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AP-4 complex subunit mu-1 (AP-4 adaptor complex mu subunit) (Adaptor-related protein complex 4 subunit mu-1) (Mu subunit of AP-4) (Mu-adaptin-related protein 2) (mu-ARP2) (Mu4-adaptin) (mu4)

 AP4M1_HUMAN             Reviewed;         453 AA.
O00189; D6W5U1; Q8WV65; Q9UHK9;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
17-APR-2007, sequence version 2.
12-SEP-2018, entry version 155.
RecName: Full=AP-4 complex subunit mu-1 {ECO:0000305};
AltName: Full=AP-4 adaptor complex mu subunit;
AltName: Full=Adaptor-related protein complex 4 subunit mu-1;
AltName: Full=Mu subunit of AP-4;
AltName: Full=Mu-adaptin-related protein 2;
Short=mu-ARP2;
AltName: Full=Mu4-adaptin;
Short=mu4;
Name=AP4M1 {ECO:0000312|HGNC:HGNC:574}; Synonyms=MUARP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=9013859; DOI=10.1016/S0014-5793(96)01500-1;
Wang X., Kilimann M.W.;
"Identification of two new mu-adaptin-related proteins, mu-ARP1 and
mu-ARP2.";
FEBS Lett. 402:57-61(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
TISSUE=Brain;
PubMed=10436028; DOI=10.1091/mbc.10.8.2787;
Hirst J., Bright N.A., Rous B., Robinson M.S.;
"Characterization of a fourth adaptor-related protein complex.";
Mol. Biol. Cell 10:2787-2802(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH LAMP2, AND
SUBCELLULAR LOCATION.
TISSUE=Spleen;
PubMed=11139587; DOI=10.1074/jbc.M010591200;
Aguilar R.C., Boehm M., Gorshkova I., Crouch R.J., Tomita K.,
Saito T., Ohno H., Bonifacino J.S.;
"Signal-binding specificity of the mu4 subunit of the adaptor protein
complex, AP-4.";
J. Biol. Chem. 276:13145-13152(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, AND SUBUNIT.
PubMed=10066790; DOI=10.1074/jbc.274.11.7278;
Dell'Angelica E.C., Mullins C., Bonifacino J.S.;
"AP-4, a novel protein complex related to clathrin adaptors.";
J. Biol. Chem. 274:7278-7285(1999).
[7]
INVOLVEMENT IN SPG50.
PubMed=19559397; DOI=10.1016/j.ajhg.2009.06.004;
Verkerk A.J., Schot R., Dumee B., Schellekens K., Swagemakers S.,
Bertoli-Avella A.M., Lequin M.H., Dudink J., Govaert P.,
van Zwol A.L., Hirst J., Wessels M.W., Catsman-Berrevoets C.,
Verheijen F.W., de Graaff E., de Coo I.F., Kros J.M., Willemsen R.,
Willems P.J., van der Spek P.J., Mancini G.M.;
"Mutation in the AP4M1 gene provides a model for neuroaxonal injury in
cerebral palsy.";
Am. J. Hum. Genet. 85:40-52(2009).
[8]
FUNCTION, AND SUBUNIT.
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).
[9]
FUNCTION, AND INTERACTION WITH NAGPA.
PubMed=26544806; DOI=10.1016/j.ajhg.2015.10.007;
Raza M.H., Mattera R., Morell R., Sainz E., Rahn R., Gutierrez J.,
Paris E., Root J., Solomon B., Brewer C., Basra M.A., Khan S.,
Riazuddin S., Braun A., Bonifacino J.S., Drayna D.;
"Association between rare variants in AP4E1, a component of
intracellular trafficking, and persistent stuttering.";
Am. J. Hum. Genet. 97:715-725(2015).
[10]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 160-453 IN COMPLEX WITH APP
PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-255 AND
ARG-283, AND SUBUNIT.
PubMed=20230749; DOI=10.1016/j.devcel.2010.01.015;
Burgos P.V., Mardones G.A., Rojas A.L., daSilva L.L., Prabhu Y.,
Hurley J.H., Bonifacino J.S.;
"Sorting of the Alzheimer's disease amyloid precursor protein mediated
by the AP-4 complex.";
Dev. Cell 18:425-436(2010).
-!- 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
(PubMed:10436028, PubMed:11139587, PubMed:10066790,
PubMed:11802162, PubMed:20230749). 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
(PubMed:11139587, PubMed:20230749). It is also involved in protein
sorting to the basolateral membrane in epithelial cells and the
proper asymmetric localization of somatodendritic proteins in
neurons (By similarity). 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
(PubMed:10436028, PubMed:11139587, PubMed:26544806,
PubMed:20230749). The adaptor protein complex 4 (AP-4) may also
recognize other types of sorting signal (By similarity).
{ECO:0000250|UniProtKB:E2RED8, ECO:0000250|UniProtKB:Q2PWT8,
ECO:0000250|UniProtKB:Q9JKC7, ECO:0000269|PubMed:10066790,
ECO:0000269|PubMed:10436028, ECO:0000269|PubMed:11139587,
ECO:0000269|PubMed:11802162, ECO:0000269|PubMed:20230749,
ECO:0000269|PubMed:26544806}.
