ID   AP4M1_MOUSE             Reviewed;         449 AA.
AC   Q9JKC7;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 152.
DE   RecName: Full=AP-4 complex subunit mu-1 {ECO:0000305};
DE   AltName: Full=AP-4 adaptor complex mu subunit;
DE   AltName: Full=Adaptor-related protein complex 4 subunit mu-1;
DE   AltName: Full=Mu subunit of AP-4;
DE   AltName: Full=Mu-adaptin-related protein 2;
DE            Short=mu-ARP2;
DE   AltName: Full=Mu4-adaptin;
DE            Short=mu4;
GN   Name=Ap4m1 {ECO:0000312|MGI:MGI:1337063};
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]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Werner H., Nave K.-A.;
RT   "Mus musculus adaptor-related protein complex AP-4 mu4 subunit.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
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   [3]
RP   FUNCTION, AND INTERACTION WITH CACNG3; GRIA1 AND 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).
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 (By similarity). It is
CC       also involved in protein sorting to the basolateral membrane in
CC       epithelial cells and the proper asymmetric localization of
CC       somatodendritic proteins in neurons (PubMed:18341993). Within AP-4, the
CC       mu-type subunit AP4M1 is directly involved in the recognition and
CC       binding of tyrosine-based sorting signals found in the cytoplasmic part
CC       of cargos. The adaptor protein complex 4 (AP-4) may also recognize
CC       other types of sorting signal (By similarity).
CC       {ECO:0000250|UniProtKB:O00189, ECO:0000269|PubMed:18341993}.
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 tyrosine-based sorting signals on
CC       the cytoplasmic tail of cargo proteins such as APP, ATG9A, LAMP2 and
CC       NAGPA. Interacts with the C-terminal domain of GRID2 (By similarity).
CC       Interacts with GRIA1 and GRIA2; the interaction is indirect via CACNG3
CC       (PubMed:18341993). Interacts with CACNG3; CACNG3 associates GRIA1 and
CC       GRIA2 with the adaptor protein complex 4 (AP-4) to target them to the
CC       somatodendritic compartment of neurons (PubMed:18341993). Interacts
CC       with HOOK1 and HOOK2; the interactions are direct, mediate the
CC       interaction between FTS-Hook-FHIP (FHF) complex and AP-4 and the
CC       perinuclear distribution of AP-4 (By similarity).
CC       {ECO:0000250|UniProtKB:O00189, ECO:0000269|PubMed:18341993}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250|UniProtKB:O00189}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:O00189}. Early endosome
CC       {ECO:0000250|UniProtKB:O00189}. Note=Found in soma and dendritic shafts
CC       of neuronal cells. {ECO:0000250|UniProtKB:Q2PWT8}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AF242858; AAF63513.1; -; mRNA.
DR   EMBL; BC011174; AAH11174.1; -; mRNA.
DR   CCDS; CCDS19794.1; -.
DR   RefSeq; NP_067367.3; NM_021392.4.
DR   AlphaFoldDB; Q9JKC7; -.
DR   SMR; Q9JKC7; -.
DR   BioGRID; 198137; 1.
DR   ComplexPortal; CPX-5154; AP-4 Adaptor complex.
DR   STRING; 10090.ENSMUSP00000019662; -.
DR   iPTMnet; Q9JKC7; -.
DR   PhosphoSitePlus; Q9JKC7; -.
DR   MaxQB; Q9JKC7; -.
DR   PaxDb; 10090-ENSMUSP00000019662; -.
DR   ProteomicsDB; 296213; -.
DR   Pumba; Q9JKC7; -.
DR   Antibodypedia; 30540; 183 antibodies from 25 providers.
DR   DNASU; 11781; -.
DR   Ensembl; ENSMUST00000019662.11; ENSMUSP00000019662.5; ENSMUSG00000019518.12.
DR   GeneID; 11781; -.
DR   KEGG; mmu:11781; -.
DR   UCSC; uc009aev.2; mouse.
DR   AGR; MGI:1337063; -.
DR   CTD; 9179; -.
DR   MGI; MGI:1337063; Ap4m1.
DR   VEuPathDB; HostDB:ENSMUSG00000019518; -.
