AP1G1_MOUSE
ID AP1G1_MOUSE Reviewed; 822 AA.
AC P22892;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=AP-1 complex subunit gamma-1;
DE AltName: Full=Adaptor protein complex AP-1 subunit gamma-1;
DE AltName: Full=Adaptor-related protein complex 1 subunit gamma-1;
DE AltName: Full=Clathrin assembly protein complex 1 gamma-1 large chain;
DE AltName: Full=Gamma-adaptin;
DE AltName: Full=Gamma1-adaptin;
DE AltName: Full=Golgi adaptor HA1/AP1 adaptin subunit gamma-1;
GN Name=Ap1g1; Synonyms=Adtg, Clapg1;
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], AND PROTEIN SEQUENCE OF 2-25.
RC TISSUE=Brain;
RX PubMed=2126014; DOI=10.1083/jcb.111.6.2319;
RA Robinson M.S.;
RT "Cloning and expression of gamma-adaptin, a component of clathrin-coated
RT vesicles associated with the Golgi apparatus.";
RL J. Cell Biol. 111:2319-2326(1990).
RN [2]
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 704-822, MUTAGENESIS OF ALA-753;
RP LEU-762 AND PRO-765, AND INTERACTION WITH EPS15 AND SYNRG.
RX PubMed=12176391; DOI=10.1016/s0969-2126(02)00801-8;
RA Kent H.M., McMahon H.T., Evans P.R., Benmerah A., Owen D.J.;
RT "Gamma-adaptin appendage domain: structure and binding site for Eps15 and
RT gamma-synergin.";
RL Structure 10:1139-1148(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 1-613, AND SUBUNIT.
RX PubMed=15377783; DOI=10.1073/pnas.0406102101;
RA Heldwein E.E., Macia E., Wang J., Yin H.L., Kirchhausen T., Harrison S.C.;
RT "Crystal structure of the clathrin adaptor protein 1 core.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14108-14113(2004).
CC -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that
CC plays a role in protein sorting in the late-Golgi/trans-Golgi network
CC (TGN) and/or endosomes. The AP complexes mediate both the recruitment
CC of clathrin to membranes and the recognition of sorting signals within
CC the cytosolic tails of transmembrane cargo molecules. In association
CC with AFTPH/aftiphilin in the aftiphilin/p200/gamma-synergin complex,
CC involved in the trafficking of transferrin from early to recycling
CC endosomes, and the membrane trafficking of furin and the lysosomal
CC enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes
CC (By similarity). {ECO:0000250|UniProtKB:O43747}.
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) (By similarity).
CC Interacts (via GAE domain) with RABEP1 (By similarity). Interacts with
CC EPS15 (PubMed:12176391). Interacts with SYNRG/gamma-synergin
CC (PubMed:12176391). Interacts (via GAE domain) with AP1AR (via coiled-
CC coil domain) (By similarity). Interacts with CLN3 (via dileucine
CC motif); this interaction facilitates lysosomal targeting (By
CC similarity). Interacts (via GAE domain) with AFTPH/aftiphilin; the
CC interaction is required to recruit AFTPH/aftiphilin to the perinuclear
CC region of the cell (By similarity). {ECO:0000250|UniProtKB:O43747,
CC ECO:0000269|PubMed:12176391}.
CC -!- INTERACTION:
CC P22892; P35585: Ap1m1; NbExp=6; IntAct=EBI-1040262, EBI-1040251;
CC P22892; Q14677: CLINT1; Xeno; NbExp=10; IntAct=EBI-1040262, EBI-1171113;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:O43747}.
CC Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC {ECO:0000250|UniProtKB:O43747}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O43747}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O43747}. Cytoplasm
CC {ECO:0000250|UniProtKB:O43747}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:O43747}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250|UniProtKB:O43747}. Membrane, clathrin-coated pit
CC {ECO:0000250|UniProtKB:O43747}. Note=Component of the coat surrounding
CC the cytoplasmic face of coated vesicles located at the Golgi complex
CC (By similarity). Co-localizes with AFTPH/aftiphilin in the cytoplasm
CC (By similarity). {ECO:0000250|UniProtKB:O43747}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; X54424; CAA38296.1; -; mRNA.
DR CCDS; CCDS80929.1; -.
DR PIR; A36680; A36680.
DR RefSeq; NP_001288140.1; NM_001301211.1.
DR PDB; 1GYU; X-ray; 1.81 A; A=704-822.
DR PDB; 1GYV; X-ray; 1.71 A; A=704-822.
DR PDB; 1GYW; X-ray; 2.40 A; A/B=695-822.
