AP1M1_MOUSE
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 03-AUG-2022, entry version 167.
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, Pancreas,
RC 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).
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. The AP complexes mediate the recruitment of clathrin to
CC membranes and the recognition of sorting signals within the cytosolic
CC tails of transmembrane cargo molecules.
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). Interacts with
CC MARCHF11 (By similarity). {ECO:0000250}.
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 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 AlphaFoldDB; P35585; -.
DR SMR; P35585; -.
DR BioGRID; 198125; 13.
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 IntAct; P35585; 8.
DR STRING; 10090.ENSMUSP00000003117; -.
DR iPTMnet; P35585; -.
DR PhosphoSitePlus; P35585; -.
DR SwissPalm; P35585; -.
DR EPD; P35585; -.
DR jPOST; P35585; -.
DR PaxDb; P35585; -.
DR PeptideAtlas; P35585; -.
DR PRIDE; P35585; -.
DR ProteomicsDB; 296263; -.
DR Antibodypedia; 27330; 176 antibodies from 27 providers.
DR DNASU; 11767; -.
DR Ensembl; ENSMUST00000003117; ENSMUSP00000003117; ENSMUSG00000003033.
DR GeneID; 11767; -.
DR KEGG; mmu:11767; -.
DR UCSC; uc009mfp.1; mouse.
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; CRAKAQI; -.
DR OrthoDB; 725236at2759; -.
DR PhylomeDB; P35585; -.
DR TreeFam; TF300393; -.
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; 17 hits in 76 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 263 other tissues.
DR ExpressionAtlas; P35585; baseline and differential.
DR Genevisible; P35585; MM.
DR GO; GO:0030121; C:AP-1 adaptor complex; IC:ComplexPortal.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; IC:ComplexPortal.
DR GO; GO:0005765; C:lysosomal membrane; IC:ComplexPortal.
DR GO; GO:0005802; C:trans-Golgi network; TAS:MGI.
DR GO; GO:0032588; C:trans-Golgi network membrane; IC:ComplexPortal.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0035646; P:endosome to melanosome transport; ISO:MGI.
DR GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR GO; GO:1903232; P:melanosome assembly; IC:ComplexPortal.
DR GO; GO:0032438; P:melanosome organization; ISO:MGI.
DR GO; GO:0060155; P:platelet dense granule organization; IC:ComplexPortal.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR DisProt; DP02898; -.
DR InterPro; IPR036168; AP2_Mu_C_sf.
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 PIRSF; PIRSF005992; Clathrin_mu; 1.
DR PRINTS; PR00314; CLATHRINADPT.
DR SUPFAM; SSF49447; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00990; CLAT_ADAPTOR_M_1; 1.
DR PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR PROSITE; PS51072; MHD; 1.
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:4P6Z"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 27..32
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 77..94
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:4P6Z"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 167..183
FT /evidence="ECO:0007829|PDB:4EN2"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 189..203
FT /evidence="ECO:0007829|PDB:4EN2"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:4EN2"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:4EN2"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:4EN2"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:4EN2"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 259..269
FT /evidence="ECO:0007829|PDB:4EN2"
FT STRAND 276..287
FT /evidence="ECO:0007829|PDB:4EN2"
FT STRAND 290..299
FT /evidence="ECO:0007829|PDB:4EN2"
FT STRAND 306..315
FT /evidence="ECO:0007829|PDB:4EN2"
FT STRAND 321..335
FT /evidence="ECO:0007829|PDB:4EN2"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:4EN2"
FT STRAND 340..351
FT /evidence="ECO:0007829|PDB:4EN2"
FT STRAND 353..361
FT /evidence="ECO:0007829|PDB:4EN2"
FT STRAND 376..388
FT /evidence="ECO:0007829|PDB:4EN2"
FT STRAND 392..398
FT /evidence="ECO:0007829|PDB:4EN2"
FT STRAND 405..414
FT /evidence="ECO:0007829|PDB:4EN2"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:4EN2"
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
