ID   AP1M1_MOUSE             Reviewed;         423 AA.
AC   P35585;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 185.
DE   RecName: Full=AP-1 complex subunit mu-1;
DE   AltName: Full=AP-mu chain family member mu1A;
DE   AltName: Full=Adaptor protein complex AP-1 subunit mu-1;
DE   AltName: Full=Adaptor-related protein complex 1 subunit mu-1;
DE   AltName: Full=Clathrin assembly protein complex 1 mu-1 medium chain 1;
DE   AltName: Full=Clathrin coat assembly protein AP47;
DE   AltName: Full=Clathrin coat-associated protein AP47;
DE   AltName: Full=Golgi adaptor HA1/AP1 adaptin mu-1 subunit;
DE   AltName: Full=Mu-adaptin 1;
DE   AltName: Full=Mu1A-adaptin;
GN   Name=Ap1m1; Synonyms=Cltnm;
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].
RX   PubMed=1761056; DOI=10.1111/j.1432-1033.1991.tb16409.x;
RA   Nakayama Y., Goebl M., O'Brine Greco B., Lemmon S., Pingchang C.E.,
RA   Kirchhausen T.;
RT   "The medium chains of the mammalian clathrin-associated proteins have a
RT   homolog in yeast.";
RL   Eur. J. Biochem. 202:569-574(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10640811; DOI=10.1159/000015391;
RA   Nakatsu F., Kadohira T., Gilbert D.J., Jenkins N.A., Kakuta H.,
RA   Copeland N.G., Saito T., Ohno H.;
RT   "Genomic structure and chromosome mapping of the genes encoding clathrin-
RT   associated adaptor medium chains mu1A (Ap1m1) and mu1B (Ap1m2).";
RL   Cytogenet. Cell Genet. 87:53-58(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-152 AND THR-154, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-152 AND THR-154, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   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   [6] {ECO:0007744|PDB:7R4H}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.34 ANGSTROMS) IN COMPLEX WITH AP-1
RP   COMPLEX AND STING1, FUNCTION, AND SUBUNIT.
RX   PubMed=36261523; DOI=10.1038/s41586-022-05354-0;
RA   Liu Y., Xu P., Rivara S., Liu C., Ricci J., Ren X., Hurley J.H.,
RA   Ablasser A.;
RT   "Clathrin-associated AP-1 controls termination of STING signalling.";
RL   Nature 610:761-767(2022).
CC   -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that
CC       plays a role in protein sorting in the trans-Golgi network (TGN) and
CC       endosomes (PubMed:36261523). The AP complexes mediate the recruitment
CC       of clathrin to membranes and the recognition of sorting signals within
CC       the cytosolic tails of transmembrane cargo molecules (PubMed:36261523).
CC       {ECO:0000269|PubMed:36261523}.
CC   -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC       of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit
CC       AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small
CC       adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3) (PubMed:36261523).
CC       Interacts with MARCHF11 (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:36261523}.
CC   -!- INTERACTION:
CC       P35585; P22892: Ap1g1; NbExp=6; IntAct=EBI-1040251, EBI-1040262;
CC       P35585; Q10567: AP1B1; Xeno; NbExp=5; IntAct=EBI-1040251, EBI-1171303;
CC       P35585; Q10589: BST2; Xeno; NbExp=2; IntAct=EBI-1040251, EBI-2476339;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle, clathrin-
CC       coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
CC       Note=Component of the coat surrounding the cytoplasmic face of coated
CC       vesicles located at the Golgi complex.
CC   -!- PTM: Phosphorylation of membrane-bound AP1M1/AP1M2 increases its
CC       affinity for sorting signals. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC       {ECO:0000305}.
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DR   EMBL; M62419; AAA37244.1; -; mRNA.
DR   EMBL; AF139405; AAF61814.1; -; Genomic_DNA.
DR   EMBL; AF139394; AAF61814.1; JOINED; Genomic_DNA.
DR   EMBL; AF139395; AAF61814.1; JOINED; Genomic_DNA.
DR   EMBL; AF139396; AAF61814.1; JOINED; Genomic_DNA.
DR   EMBL; AF139397; AAF61814.1; JOINED; Genomic_DNA.
DR   EMBL; AF139398; AAF61814.1; JOINED; Genomic_DNA.
DR   EMBL; AF139399; AAF61814.1; JOINED; Genomic_DNA.
DR   EMBL; AF139400; AAF61814.1; JOINED; Genomic_DNA.
DR   EMBL; AF139401; AAF61814.1; JOINED; Genomic_DNA.
DR   EMBL; AF139402; AAF61814.1; JOINED; Genomic_DNA.
DR   EMBL; AF139403; AAF61814.1; JOINED; Genomic_DNA.
DR   EMBL; AF139404; AAF61814.1; JOINED; Genomic_DNA.
DR   EMBL; BC003823; AAH03823.1; -; mRNA.
DR   CCDS; CCDS22411.1; -.
DR   PIR; S19693; S19693.
DR   RefSeq; NP_031482.1; NM_007456.5.