DR PDB; 1W63; X-ray; 4.00 A; A/C/E/G/I/K=1-613.
DR PDB; 2A7B; X-ray; 1.65 A; A=704-822.
DR PDB; 3ZY7; X-ray; 1.09 A; A/B=704-822.
DR PDB; 4HMY; X-ray; 7.00 A; A=1-595.
DR PDB; 4P6Z; X-ray; 3.00 A; G=1-613.
DR PDB; 6CM9; EM; 3.73 A; G=1-595.
DR PDB; 6CRI; EM; 6.80 A; G/Q/R=4-588.
DR PDB; 6D83; EM; 4.27 A; G=1-595.
DR PDB; 6D84; EM; 6.72 A; G/K=1-595.
DR PDB; 6DFF; EM; 3.90 A; G=1-595.
DR PDBsum; 1GYU; -.
DR PDBsum; 1GYV; -.
DR PDBsum; 1GYW; -.
DR PDBsum; 1W63; -.
DR PDBsum; 2A7B; -.
DR PDBsum; 3ZY7; -.
DR PDBsum; 4HMY; -.
DR PDBsum; 4P6Z; -.
DR PDBsum; 6CM9; -.
DR PDBsum; 6CRI; -.
DR PDBsum; 6D83; -.
DR PDBsum; 6D84; -.
DR PDBsum; 6DFF; -.
DR AlphaFoldDB; P22892; -.
DR BMRB; P22892; -.
DR SMR; P22892; -.
DR BioGRID; 198123; 25.
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 ComplexPortal; CPX-5144; Endothelial AP-1 Adaptor complex, sigma1a variant.
DR CORUM; P22892; -.
DR IntAct; P22892; 18.
DR MINT; P22892; -.
DR STRING; 10090.ENSMUSP00000090844; -.
DR iPTMnet; P22892; -.
DR PhosphoSitePlus; P22892; -.
DR SwissPalm; P22892; -.
DR EPD; P22892; -.
DR jPOST; P22892; -.
DR MaxQB; P22892; -.
DR PaxDb; P22892; -.
DR PeptideAtlas; P22892; -.
DR PRIDE; P22892; -.
DR ProteomicsDB; 296262; -.
DR Antibodypedia; 3960; 258 antibodies from 34 providers.
DR DNASU; 11765; -.
DR Ensembl; ENSMUST00000034171; ENSMUSP00000034171; ENSMUSG00000031731.
DR GeneID; 11765; -.
DR KEGG; mmu:11765; -.
DR UCSC; uc012gkl.3; mouse.
DR CTD; 164; -.
DR MGI; MGI:101919; Ap1g1.
DR VEuPathDB; HostDB:ENSMUSG00000031731; -.
DR eggNOG; KOG1062; Eukaryota.
DR GeneTree; ENSGT00950000182838; -.
DR HOGENOM; CLU_003824_0_0_1; -.
DR InParanoid; P22892; -.
DR PhylomeDB; P22892; -.
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 BioGRID-ORCS; 11765; 7 hits in 58 CRISPR screens.
DR ChiTaRS; Ap1g1; mouse.
DR EvolutionaryTrace; P22892; -.
DR PRO; PR:P22892; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P22892; protein.
DR Bgee; ENSMUSG00000031731; Expressed in undifferentiated genital tubercle and 250 other tissues.
DR ExpressionAtlas; P22892; baseline and differential.
DR Genevisible; P22892; MM.
DR GO; GO:0030121; C:AP-1 adaptor complex; IBA:GO_Central.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IC:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; IC:ComplexPortal.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR GO; GO:0032588; C:trans-Golgi network membrane; IC:ComplexPortal.
DR GO; GO:0140312; F:cargo adaptor activity; IBA:GO_Central.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0030742; F:GTP-dependent protein binding; ISO:MGI.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0110010; P:basolateral protein secretion; IC:ComplexPortal.
DR GO; GO:0035646; P:endosome to melanosome transport; ISO:MGI.
DR GO; GO:0090160; P:Golgi to lysosome transport; ISO:MGI.
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; IC:ComplexPortal.
DR GO; GO:0060155; P:platelet dense granule organization; IC:ComplexPortal.
DR GO; GO:0043323; P:positive regulation of natural killer cell degranulation; ISO:MGI.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISO:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR017107; AP1_complex_gsu.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR008153; GAE_dom.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR PIRSF; PIRSF037094; AP1_complex_gamma; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR PROSITE; PS50180; GAE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coated pit; Cytoplasm; Cytoplasmic vesicle;
KW Direct protein sequencing; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2126014"
FT CHAIN 2..822
FT /note="AP-1 complex subunit gamma-1"
FT /id="PRO_0000193759"
FT DOMAIN 702..817
FT /note="GAE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00093"
FT REGION 593..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 753
FT /note="A->D: Strongly reduces interaction with EPS15 and
FT SYNRG."
