRGDG
ELSSELFRSE SLSGPPSAEK LESVSLPVPS LFADNNMEVF NPPSSSATST VKEETPECRH
SGLVEICSNE AVSVSSYKVW RDDCLLVIWA VTSKTDSEFT DAQLEIFPVE NFKIIEQPEC
SSPVIETERT KSFQYSVQME SPCIEGTLSG FIKYQMMDTH SVQLEFSMNL PLLDFIRPLK
ISTEDFGKLW LSFANDVKQT IKISEPGVAL TSVLTELQQN LRLRVIDVIG NEGLLACKLL
PSTPCVLHCR VHADAVALWF RSSSSVLSDY LSCHCQKVMQ TS


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