ID   AP3M1_MOUSE             Reviewed;         418 AA.
AC   Q9JKC8; Q5BKQ6;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 158.
DE   RecName: Full=AP-3 complex subunit mu-1;
DE   AltName: Full=AP-3 adaptor complex mu3A subunit;
DE   AltName: Full=Adaptor-related protein complex 3 subunit mu-1;
DE   AltName: Full=Mu-adaptin 3A;
DE   AltName: Full=Mu3A-adaptin;
GN   Name=Ap3m1;
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   "Mouse medium chain clathrin adaptor protein mu3A.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland, and Testis;
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   INTERACTION WITH AGAP1.
RX   PubMed=12967569; DOI=10.1016/s1534-5807(03)00234-x;
RA   Nie Z., Boehm M., Boja E.S., Vass W.C., Bonifacino J.S., Fales H.M.,
RA   Randazzo P.A.;
RT   "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP
RT   AGAP1.";
RL   Dev. Cell 5:513-521(2003).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   FUNCTION, AND ASSOCIATION WITH THE BLOC-1 COMPLEX.
RX   PubMed=21998198; DOI=10.1091/mbc.e11-07-0592;
RA   Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A., Craige B.,
RA   Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.;
RT   "The schizophrenia susceptibility factor dysbindin and its associated
RT   complex sort cargoes from cell bodies to the synapse.";
RL   Mol. Biol. Cell 22:4854-4867(2011).
CC   -!- FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is
CC       not clathrin-associated. The complex is associated with the Golgi
CC       region as well as more peripheral structures. It facilitates the
CC       budding of vesicles from the Golgi membrane and may be directly
CC       involved in trafficking to lysosomes. In concert with the BLOC-1
CC       complex, AP-3 is required to target cargos into vesicles assembled at
CC       cell bodies for delivery into neurites and nerve terminals.
CC       {ECO:0000269|PubMed:21998198}.
CC   -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed
CC       of two large adaptins (delta-type subunit AP3D1 and beta-type subunit
CC       AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and
CC       a small adaptin (sigma-type subunit APS1 or AP3S2). Interacts with
CC       AGAP1. AP-3 associates with the BLOC-1 complex.
CC       {ECO:0000269|PubMed:12967569}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=Component of the coat surrounding the
CC       cytoplasmic face of coated vesicles located at the Golgi complex.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AF242857; AAF63512.1; -; mRNA.
DR   EMBL; BC024595; AAH24595.1; -; mRNA.
DR   EMBL; BC090983; AAH90983.1; -; mRNA.
DR   CCDS; CCDS26861.1; -.
DR   RefSeq; NP_061299.3; NM_018829.4.
DR   RefSeq; XP_006519355.1; XM_006519292.1.
DR   RefSeq; XP_006519356.1; XM_006519293.1.
DR   AlphaFoldDB; Q9JKC8; -.
DR   SMR; Q9JKC8; -.
DR   BioGRID; 207741; 5.
DR   ComplexPortal; CPX-5145; Ubiquitous AP-3 Adaptor complex, sigma3a variant.
DR   ComplexPortal; CPX-5146; Ubiquitous AP-3 Adaptor complex, sigma3b variant.
DR   CORUM; Q9JKC8; -.
DR   IntAct; Q9JKC8; 4.
DR   MINT; Q9JKC8; -.
DR   STRING; 10090.ENSMUSP00000117346; -.
DR   iPTMnet; Q9JKC8; -.
DR   PhosphoSitePlus; Q9JKC8; -.
DR   SwissPalm; Q9JKC8; -.
DR   EPD; Q9JKC8; -.
DR   jPOST; Q9JKC8; -.
DR   MaxQB; Q9JKC8; -.
DR   PaxDb; 10090-ENSMUSP00000117346; -.
DR   PeptideAtlas; Q9JKC8; -.
DR   ProteomicsDB; 282133; -.
DR   Pumba; Q9JKC8; -.
DR   Antibodypedia; 45437; 145 antibodies from 28 providers.
DR   DNASU; 55946; -.
