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AP-1 complex subunit gamma-1 (Adaptor protein complex AP-1 subunit gamma-1) (Adaptor-related protein complex 1 subunit gamma-1) (Clathrin assembly protein complex 1 gamma-1 large chain) (Gamma-adaptin) (Gamma1-adaptin) (Golgi adaptor HA1/AP1 adaptin subunit gamma-1)

 AP1G1_MOUSE             Reviewed;         822 AA.
P22892;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
18-JUL-2018, entry version 164.
RecName: Full=AP-1 complex subunit gamma-1;
AltName: Full=Adaptor protein complex AP-1 subunit gamma-1;
AltName: Full=Adaptor-related protein complex 1 subunit gamma-1;
AltName: Full=Clathrin assembly protein complex 1 gamma-1 large chain;
AltName: Full=Gamma-adaptin;
AltName: Full=Gamma1-adaptin;
AltName: Full=Golgi adaptor HA1/AP1 adaptin subunit gamma-1;
Name=Ap1g1; Synonyms=Adtg, Clapg1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-25.
TISSUE=Brain;
PubMed=2126014; DOI=10.1083/jcb.111.6.2319;
Robinson M.S.;
"Cloning and expression of gamma-adaptin, a component of clathrin-
coated vesicles associated with the Golgi apparatus.";
J. Cell Biol. 111:2319-2326(1990).
[2]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[3]
X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 704-822, MUTAGENESIS OF
ALA-753; LEU-762 AND PRO-765, AND INTERACTION WITH EPS15 AND SYNRG.
PubMed=12176391; DOI=10.1016/S0969-2126(02)00801-8;
Kent H.M., McMahon H.T., Evans P.R., Benmerah A., Owen D.J.;
"Gamma-adaptin appendage domain: structure and binding site for Eps15
and gamma-synergin.";
Structure 10:1139-1148(2002).
[4]
X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 1-613, AND SUBUNIT.
PubMed=15377783; DOI=10.1073/pnas.0406102101;
Heldwein E.E., Macia E., Wang J., Yin H.L., Kirchhausen T.,
Harrison S.C.;
"Crystal structure of the clathrin adaptor protein 1 core.";
Proc. Natl. Acad. Sci. U.S.A. 101:14108-14113(2004).
-!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1
that plays a role in protein sorting in the late-Golgi/trans-Golgi
network (TGN) and/or endosomes. The AP complexes mediate both the
recruitment of clathrin to membranes and the recognition of
sorting signals within the cytosolic tails of transmembrane cargo
molecules.
-!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer
composed of two large adaptins (gamma-type subunit AP1G1 and beta-
type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or
AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or
AP1S3) (By similarity). Binds RABEP1 (By similarity). Binds EPS15
and SYNRG. Interacts (via GAE domain) with AP1AR (via coiled-coil
domain) (By similarity). {ECO:0000250}.
-!- INTERACTION:
P35585:Ap1m1; NbExp=6; IntAct=EBI-1040262, EBI-1040251;
Q14677:CLINT1 (xeno); NbExp=10; IntAct=EBI-1040262, EBI-1171113;
-!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle,
clathrin-coated vesicle membrane; Peripheral membrane protein;
Cytoplasmic side. Note=Component of the coat surrounding the
cytoplasmic face of coated vesicles located at the Golgi complex.
-!- TISSUE SPECIFICITY: Widely expressed.
-!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X54424; CAA38296.1; -; mRNA.
CCDS; CCDS80929.1; -.
PIR; A36680; A36680.
RefSeq; NP_001288140.1; NM_001301211.1.
UniGene; Mm.37210; -.
UniGene; Mm.486894; -.
PDB; 1GYU; X-ray; 1.81 A; A=704-822.
PDB; 1GYV; X-ray; 1.71 A; A=704-822.
PDB; 1GYW; X-ray; 2.40 A; A/B=695-822.
PDB; 1W63; X-ray; 4.00 A; A/C/E/G/I/K=1-613.
PDB; 2A7B; X-ray; 1.65 A; A=704-822.
PDB; 3ZY7; X-ray; 1.09 A; A/B=704-822.