-!- 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) (PubMed:10436028,
PubMed:10066790, PubMed:11802162). Interacts with tyrosine-based
sorting signals on the cytoplasmic tail of cargo proteins such as
APP, LAMP2 and NAGPA (PubMed:11139587, PubMed:26544806,
PubMed:20230749). Interacts with the C-terminal domain of GRID2
(By similarity). Interacts with GRIA1 and GRIA2; the interaction
is indirect via CACNG3 (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q2PWT8,
ECO:0000250|UniProtKB:Q9JKC7, ECO:0000269|PubMed:10066790,
ECO:0000269|PubMed:10436028, ECO:0000269|PubMed:11139587,
ECO:0000269|PubMed:11802162, ECO:0000269|PubMed:20230749,
ECO:0000269|PubMed:26544806}.
-!- INTERACTION:
Q96K76:USP47; NbExp=3; IntAct=EBI-3914106, EBI-2514143;
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane {ECO:0000269|PubMed:20230749}; Peripheral membrane
protein {ECO:0000305}. Early endosome
{ECO:0000269|PubMed:20230749}. Note=Found in soma and dendritic
shafts of neuronal cells. {ECO:0000250|UniProtKB:Q2PWT8}.
-!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in testis and
lowly expressed in brain and lung. {ECO:0000269|PubMed:9013859}.
-!- DISEASE: Spastic paraplegia 50, autosomal recessive (SPG50)
[MIM:612936]: A form of spastic paraplegia, a neurodegenerative
disorder characterized by a slow, gradual, progressive weakness
and spasticity of the lower limbs. Rate of progression and the
severity of symptoms are quite variable. Initial symptoms may
include difficulty with balance, weakness and stiffness in the
legs, muscle spasms, and dragging the toes when walking. In some
forms of the disorder, bladder symptoms (such as incontinence) may
appear, or the weakness and stiffness may spread to other parts of
the body. SPG50 affected individuals present postnatally with
early infantile hypotonia, delayed psychomotor development,
strabismus, lack of independent walking and severe mental
retardation. They develop progressive spasticity of all limbs with
generalized hypertonia, hyperreflexia, and extensor plantar
responses by the end of the first year of life. Speech is absent
or limited. Pseudobulbar signs, such as drooling, stereotypic
laughter, and exaggerated jaw jerk, are part of the clinical
picture. {ECO:0000269|PubMed:19559397}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the adaptor complexes medium subunit
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y08387; CAA69667.1; -; mRNA.
EMBL; AF155158; AAD43328.1; -; mRNA.
EMBL; AF020796; AAD25869.1; -; mRNA.
EMBL; CH471091; EAW76594.1; -; Genomic_DNA.
EMBL; CH471091; EAW76597.1; -; Genomic_DNA.
EMBL; BC018705; AAH18705.1; -; mRNA.
CCDS; CCDS5685.1; -.
RefSeq; NP_004713.2; NM_004722.3.
UniGene; Hs.632317; -.
PDB; 3L81; X-ray; 1.60 A; A=160-453.
PDB; 4MDR; X-ray; 1.85 A; A=160-453.
PDBsum; 3L81; -.
PDBsum; 4MDR; -.
ProteinModelPortal; O00189; -.
SMR; O00189; -.
BioGrid; 114616; 34.
CORUM; O00189; -.
IntAct; O00189; 31.
MINT; O00189; -.
STRING; 9606.ENSP00000352603; -.
iPTMnet; O00189; -.
PhosphoSitePlus; O00189; -.
BioMuta; AP4M1; -.
EPD; O00189; -.
MaxQB; O00189; -.
PaxDb; O00189; -.
PeptideAtlas; O00189; -.
PRIDE; O00189; -.
ProteomicsDB; 47769; -.
TopDownProteomics; O00189; -.
DNASU; 9179; -.
Ensembl; ENST00000359593; ENSP00000352603; ENSG00000221838.
Ensembl; ENST00000421755; ENSP00000412185; ENSG00000221838.
GeneID; 9179; -.
KEGG; hsa:9179; -.
UCSC; uc003utb.5; human.
CTD; 9179; -.
DisGeNET; 9179; -.
EuPathDB; HostDB:ENSG00000221838.9; -.
GeneCards; AP4M1; -.
HGNC; HGNC:574; AP4M1.
HPA; HPA066774; -.
MalaCards; AP4M1; -.
MIM; 602296; gene.
MIM; 612936; phenotype.
neXtProt; NX_O00189; -.
OpenTargets; ENSG00000221838; -.
Orphanet; 280763; Severe intellectual disability and progressive spastic paraplegia.
PharmGKB; PA24866; -.
eggNOG; KOG0937; Eukaryota.
eggNOG; ENOG410XPFS; LUCA.
GeneTree; ENSGT00530000062779; -.
HOGENOM; HOG000173245; -.
HOVERGEN; HBG102734; -.
