ID   AP4M1_CANLF             Reviewed;         452 AA.
AC   E2RED8;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=AP-4 complex subunit mu-1 {ECO:0000305};
GN   Name=AP4M1 {ECO:0000250|UniProtKB:O00189};
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer;
RX   PubMed=16341006; DOI=10.1038/nature04338;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA   Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA   Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA   Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA   Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA   Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA   Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA   Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA   Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA   Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA   Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA   Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA   Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA   Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA   Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA   Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA   Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA   Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA   Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA   LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA   Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA   Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA   Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA   Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA   Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA   Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA   Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA   Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA   Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA   Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA   Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA   Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA   Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11802162; DOI=10.1038/ncb745;
RA   Simmen T., Hoening S., Icking A., Tikkanen R., Hunziker W.;
RT   "AP-4 binds basolateral signals and participates in basolateral sorting in
RT   epithelial MDCK cells.";
RL   Nat. Cell Biol. 4:154-159(2002).
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:11802162). 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:11802162}.
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. Interacts with
CC       GRIA1 and GRIA2; the interaction is indirect via CACNG3. Interacts with
CC       CACNG3; CACNG3 associates GRIA1 and GRIA2 with the adaptor protein
CC       complex 4 (AP-4) to target them to the somatodendritic compartment of
CC       neurons. Interacts with HOOK1 and HOOK2; the interactions are direct,
CC       mediate the interaction between FTS-Hook-FHIP (FHF) complex and AP-4
CC       and the perinuclear distribution of AP-4 (By similarity).
CC       {ECO:0000250|UniProtKB:O00189}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000269|PubMed:11802162}; Peripheral membrane protein
CC       {ECO:0000305}. Early endosome {ECO:0000269|PubMed:11802162}. Note=Found
CC       in soma and dendritic shafts of neuronal cells.
CC       {ECO:0000250|UniProtKB:Q2PWT8}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC       {ECO:0000255}.
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DR   EMBL; AAEX03004275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_546965.2; XM_546965.4.
DR   AlphaFoldDB; E2RED8; -.
DR   SMR; E2RED8; -.
DR   STRING; 9612.ENSCAFP00000021690; -.
DR   PaxDb; E2RED8; -.
DR   eggNOG; KOG0937; Eukaryota.
DR   HOGENOM; CLU_026996_5_0_1; -.
DR   InParanoid; E2RED8; -.
DR   OMA; NVCATIP; -.
DR   OrthoDB; 662490at2759; -.
DR   TreeFam; TF329745; -.
DR   Proteomes; UP000002254; Unplaced.
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; IDA:UniProtKB.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR   GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR   GO; GO:0090160; P:Golgi to lysosome transport; ISS:UniProtKB.
DR   GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR   GO; GO:1903361; P:protein localization to basolateral plasma membrane; IMP:UniProtKB.
DR   GO; GO:0006605; P:protein targeting; IDA:UniProtKB.
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   3: Inferred from homology;
KW   Endosome; Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..452
FT                   /note="AP-4 complex subunit mu-1"
FT                   /id="PRO_0000442254"
FT   DOMAIN          184..451
FT                   /note="MHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
SQ   SEQUENCE   452 AA;  49894 MW;  CFD23BDD6A14F1DA CRC64;
     MISQFFILSS KGDPLIYKDF RGDSGGRDVA ELFYRKLTGL PGDESPVVMH HDDRHFIHIR
     HSGLYLVATT SENISPFSLL ELLSRLATLL GDYCGSLSEG TISRNVALVY ELLDEVLDYG
     YVQTTSMEML RNFIQTEAVV SKPFSLFDLS SVGLFGAETQ QSKVAPSTAA SRPVLASRSD
     QSQKNEVFLD VVERLSVLIA SNGSLLKVDV QGEIRLKSFL PSGSEMRIGL TEEFCVGKSE
     LRGYGPGIRV DEVSFHSSVL LEEFESHRIL RLQPPQGELT VMRYQLSDDL PSPLPFRLFP
     SVQWDRGSGR LQVYLKLRCD LPPKSQALNV RLHLPLPRGV VSLSQELSGP EQKAELGEGA
     LRWDLPRVQG GSQLSGLFQM DVPGLPGPPG QGHSATAPLG LGPASLSFEL PRHTCSGLQV
     RFLRLAFRPC GSTSPHKWVR HLSHSDAYVI RI