PDB; 4HMY; X-ray; 7.00 A; A=1-595.
PDB; 4P6Z; X-ray; 3.00 A; G=1-613.
PDBsum; 1GYU; -.
PDBsum; 1GYV; -.
PDBsum; 1GYW; -.
PDBsum; 1W63; -.
PDBsum; 2A7B; -.
PDBsum; 3ZY7; -.
PDBsum; 4HMY; -.
PDBsum; 4P6Z; -.
ProteinModelPortal; P22892; -.
SMR; P22892; -.
BioGrid; 198123; 3.
CORUM; P22892; -.
IntAct; P22892; 19.
MINT; P22892; -.
STRING; 10090.ENSMUSP00000090844; -.
iPTMnet; P22892; -.
PhosphoSitePlus; P22892; -.
SwissPalm; P22892; -.
EPD; P22892; -.
MaxQB; P22892; -.
PaxDb; P22892; -.
PeptideAtlas; P22892; -.
PRIDE; P22892; -.
Ensembl; ENSMUST00000034171; ENSMUSP00000034171; ENSMUSG00000031731.
GeneID; 11765; -.
KEGG; mmu:11765; -.
UCSC; uc012gkl.3; mouse.
CTD; 164; -.
MGI; MGI:101919; Ap1g1.
eggNOG; KOG1062; Eukaryota.
eggNOG; ENOG410XPKK; LUCA.
GeneTree; ENSGT00390000012618; -.
HOGENOM; HOG000210271; -.
HOVERGEN; HBG067473; -.
InParanoid; P22892; -.
KO; K12391; -.
PhylomeDB; P22892; -.
Reactome; R-MMU-2132295; MHC class II antigen presentation.
Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
EvolutionaryTrace; P22892; -.
PRO; PR:P22892; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031731; -.
CleanEx; MM_AP1G1; -.
ExpressionAtlas; P22892; baseline and differential.
Genevisible; P22892; MM.
GO; GO:0030121; C:AP-1 adaptor complex; IEA:InterPro.
GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
GO; GO:0055037; C:recycling endosome; ISO:MGI.
GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
GO; GO:0005518; F:collagen binding; ISO:MGI.
GO; GO:0030742; F:GTP-dependent protein binding; ISO:MGI.
GO; GO:0019894; F:kinesin binding; ISO:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0017137; F:Rab GTPase binding; ISO:MGI.
GO; GO:0035646; P:endosome to melanosome transport; ISO:MGI.
GO; GO:0090160; P:Golgi to lysosome transport; ISO:MGI.
GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:MGI.
GO; GO:0043323; P:positive regulation of natural killer cell degranulation; ISO:MGI.
GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISO:MGI.
GO; GO:0016192; P:vesicle-mediated transport; TAS:MGI.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR017107; AP1_complex_gsu.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
InterPro; IPR013041; Clathrin_app_Ig-like_sf.
InterPro; IPR008153; GAE_dom.
Pfam; PF01602; Adaptin_N; 1.
Pfam; PF02883; Alpha_adaptinC2; 1.
PIRSF; PIRSF037094; AP1_complex_gamma; 1.
SMART; SM00809; Alpha_adaptinC2; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF49348; SSF49348; 1.
PROSITE; PS50180; GAE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasmic vesicle;
Direct protein sequencing; Golgi apparatus; Membrane;
Protein transport; Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2126014}.
CHAIN 2 822 AP-1 complex subunit gamma-1.
/FTId=PRO_0000193759.
DOMAIN 702 817 GAE. {ECO:0000255|PROSITE-
ProRule:PRU00093}.
MUTAGEN 753 753 A->D: Strongly reduces interaction with
EPS15 and SYNRG.
{ECO:0000269|PubMed:12176391}.
MUTAGEN 762 762 L->E: Strongly reduces interaction with
EPS15 and SYNRG.
{ECO:0000269|PubMed:12176391}.
MUTAGEN 765 765 P->N: Reduces interaction with EPS15 and
SYNRG. {ECO:0000269|PubMed:12176391}.
HELIX 7 15 {ECO:0000244|PDB:4P6Z}.
HELIX 20 39 {ECO:0000244|PDB:4P6Z}.