InParanoid; O00189; -.
KO; K12402; -.
PhylomeDB; O00189; -.
TreeFam; TF329745; -.
Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
SignaLink; O00189; -.
ChiTaRS; AP4M1; human.
EvolutionaryTrace; O00189; -.
GeneWiki; AP4M1; -.
GenomeRNAi; 9179; -.
PRO; PR:O00189; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000221838; Expressed in 136 organ(s), highest expression level in right testis.
CleanEx; HS_AP4M1; -.
ExpressionAtlas; O00189; baseline and differential.
Genevisible; O00189; HS.
GO; GO:0030124; C:AP-4 adaptor complex; IDA:UniProtKB.
GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0031904; C:endosome lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0019904; F:protein domain specific binding; IDA:UniProtKB.
GO; GO:0006895; P:Golgi to endosome transport; IMP:UniProtKB.
GO; GO:0090160; P:Golgi to lysosome transport; IDA:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
GO; GO:0008104; P:protein localization; ISS:UniProtKB.
GO; GO:1903361; P:protein localization to basolateral plasma membrane; ISS:UniProtKB.
GO; GO:0006605; P:protein targeting; IDA:UniProtKB.
GO; GO:0006622; P:protein targeting to lysosome; IDA:UniProtKB.
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.
1: Evidence at protein level;
3D-structure; Complete proteome; Endosome; Golgi apparatus;
Hereditary spastic paraplegia; Membrane; Neurodegeneration;
Protein transport; Reference proteome; Transport.
CHAIN 1 453 AP-4 complex subunit mu-1.
/FTId=PRO_0000193787.
DOMAIN 184 452 MHD. {ECO:0000255|PROSITE-
ProRule:PRU00404}.
MUTAGEN 255 255 F->A: Abolishes interaction with APP.
{ECO:0000269|PubMed:20230749}.
MUTAGEN 283 283 R->D: Strongly reduced interaction with
APP. {ECO:0000269|PubMed:20230749}.
CONFLICT 338 338 R -> G (in Ref. 2; AAD43328).
{ECO:0000305}.
CONFLICT 345 345 Q -> R (in Ref. 1; CAA69667 and 3;
AAD25869). {ECO:0000305}.
CONFLICT 400 400 L -> M (in Ref. 2; AAD43328).
{ECO:0000305}.
CONFLICT 417 417 S -> C (in Ref. 2; AAD43328).
{ECO:0000305}.
STRAND 186 199 {ECO:0000244|PDB:3L81}.
STRAND 205 218 {ECO:0000244|PDB:3L81}.
STRAND 225 230 {ECO:0000244|PDB:3L81}.
STRAND 235 237 {ECO:0000244|PDB:3L81}.
TURN 240 242 {ECO:0000244|PDB:3L81}.
STRAND 246 256 {ECO:0000244|PDB:3L81}.
HELIX 264 267 {ECO:0000244|PDB:3L81}.
STRAND 269 272 {ECO:0000244|PDB:3L81}.
STRAND 276 286 {ECO:0000244|PDB:3L81}.
STRAND 295 304 {ECO:0000244|PDB:3L81}.
TURN 306 308 {ECO:0000244|PDB:3L81}.
STRAND 309 319 {ECO:0000244|PDB:3L81}.
STRAND 326 335 {ECO:0000244|PDB:3L81}.
STRAND 341 349 {ECO:0000244|PDB:3L81}.
STRAND 353 357 {ECO:0000244|PDB:3L81}.
STRAND 360 365 {ECO:0000244|PDB:3L81}.
STRAND 373 381 {ECO:0000244|PDB:3L81}.
STRAND 405 412 {ECO:0000244|PDB:3L81}.
STRAND 421 427 {ECO:0000244|PDB:3L81}.
STRAND 437 451 {ECO:0000244|PDB:3L81}.
SEQUENCE 453 AA; 49977 MW; AE3DCA8C5AED08B7 CRC64;
MISQFFILSS KGDPLIYKDF RGDSGGRDVA ELFYRKLTGL PGDESPVVMH HHGRHFIHIR
HSGLYLVVTT SENVSPFSLL ELLSRLATLL GDYCGSLGEG TISRNVALVY ELLDEVLDYG
YVQTTSTEML RNFIQTEAVV SKPFSLFDLS SVGLFGAETQ QSKVAPSSAA SRPVLSSRSD
QSQKNEVFLD VVERLSVLIA SNGSLLKVDV QGEIRLKSFL PSGSEMRIGL TEEFCVGKSE
LRGYGPGIRV DEVSFHSSVN LDEFESHRIL RLQPPQGELT VMRYQLSDDL PSPLPFRLFP
SVQWDRGSGR LQVYLKLRCD LLSKSQALNV RLHLPLPRGV VSLSQELSSP EQKAELAEGA
LRWDLPRVQG GSQLSGLFQM DVPGPPGPPS HGLSTSASPL GLGPASLSFE LPRHTCSGLQ
VRFLRLAFRP CGNANPHKWV RHLSHSDAYV IRI


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