AP4M1_RAT
ID AP4M1_RAT Reviewed; 453 AA.
AC Q2PWT8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
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|RGD:1310233};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABC02084.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH GRID2, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley {ECO:0000250|UniProtKB:O00189, ECO:0000305};
RC TISSUE=Brain {ECO:0000269|PubMed:14572453};
RX PubMed=14572453; DOI=10.1016/s1044-7431(03)00164-7;
RA Yap C.C., Murate M., Kishigami S., Muto Y., Kishida H., Hashikawa T.,
RA Yano R.;
RT "Adaptor protein complex-4 (AP-4) is expressed in the central nervous
RT system neurons and interacts with glutamate receptor delta2.";
RL Mol. Cell. Neurosci. 24:283-295(2003).
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 Within AP-4, the mu-type subunit AP4M1 is directly involved in the
CC recognition and binding of tyrosine-based sorting signals found in the
CC cytoplasmic part of cargos (By similarity). The adaptor protein complex
CC 4 (AP-4) may also recognize other types of sorting signal
CC (PubMed:14572453). {ECO:0000250|UniProtKB:O00189,
CC ECO:0000269|PubMed:14572453}.
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 (By similarity). Interacts with the C-terminal domain of GRID2
CC (PubMed:14572453). Interacts with GRIA1 and GRIA2; the interaction is
CC indirect via CACNG3. 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 (By similarity). Interacts with
CC HOOK1 and HOOK2; the interactions are direct, mediate the interaction
CC between FTS-Hook-FHIP (FHF) complex and AP-4 and the perinuclear
CC distribution of AP-4 (By similarity). {ECO:0000250|UniProtKB:O00189,
CC ECO:0000269|PubMed:14572453}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000305|PubMed:14572453}; Peripheral membrane protein
CC {ECO:0000305|PubMed:14572453}. Early endosome
CC {ECO:0000250|UniProtKB:O00189}. Note=Found in soma and dendritic shafts
CC of neuronal cells. {ECO:0000269|PubMed:14572453}.
CC -!- TISSUE SPECIFICITY: High levels in the olfactory bulb, the cerebral
CC cortex, the granule and Purkinje cell layers of the cerebellar cortex
CC and the CA3 region of the hippocampus. Low levels found in molecular
CC layer of cerebellum. {ECO:0000269|PubMed:14572453}.
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ298439; ABC02084.1; -; mRNA.
DR RefSeq; NP_001033066.1; NM_001037977.1.
DR AlphaFoldDB; Q2PWT8; -.
DR SMR; Q2PWT8; -.
DR STRING; 10116.ENSRNOP00000001827; -.
DR PaxDb; Q2PWT8; -.
DR PRIDE; Q2PWT8; -.
DR Ensembl; ENSRNOT00000001827; ENSRNOP00000001827; ENSRNOG00000001353.
DR GeneID; 304344; -.
DR KEGG; rno:304344; -.
DR UCSC; RGD:1310233; rat.
DR CTD; 9179; -.
DR RGD; 1310233; Ap4m1.
DR eggNOG; KOG0937; Eukaryota.
DR GeneTree; ENSGT00940000159929; -.
DR HOGENOM; CLU_026996_5_0_1; -.
DR InParanoid; Q2PWT8; -.
DR OMA; NVCATIP; -.
DR OrthoDB; 662490at2759; -.
DR PhylomeDB; Q2PWT8; -.
DR TreeFam; TF329745; -.
DR Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis.
DR PRO; PR:Q2PWT8; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001353; Expressed in stomach and 19 other tissues.
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:RGD.
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; ISS:UniProtKB.
DR GO; GO:1903361; P:protein localization to basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0006605; P:protein targeting; ISS:UniProtKB.
DR GO; GO:0006622; P:protein targeting to lysosome; ISO:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR001392; Clathrin_mu.
DR InterPro; IPR018240; Clathrin_mu_CS.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR028565; MHD.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR PIRSF; PIRSF005992; Clathrin_mu; 1.
DR PRINTS; PR00314; CLATHRINADPT.
DR SUPFAM; SSF49447; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW Endosome; Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..453
FT /note="AP-4 complex subunit mu-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000229750"
FT DOMAIN 184..452
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 383..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 49853 MW; 9605A72F134568FC CRC64;
MISQFFILSS KGDPLIYKDF RGDSGGRDVA ELFYRKLTGL PGGESPVVMY HDDRHFIHIR
HSGLYLVATT SENVSPFSLL ELLSRLATLL GDYCGSLNEG TISRNVALVY ELLDEVLDYG
YVQTTSTDML RNFIQTEAAV SKPFSLFDLS SVGLFGAETQ QNRVAPSSAA SRPVLSSRSD
QSQKNEVFLD VVERLSVLIA SNGSLLKVDV QGEIRLKSFL PSSSEICIGL TEEFCVGKSE
LRGYGPGIRV DEVSFHSSVN LDEFESHRIL HLQPPQGELT VMRYQLSDDL PSPLPFRLFP
SVQWDQGSGR LQVYLKLRCD LPPKSQALNI HLHLPLPRGV VSLSQELSSP DQKAELGEGA
LHWDLPRVQG GSQLSGLFQM DVPGLQGPPS RGPSPSAPPL GLGPASLSFE LPRHTCSGLQ
VRFLRLSFSA CGNANPHKWV RHLSHSNAYV IRI