STRAND 43 45 {ECO:0000244|PDB:4P6Z}.
HELIX 46 58 {ECO:0000244|PDB:4P6Z}.
HELIX 64 66 {ECO:0000244|PDB:4P6Z}.
HELIX 67 74 {ECO:0000244|PDB:4P6Z}.
STRAND 76 78 {ECO:0000244|PDB:4P6Z}.
HELIX 79 92 {ECO:0000244|PDB:4P6Z}.
HELIX 100 111 {ECO:0000244|PDB:4P6Z}.
HELIX 116 129 {ECO:0000244|PDB:4P6Z}.
HELIX 132 146 {ECO:0000244|PDB:4P6Z}.
HELIX 151 167 {ECO:0000244|PDB:4P6Z}.
HELIX 170 175 {ECO:0000244|PDB:4P6Z}.
HELIX 176 179 {ECO:0000244|PDB:4P6Z}.
HELIX 188 204 {ECO:0000244|PDB:4P6Z}.
HELIX 206 212 {ECO:0000244|PDB:4P6Z}.
HELIX 216 228 {ECO:0000244|PDB:4P6Z}.
TURN 233 235 {ECO:0000244|PDB:4P6Z}.
HELIX 243 255 {ECO:0000244|PDB:4P6Z}.
TURN 256 259 {ECO:0000244|PDB:4P6Z}.
HELIX 262 277 {ECO:0000244|PDB:4P6Z}.
HELIX 283 298 {ECO:0000244|PDB:4P6Z}.
HELIX 303 317 {ECO:0000244|PDB:4P6Z}.
HELIX 322 334 {ECO:0000244|PDB:4P6Z}.
STRAND 336 339 {ECO:0000244|PDB:4P6Z}.
HELIX 340 343 {ECO:0000244|PDB:4P6Z}.
HELIX 347 352 {ECO:0000244|PDB:4P6Z}.
HELIX 353 355 {ECO:0000244|PDB:4P6Z}.
HELIX 359 370 {ECO:0000244|PDB:4P6Z}.
TURN 375 377 {ECO:0000244|PDB:4P6Z}.
HELIX 378 390 {ECO:0000244|PDB:4P6Z}.
HELIX 394 410 {ECO:0000244|PDB:4P6Z}.
HELIX 415 428 {ECO:0000244|PDB:4P6Z}.
HELIX 430 432 {ECO:0000244|PDB:4P6Z}.
HELIX 435 437 {ECO:0000244|PDB:4P6Z}.
HELIX 438 446 {ECO:0000244|PDB:4P6Z}.
TURN 449 452 {ECO:0000244|PDB:4P6Z}.
HELIX 453 465 {ECO:0000244|PDB:4P6Z}.
HELIX 470 482 {ECO:0000244|PDB:4P6Z}.
HELIX 484 488 {ECO:0000244|PDB:4P6Z}.
HELIX 503 514 {ECO:0000244|PDB:4P6Z}.
HELIX 520 536 {ECO:0000244|PDB:4P6Z}.
HELIX 541 550 {ECO:0000244|PDB:4P6Z}.
HELIX 551 553 {ECO:0000244|PDB:4P6Z}.
HELIX 557 572 {ECO:0000244|PDB:4P6Z}.
HELIX 576 580 {ECO:0000244|PDB:4P6Z}.
STRAND 707 712 {ECO:0000244|PDB:3ZY7}.
STRAND 715 722 {ECO:0000244|PDB:3ZY7}.
STRAND 730 739 {ECO:0000244|PDB:3ZY7}.
STRAND 741 743 {ECO:0000244|PDB:3ZY7}.
STRAND 745 753 {ECO:0000244|PDB:3ZY7}.
STRAND 758 762 {ECO:0000244|PDB:3ZY7}.
HELIX 772 774 {ECO:0000244|PDB:3ZY7}.
STRAND 778 785 {ECO:0000244|PDB:3ZY7}.
STRAND 794 802 {ECO:0000244|PDB:3ZY7}.
STRAND 805 813 {ECO:0000244|PDB:3ZY7}.
HELIX 818 820 {ECO:0000244|PDB:3ZY7}.
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


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