DR   Ensembl; ENSMUST00000154460.8; ENSMUSP00000117346.2; ENSMUSG00000021824.14.
DR   GeneID; 55946; -.
DR   KEGG; mmu:55946; -.
DR   UCSC; uc007sla.2; mouse.
DR   AGR; MGI:1929212; -.
DR   CTD; 26985; -.
DR   MGI; MGI:1929212; Ap3m1.
DR   VEuPathDB; HostDB:ENSMUSG00000021824; -.
DR   eggNOG; KOG2740; Eukaryota.
DR   GeneTree; ENSGT00940000158184; -.
DR   HOGENOM; CLU_026996_6_2_1; -.
DR   InParanoid; Q9JKC8; -.
DR   OMA; INVHFTI; -.
DR   OrthoDB; 831588at2759; -.
DR   PhylomeDB; Q9JKC8; -.
DR   TreeFam; TF315187; -.
DR   BioGRID-ORCS; 55946; 3 hits in 78 CRISPR screens.
DR   ChiTaRS; Ap3m1; mouse.
DR   PRO; PR:Q9JKC8; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q9JKC8; Protein.
DR   Bgee; ENSMUSG00000021824; Expressed in ectoplacental cone and 260 other cell types or tissues.
DR   ExpressionAtlas; Q9JKC8; baseline and differential.
DR   GO; GO:0030123; C:AP-3 adaptor complex; NAS:ComplexPortal.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005769; C:early endosome; NAS:ComplexPortal.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR   GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
DR   GO; GO:0048490; P:anterograde synaptic vesicle transport; IMP:UniProtKB.
DR   GO; GO:0035654; P:clathrin-coated vesicle cargo loading, AP-3-mediated; NAS:ComplexPortal.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0046907; P:intracellular transport; NAS:ComplexPortal.
DR   GO; GO:1903232; P:melanosome assembly; NAS:ComplexPortal.
DR   GO; GO:0060155; P:platelet dense granule organization; NAS:ComplexPortal.
DR   GO; GO:0016192; P:vesicle-mediated transport; NAS:ComplexPortal.
DR   CDD; cd09260; AP-3_Mu3A_Cterm; 1.
DR   CDD; cd14837; AP3_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; 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   PANTHER; PTHR10529; AP COMPLEX SUBUNIT MU; 1.
DR   PANTHER; PTHR10529:SF342; AP-3 COMPLEX SUBUNIT MU-1; 1.
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; Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor; 1.
DR   SUPFAM; SSF64356; SNARE-like; 1.
DR   PROSITE; PS00990; CLAT_ADAPTOR_M_1; 1.
DR   PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR   PROSITE; PS51072; MHD; 1.
DR   Genevisible; Q9JKC8; MM.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Golgi apparatus; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..418
FT                   /note="AP-3 complex subunit mu-1"
FT                   /id="PRO_0000193782"
FT   DOMAIN          176..417
FT                   /note="MHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
SQ   SEQUENCE   418 AA;  46936 MW;  69EC322D820C47D3 CRC64;
     MIHSLFLINC SGDIFLEKHW KSVVSQSVCD YFFEAQEKAA DVENVPPVIS TPHHYLISIY
     RDKLFFVSVI QTEVPPLFVI EFLHRVADTF QDYFGECSEA AIKDNVVIVY ELLEEMLDNG
     FPLATESNIL KELIKPPTIL RSVVNSITGS SNVGDTLPTG QLSNIPWRRA GVKYTNNEAY
     FDVVEEIDAI IDKSGSTVFA EIQGVIDACI KLSGMPDLSL SFMNPRLLDD VSFHPCIRFK
     RWESERVLSF IPPDGNFRLI SYRVSSQNLV AIPVYVKHSI SFKENSSCGR FDITIGPKQN
     MGKTIEGITV TVHMPKVVLN MNLTPTQGSY TFDPVTKVLA WDVGKITPQK LPSLKGLVNL
     QSGAPKPEEN PNLNIQFKIQ QLAISGLKVN RLDMYGEKYK PFKGVKYVTK AGKFQVRT
//