DR   PDB; 1W63; X-ray; 4.00 A; M/N/O/P/R/V=1-423.
DR   PDB; 4EMZ; X-ray; 2.90 A; A/M=158-423.
DR   PDB; 4EN2; X-ray; 2.58 A; A/M=158-423.
DR   PDB; 4HMY; X-ray; 7.00 A; M=1-423.
DR   PDB; 4P6Z; X-ray; 3.00 A; M=1-423.
DR   PDB; 6CM9; EM; 3.73 A; M=1-423.
DR   PDB; 6CRI; EM; 6.80 A; M/W/X=2-423.
DR   PDB; 6D83; EM; 4.27 A; M=1-423.
DR   PDB; 6D84; EM; 6.72 A; M/P=1-423.
DR   PDB; 6DFF; EM; 3.90 A; M=1-423.
DR   PDB; 7R4H; EM; 2.34 A; M=1-423.
DR   PDB; 7UX3; EM; 9.60 A; M=2-423.
DR   PDB; 8D4C; EM; 9.30 A; J/M=1-423.
DR   PDB; 8D4D; EM; 9.60 A; J/M=1-423.
DR   PDB; 8D4E; EM; 9.20 A; M=2-423.
DR   PDB; 8D4F; EM; 9.80 A; J/M=1-423.
DR   PDB; 8D4G; EM; 11.60 A; J/M=1-423.
DR   PDB; 8D9R; EM; 20.00 A; M/j/k/l/m/n=1-423.
DR   PDB; 8D9S; EM; 20.00 A; M/j/k/l/m/n=1-423.
DR   PDB; 8D9T; EM; 20.00 A; M/i/j/k/l/m=1-423.
DR   PDB; 8D9U; EM; 20.00 A; M/i/j/k/l/m=1-423.
DR   PDB; 8D9V; EM; 9.40 A; J/M=1-423.
DR   PDB; 8D9W; EM; 9.30 A; M/X/Z/a=1-423.
DR   AlphaFoldDB; P35585; -.
DR   EMDB; EMD-14312; -.
DR   EMDB; EMD-26853; -.
DR   EMDB; EMD-27181; -.
DR   EMDB; EMD-27182; -.
DR   EMDB; EMD-27183; -.
DR   EMDB; EMD-27184; -.
DR   EMDB; EMD-27185; -.
DR   EMDB; EMD-7563; -.
DR   SMR; P35585; -.
DR   BioGRID; 198125; 18.
DR   ComplexPortal; CPX-5141; Ubiquitous AP-1 Adaptor complex, sigma1a variant.
DR   ComplexPortal; CPX-5142; Ubiquitous AP-1 Adaptor complex, sigma1b variant.
DR   ComplexPortal; CPX-5143; Ubiquitous AP-1 Adaptor complex, sigma1c variant.
DR   CORUM; P35585; -.
DR   DIP; DIP-35323N; -.
DR   FunCoup; P35585; 3712.
DR   IntAct; P35585; 9.
DR   STRING; 10090.ENSMUSP00000003117; -.
DR   GlyGen; P35585; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P35585; -.
DR   PhosphoSitePlus; P35585; -.
DR   SwissPalm; P35585; -.
DR   jPOST; P35585; -.
DR   PaxDb; 10090-ENSMUSP00000003117; -.
DR   PeptideAtlas; P35585; -.
DR   ProteomicsDB; 296263; -.
DR   Pumba; P35585; -.
DR   Antibodypedia; 27330; 173 antibodies from 27 providers.
DR   DNASU; 11767; -.
DR   Ensembl; ENSMUST00000003117.15; ENSMUSP00000003117.9; ENSMUSG00000003033.16.
DR   GeneID; 11767; -.
DR   KEGG; mmu:11767; -.
DR   UCSC; uc009mfp.1; mouse.
DR   AGR; MGI:102776; -.
DR   CTD; 8907; -.
DR   MGI; MGI:102776; Ap1m1.
DR   VEuPathDB; HostDB:ENSMUSG00000003033; -.
DR   eggNOG; KOG0937; Eukaryota.
DR   GeneTree; ENSGT00940000157924; -.
DR   HOGENOM; CLU_026996_0_2_1; -.
DR   InParanoid; P35585; -.
DR   OMA; KPLIWCD; -.
DR   OrthoDB; 10259133at2759; -.
DR   PhylomeDB; P35585; -.
DR   Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR   Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR   Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 11767; 18 hits in 81 CRISPR screens.
DR   EvolutionaryTrace; P35585; -.
DR   PRO; PR:P35585; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; P35585; protein.
DR   Bgee; ENSMUSG00000003033; Expressed in seminiferous tubule of testis and 267 other cell types or tissues.
DR   ExpressionAtlas; P35585; baseline and differential.
DR   GO; GO:0030121; C:AP-1 adaptor complex; NAS:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0005769; C:early endosome; NAS:ComplexPortal.
DR   GO; GO:0005765; C:lysosomal membrane; NAS:ComplexPortal.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0005802; C:trans-Golgi network; TAS:MGI.
