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AP-4 complex subunit mu-1

 AP4M1_CANLF             Reviewed;         452 AA.
E2RED8;
22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
31-OCT-2012, sequence version 2.
28-MAR-2018, entry version 52.
RecName: Full=AP-4 complex subunit mu-1 {ECO:0000305};
Name=AP4M1 {ECO:0000250|UniProtKB:O00189};
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Boxer;
PubMed=16341006; DOI=10.1038/nature04338;
Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
"Genome sequence, comparative analysis and haplotype structure of the
domestic dog.";
Nature 438:803-819(2005).
[2]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11802162; DOI=10.1038/ncb745;
Simmen T., Hoening S., Icking A., Tikkanen R., Hunziker W.;
"AP-4 binds basolateral signals and participates in basolateral
sorting in epithelial MDCK cells.";
Nat. Cell Biol. 4:154-159(2002).
-!- 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 (By similarity). It is also involved in protein
sorting to the basolateral membrane in epithelial cells and the
proper asymmetric localization of somatodendritic proteins in
neurons (PubMed:11802162). Within AP-4, the mu-type subunit AP4M1
is directly involved in the recognition and binding of tyrosine-
based sorting signals found in the cytoplasmic part of cargos. The
adaptor protein complex 4 (AP-4) may also recognize other types of
sorting signal (By similarity). {ECO:0000250|UniProtKB:O00189,
ECO:0000269|PubMed:11802162}.
-!- 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 tyrosine-
based sorting signals on the cytoplasmic tail of cargo proteins
such as APP, LAMP2 and NAGPA. Interacts with the C-terminal domain
of GRID2. Interacts with GRIA1 and GRIA2; the interaction is
indirect via CACNG3. Interacts with CACNG3; CACNG3 associates
GRIA1 and GRIA2 with the adaptor protein complex 4 (AP-4) to
target them to the somatodendritic compartment of neurons.
{ECO:0000250|UniProtKB:O00189}.
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane {ECO:0000269|PubMed:11802162}; Peripheral membrane
protein {ECO:0000305}. Early endosome
{ECO:0000269|PubMed:11802162}. Note=Found in soma and dendritic
shafts of neuronal cells. {ECO:0000250|UniProtKB:Q2PWT8}.
-!- SIMILARITY: Belongs to the adaptor complexes medium subunit
family. {ECO:0000255|SAAS:SAAS00535636}.
-----------------------------------------------------------------------
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EMBL; AAEX03004275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; XP_546965.2; XM_546965.4.
ProteinModelPortal; E2RED8; -.
STRING; 9615.ENSCAFP00000021690; -.
PaxDb; E2RED8; -.
Ensembl; ENSCAFT00000023359; ENSCAFP00000021690; ENSCAFG00000014674.
GeneID; 489847; -.
CTD; 9179; -.
VGNC; VGNC:37970; AP4M1.
eggNOG; KOG0937; Eukaryota.
eggNOG; ENOG410XPFS; LUCA.
GeneTree; ENSGT00530000062779; -.
InParanoid; E2RED8; -.
OMA; IHIRHSG; -.
OrthoDB; EOG091G0ISV; -.
TreeFam; TF329745; -.
Reactome; R-CFA-432720; Lysosome Vesicle Biogenesis.
Proteomes; UP000002254; Chromosome 6.
Bgee; ENSCAFG00000014674; -.
GO; GO:0030124; C:AP-4 adaptor complex; ISS:UniProtKB.
GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0006895; P:Golgi to endosome transport; IEA:Ensembl.
GO; GO:0090160; P:Golgi to lysosome transport; ISS:UniProtKB.
GO; GO:0008104; P:protein localization; ISS:UniProtKB.
GO; GO:1903361; P:protein localization to basolateral plasma membrane; IMP:UniProtKB.
GO; GO:0006605; P:protein targeting; IDA:UniProtKB.
GO; GO:0006622; P:protein targeting to lysosome; IEA:Ensembl.
InterPro; IPR036168; AP2_Mu_C_sf.
InterPro; IPR022775; AP_mu_sigma_su.
InterPro; IPR001392; Clathrin_mu.
InterPro; IPR018240; Clathrin_mu_CS.
InterPro; IPR011012; Longin-like_dom_sf.
InterPro; IPR028565; MHD.
Pfam; PF00928; Adap_comp_sub; 1.
Pfam; PF01217; Clat_adaptor_s; 1.
PIRSF; PIRSF005992; Clathrin_mu; 1.
PRINTS; PR00314; CLATHRINADPT.
SUPFAM; SSF49447; SSF49447; 1.
SUPFAM; SSF64356; SSF64356; 1.
PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
PROSITE; PS51072; MHD; 1.
3: Inferred from homology;
Complete proteome; Endosome; Golgi apparatus; Membrane;
Protein transport; Reference proteome; Transport.
CHAIN 1 452 AP-4 complex subunit mu-1.
/FTId=PRO_0000442254.
DOMAIN 184 451 MHD. {ECO:0000255|PROSITE-
ProRule:PRU00404}.
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


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