AP4E1_MOUSE
ID AP4E1_MOUSE Reviewed; 1122 AA.
AC Q80V94; A2ASB4;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=AP-4 complex subunit epsilon-1 {ECO:0000305};
DE AltName: Full=AP-4 adaptor complex subunit epsilon;
DE AltName: Full=Adaptor-related protein complex 4 subunit epsilon-1;
DE AltName: Full=Epsilon subunit of AP-4;
DE AltName: Full=Epsilon-adaptin;
GN Name=Ap4e1 {ECO:0000312|MGI:MGI:1336993};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH42530.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 590-1122.
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH42530.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH42530.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH GRIA2.
RX PubMed=18341993; DOI=10.1016/j.neuron.2008.02.012;
RA Matsuda S., Miura E., Matsuda K., Kakegawa W., Kohda K., Watanabe M.,
RA Yuzaki M.;
RT "Accumulation of AMPA receptors in autophagosomes in neuronal axons lacking
RT adaptor protein AP-4.";
RL Neuron 57:730-745(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the adaptor protein complex 4 (AP-4). Adaptor
CC protein complexes are vesicle coat components involved both in vesicle
CC formation and cargo selection. They control the vesicular transport of
CC proteins in different trafficking pathways. AP-4 forms a non clathrin-
CC associated coat on vesicles departing the trans-Golgi network (TGN) and
CC may be involved in the targeting of proteins from the trans-Golgi
CC network (TGN) to the endosomal-lysosomal system. It is also involved in
CC protein sorting to the basolateral membrane in epithelial cells and the
CC proper asymmetric localization of somatodendritic proteins in neurons.
CC AP-4 is involved in the recognition and binding of tyrosine-based
CC sorting signals found in the cytoplasmic part of cargos, but may also
CC recognize other types of sorting signal.
CC {ECO:0000250|UniProtKB:Q9UPM8}.
CC -!- SUBUNIT: Adaptor protein complex 4 (AP-4) is a heterotetramer composed
CC of two large adaptins (epsilon-type subunit AP4E1 and beta-type subunit
CC AP4B1), a medium adaptin (mu-type subunit AP4M1) and a small adaptin
CC (sigma-type AP4S1). Interacts with TEPSIN (By similarity). Interacts
CC with GRIA2; probably indirect it mediates the somatodendritic
CC localization of GRIA2 in neurons (PubMed:18341993).
CC {ECO:0000250|UniProtKB:Q9UPM8, ECO:0000269|PubMed:18341993}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q9UPM8}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9UPM8}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK144636; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK144636; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL928590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042530; AAH42530.1; -; mRNA.
DR CCDS; CCDS38231.1; -.
DR RefSeq; NP_780759.2; NM_175550.3.
DR AlphaFoldDB; Q80V94; -.
DR SMR; Q80V94; -.
DR BioGRID; 223764; 1.
DR ComplexPortal; CPX-5154; AP-4 Adaptor complex.
DR STRING; 10090.ENSMUSP00000002063; -.
DR iPTMnet; Q80V94; -.
DR PhosphoSitePlus; Q80V94; -.
DR EPD; Q80V94; -.
DR MaxQB; Q80V94; -.
DR PaxDb; Q80V94; -.
DR PeptideAtlas; Q80V94; -.
DR PRIDE; Q80V94; -.
DR ProteomicsDB; 296360; -.
DR Antibodypedia; 24780; 29 antibodies from 11 providers.
DR DNASU; 108011; -.
DR Ensembl; ENSMUST00000002063; ENSMUSP00000002063; ENSMUSG00000001998.
DR GeneID; 108011; -.
DR KEGG; mmu:108011; -.
DR UCSC; uc008men.1; mouse.
DR CTD; 23431; -.
DR MGI; MGI:1336993; Ap4e1.
DR VEuPathDB; HostDB:ENSMUSG00000001998; -.
DR eggNOG; KOG1062; Eukaryota.
DR GeneTree; ENSGT00950000182838; -.
DR HOGENOM; CLU_003824_3_1_1; -.
DR InParanoid; Q80V94; -.
DR OMA; VLMAMTK; -.
DR OrthoDB; 250202at2759; -.
DR PhylomeDB; Q80V94; -.
DR TreeFam; TF332488; -.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR BioGRID-ORCS; 108011; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Ap4e1; mouse.
DR PRO; PR:Q80V94; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80V94; protein.
DR Bgee; ENSMUSG00000001998; Expressed in manus and 226 other tissues.
DR ExpressionAtlas; Q80V94; baseline and differential.
DR Genevisible; Q80V94; MM.
DR GO; GO:0030124; C:AP-4 adaptor complex; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; TAS:MGI.
DR GO; GO:0140312; F:cargo adaptor activity; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR017109; AP4_complex_esu.
DR InterPro; IPR028269; AP4E1_C.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF14807; AP4E_app_platf; 1.
DR PIRSF; PIRSF037097; AP4_complex_epsilon; 1.
DR SMART; SM01356; AP4E_app_platf; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1122
FT /note="AP-4 complex subunit epsilon-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000229749"
FT REGION 714..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..1122
FT /note="Interaction with TEPSIN"
FT /evidence="ECO:0000250|UniProtKB:Q9UPM8"
FT REGION 797..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPM8"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPM8"
FT CONFLICT 338
FT /note="K -> Q (in Ref. 1; AK144636)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="E -> G (in Ref. 1; AK144636)"
FT /evidence="ECO:0000305"
FT CONFLICT 936
FT /note="D -> E (in Ref. 1; AK144636)"
FT /evidence="ECO:0000305"
FT CONFLICT 954
FT /note="I -> M (in Ref. 1; AK144636)"
FT /evidence="ECO:0000305"
SQ 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