DR   GO; GO:0032588; C:trans-Golgi network membrane; NAS:ComplexPortal.
DR   GO; GO:0035615; F:clathrin-cargo adaptor activity; IBA:GO_Central.
DR   GO; GO:0035646; P:endosome to melanosome transport; ISO:GO_Central.
DR   GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR   GO; GO:1903232; P:melanosome assembly; NAS:ComplexPortal.
DR   GO; GO:0032438; P:melanosome organization; ISO:GO_Central.
DR   GO; GO:0060155; P:platelet dense granule organization; NAS:ComplexPortal.
DR   GO; GO:0016192; P:vesicle-mediated transport; TAS:MGI.
DR   CDD; cd09258; AP-1_Mu1A_Cterm; 1.
DR   CDD; cd14835; AP1_Mu_N; 1.
DR   DisProt; DP02898; -.
DR   FunFam; 2.60.40.1170:FF:000002; AP-1 complex subunit mu-1 isoform 1; 1.
DR   FunFam; 3.30.450.60:FF:000006; AP-1 complex subunit mu-1 isoform 1; 1.
DR   Gene3D; 3.30.450.60; -; 1.
DR   Gene3D; 2.60.40.1170; Mu homology domain, subdomain B; 2.
DR   InterPro; IPR050431; Adaptor_comp_med_subunit.
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   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   PDBsum; 1W63; -.
DR   PDBsum; 4EMZ; -.
DR   PDBsum; 4EN2; -.
DR   PDBsum; 4HMY; -.
DR   PDBsum; 4P6Z; -.
DR   PDBsum; 6CM9; -.
DR   PDBsum; 6CRI; -.
DR   PDBsum; 6D83; -.
DR   PDBsum; 6D84; -.
DR   PDBsum; 6DFF; -.
DR   PDBsum; 7R4H; -.
DR   PDBsum; 7UX3; -.
DR   PDBsum; 8D4C; -.
DR   PDBsum; 8D4D; -.
DR   PDBsum; 8D4E; -.
DR   PDBsum; 8D4F; -.
DR   PDBsum; 8D4G; -.
DR   PDBsum; 8D9R; -.
DR   PDBsum; 8D9S; -.
DR   PDBsum; 8D9T; -.
DR   PDBsum; 8D9U; -.
DR   PDBsum; 8D9V; -.
DR   PDBsum; 8D9W; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BXS5"
FT   CHAIN           2..423
FT                   /note="AP-1 complex subunit mu-1"
FT                   /id="PRO_0000193771"
FT   DOMAIN          168..421
FT                   /note="MHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BXS5"
FT   MOD_RES         152
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         154
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         223
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q32Q06"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          15..22
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   HELIX           29..32
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   HELIX           33..42
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          48..52
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          55..61
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          66..73
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   HELIX           77..94
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   HELIX           101..105
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   HELIX           107..117
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   HELIX           128..131
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   TURN            132..134
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   HELIX           148..150
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   HELIX           151..153
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:4P6Z"
FT   STRAND          170..183
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          185..187
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          189..203
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          205..207
FT                   /evidence="ECO:0007829|PDB:4P6Z"
FT   STRAND          209..214
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   HELIX           217..223
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          234..238
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   HELIX           244..250
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          253..255
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   HELIX           256..258
FT                   /evidence="ECO:0007829|PDB:4EMZ"
FT   STRAND          259..270
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   HELIX           273..275
FT                   /evidence="ECO:0007829|PDB:4EN2"
FT   STRAND          276..286
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   TURN            287..289
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          290..299
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          306..315
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          321..335
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   TURN            336..339
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          340..349
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          353..361
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          381..384
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          392..398
FT                   /evidence="ECO:0007829|PDB:7R4H"
FT   STRAND          406..420
FT                   /evidence="ECO:0007829|PDB:7R4H"
SQ   SEQUENCE   423 AA;  48543 MW;  1213566B3A681B4C CRC64;
     MSASAVYVLD LKGKVLICRN YRGDVDMSEV EHFMPILMEK EEEGMLSPIL AHGGVRFMWI
     KHNNLYLVAT SKKNACVSLV FSFLYKVVQV FSEYFKELEE ESIRDNFVII YELLDELMDF
     GYPQTTDSKI LQEYITQEGH KLETGAPRPP ATVTNAVSWR SEGIKYRKNE VFLDVIEAVN
     LLVSANGNVL RSEIVGSIKM RVFLSGMPEL RLGLNDKVLF DNTGRGKSKS VELEDVKFHQ
     CVRLSRFEND RTISFIPPDG EFELMSYRLN THVKPLIWIE SVIEKHSHSR IEYMVKAKSQ
     FKRRSTANNV EIHIPVPNDA DSPKFKTTVG SVKWVPENSE IVWSVKSFPG GKEYLMRAHF
     GLPSVEAEDK EGKPPISVKF EIPYFTTSGI QVRYLKIIEK SGYQALPWVR YITQNGDYQL
     RTQ
//