FT /evidence="ECO:0000269|PubMed:12176391"
FT MUTAGEN 762
FT /note="L->E: Strongly reduces interaction with EPS15 and
FT SYNRG."
FT /evidence="ECO:0000269|PubMed:12176391"
FT MUTAGEN 765
FT /note="P->N: Reduces interaction with EPS15 and SYNRG."
FT /evidence="ECO:0000269|PubMed:12176391"
FT HELIX 7..15
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 20..39
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 79..92
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 132..146
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 151..167
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 188..204
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 206..212
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 216..228
FT /evidence="ECO:0007829|PDB:4P6Z"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:4P6Z"
FT TURN 256..259
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 262..277
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 283..298
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 303..317
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 322..334
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 347..352
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 359..370
FT /evidence="ECO:0007829|PDB:4P6Z"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 378..390
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 394..410
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 415..428
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 438..446
FT /evidence="ECO:0007829|PDB:4P6Z"
FT TURN 449..452
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 453..465
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 470..482
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 484..488
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 503..514
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 520..536
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 541..550
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 551..553
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 557..572
FT /evidence="ECO:0007829|PDB:4P6Z"
FT HELIX 576..580
FT /evidence="ECO:0007829|PDB:4P6Z"
FT STRAND 707..712
FT /evidence="ECO:0007829|PDB:3ZY7"
FT STRAND 715..722
FT /evidence="ECO:0007829|PDB:3ZY7"
FT STRAND 730..739
FT /evidence="ECO:0007829|PDB:3ZY7"
FT STRAND 741..743
FT /evidence="ECO:0007829|PDB:3ZY7"
FT STRAND 745..753
FT /evidence="ECO:0007829|PDB:3ZY7"
FT STRAND 758..762
FT /evidence="ECO:0007829|PDB:3ZY7"
FT HELIX 772..774
FT /evidence="ECO:0007829|PDB:3ZY7"
FT STRAND 778..785
FT /evidence="ECO:0007829|PDB:3ZY7"
FT STRAND 794..802
FT /evidence="ECO:0007829|PDB:3ZY7"
FT STRAND 805..813
FT /evidence="ECO:0007829|PDB:3ZY7"
FT HELIX 818..820
FT /evidence="ECO:0007829|PDB:3ZY7"
SQ SEQUENCE 822 AA; 91350 MW; 15317E4BCD9503EB CRC64;
MPAPIRLREL IRTIRTARTQ AEEREMIQKE CAAIRSSFRE EDNTYRCRNV AKLLYMHMLG
YPAHFGQLEC LKLIASQKFT DKRIGYLGAM LLLDERQDVH LLMTNCIKND LNHSTQFVQG
LALCTLGCMG SSEMCRDLAG EVEKLLKTSN SYLRKKAALC AVHVIRKVPE LMEMFLPATK
NLLNEKNHGV LHTSVVLLTE MCERSPDMLA HFRKLVPQLV RILKNLIMSG YSPEHDVSGI
SDPFLQVRIL RLLRILGRND DDSSEAMNDI LAQVATNTET SKNVGNAILY ETVLTIMDIK
SESGLRVLAI NILGRFLLNN DKNIRYVALT SLLKTVQTDH NAVQRHRSTI VDCLKDLDVS
IKRRAMELSF ALVNGNNIRG MMKELLYFLD SCEPEFKADC ASGIFLAAEK YAPSKRWHID
TIMRVLTTAG SYVRDDAVPN LIQLITNSVE MHAYTVQRLY KAILGDYSQQ PLVQVAAWCI
GEYGDLLVSG QCEEEEPIQV TEDEVLDILE SVLISNMSTS VTRGYALTAI MKLSTRFTCT
VNRIKKVVSI YGSSIDVELQ QRAVEYNALF KKYDHMRSAL LERMPVMEKV TTNGPSEIVQ
TNGETEPAPL ETKPPPSGPQ PTSQANDLLD LLGGNDITPV IPTAPTSKPA SAGGELLDLL
GDITLTGAPA AAPTPASVPQ ISQPPFLLDG LSSQPLFNDI APGIPSITAY SKNGLKIEFT
FERSNTNPSV TVITIQASNS TELDMTDFVF QAAVPKTFQL QLLSPSSSVV PAFNTGTITQ
VIKVLNPQKQ QLRMRIKLTY NHKGSAMQDL AEVNNFPPQS WQ