DR   eggNOG; KOG0937; Eukaryota.
DR   GeneTree; ENSGT00940000159929; -.
DR   HOGENOM; CLU_026996_5_0_1; -.
DR   InParanoid; Q9JKC7; -.
DR   OMA; DYGYIQN; -.
DR   OrthoDB; 5353102at2759; -.
DR   PhylomeDB; Q9JKC7; -.
DR   TreeFam; TF329745; -.
DR   Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR   BioGRID-ORCS; 11781; 5 hits in 76 CRISPR screens.
DR   ChiTaRS; Ap4m1; mouse.
DR   PRO; PR:Q9JKC7; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9JKC7; Protein.
DR   Bgee; ENSMUSG00000019518; Expressed in spermatid and 143 other cell types or tissues.
DR   ExpressionAtlas; Q9JKC7; baseline and differential.
DR   GO; GO:0030124; C:AP-4 adaptor complex; ISS:UniProtKB.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR   GO; GO:0006895; P:Golgi to endosome transport; ISS:UniProtKB.
DR   GO; GO:0090160; P:Golgi to lysosome transport; ISS:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR   GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR   GO; GO:1903361; P:protein localization to basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0006605; P:protein targeting; IMP:UniProtKB.
DR   GO; GO:0006622; P:protein targeting to lysosome; ISO:MGI.
DR   GO; GO:0016192; P:vesicle-mediated transport; TAS:MGI.
DR   CDD; cd09253; AP-4_Mu4_Cterm; 1.
DR   CDD; cd14838; AP4_Mu_N; 1.
DR   Gene3D; 3.30.450.60; -; 1.
DR   Gene3D; 2.60.40.1170; Mu homology domain, subdomain B; 2.
DR   InterPro; IPR036168; AP2_Mu_C_sf.
DR   InterPro; IPR001392; Clathrin_mu.
DR   InterPro; IPR018240; Clathrin_mu_CS.
DR   InterPro; IPR011012; Longin-like_dom_sf.
DR   InterPro; IPR028565; MHD.
DR   PANTHER; PTHR10529; AP COMPLEX SUBUNIT MU; 1.
DR   PANTHER; PTHR10529:SF270; AP-4 COMPLEX SUBUNIT MU-1; 1.
DR   Pfam; PF00928; Adap_comp_sub; 1.
DR   PIRSF; PIRSF005992; Clathrin_mu; 1.
DR   PRINTS; PR00314; CLATHRINADPT.
DR   SUPFAM; SSF49447; Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor; 1.
DR   SUPFAM; SSF64356; SNARE-like; 1.
DR   PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR   PROSITE; PS51072; MHD; 1.
DR   Genevisible; Q9JKC7; MM.
PE   1: Evidence at protein level;
KW   Endosome; Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..449
FT                   /note="AP-4 complex subunit mu-1"
FT                   /id="PRO_0000193788"
FT   DOMAIN          184..448
FT                   /note="MHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
SQ   SEQUENCE   449 AA;  49509 MW;  579AEAE1F82B5D04 CRC64;
     MISQFFILSS KGDPLIYKDF RGDSGGRDVA ELFYRKLTGL PGGESPVVMY HGDRHFIHIR
     HSGLYLVATT LENVSPFSLL ELLSRLATLL GDYCGSLNEG TISRNVALVY ELLDEVLDYG
     YVQTTSTEML RNFIQTEAVV SKPFSLFDLS SVGLFGAETQ QNKVAPSSAA SRPVLSSRSD
     QSQKNEVFLD VVERLSVLIA SNGSLLKVDV QGEIRLKSFL PSGSEICIGL TEEFCVGKSE
     LRGYGPGIRV DEVSFHSSVN LDEFESHRIL RLQPPQGELT VMRYQLSDDL PSPLPFRLFP
     SVQWDQGSGR LQVYLKLRCD LPPKSQALNI HLHLPLPRGV ISLSQELSSP DQKAELGEGA
     LHWDLPRVQG GSQLSGLFQM DVPGLQGLPN HGPSPLGLGP ASLSFELPRH TCSGLQVRFL
     RLSFSACGNA NPHKWVRHLS HSNAYVIRI
//