ID AP1G1_HUMAN Reviewed; 822 AA. AC O43747; O75709; O75842; Q9UG09; Q9Y3U4; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 5. DT 27-MAR-2024, entry version 217. 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=Gamma1-adaptin; DE AltName: Full=Golgi adaptor HA1/AP1 adaptin subunit gamma-1; GN Name=AP1G1; Synonyms=ADTG, CLAPG1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2). RX PubMed=9653655; DOI=10.1006/geno.1998.5289; RA Peyrard M., Parveneh S., Lagerkrantz S., Ekman M., Fransson I., Sahlen S., RA Dumanski J.P.; RT "Cloning, expression pattern, and chromosomal assignment to 16q23 of the RT human gamma-adaptin gene (ADTG)."; RL Genomics 50:275-280(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT HIS-685. RX PubMed=9733768; DOI=10.1074/jbc.273.38.24693; RA Takatsu H., Sakurai M., Shin H.-W., Murakami K., Nakayama K.; RT "Identification and characterization of novel clathrin adaptor-related RT proteins."; RL J. Biol. Chem. 273:24693-24700(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 539-822. RC TISSUE=Fetal brain, and Uterus; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP INTERACTION WITH RABEP1, AND SUBCELLULAR LOCATION. RX PubMed=12773381; DOI=10.1093/emboj/cdg257; RA Deneka M., Neeft M., Popa I., van Oort M., Sprong H., Oorschot V., RA Klumperman J., Schu P., van der Sluijs P.; RT "Rabaptin-5alpha/rabaptin-4 serves as a linker between rab4 and gamma(1)- RT adaptin in membrane recycling from endosomes."; RL EMBO J. 22:2645-2657(2003). RN [6] RP INTERACTION WITH RABEP1 AND AFTPH. RX PubMed=14665628; DOI=10.1074/jbc.m311873200; RA Mattera R., Ritter B., Sidhu S.S., McPherson P.S., Bonifacino J.S.; RT "Definition of the consensus motif recognized by gamma-adaptin ear RT domains."; RL J. Biol. Chem. 279:8018-8028(2004). RN [7] RP INTERACTION WITH AP1AR. RX PubMed=15775984; DOI=10.1038/sj.emboj.7600600; RA Neubrand V.E., Will R.D., Moebius W., Poustka A., Wiemann S., Schu P., RA Dotti C.G., Pepperkok R., Simpson J.C.; RT "Gamma-BAR, a novel AP-1-interacting protein involved in post-Golgi RT trafficking."; RL EMBO J. 24:1122-1133(2005). RN [8] RP INTERACTION WITH CLN3. RX PubMed=15598649; DOI=10.1074/jbc.m411862200; RA Kyttaelae A., Yliannala K., Schu P., Jalanko A., Luzio J.P.; RT "AP-1 and AP-3 facilitate lysosomal targeting of Batten disease protein RT CLN3 via its dileucine motif."; RL J. Biol. Chem. 280:10277-10283(2005). RN [9] RP FUNCTION, INTERACTION WITH AFTPH, AND SUBCELLULAR LOCATION. RX PubMed=15758025; DOI=10.1091/mbc.e04-12-1077; RA Hirst J., Borner G.H., Harbour M., Robinson M.S.; RT "The aftiphilin/p200/gamma-synergin complex."; RL Mol. Biol. Cell 16:2554-2565(2005). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 703-822, AND INTERACTION WITH RP RABEP1 AND SYNRG. RX PubMed=12042876; DOI=10.1038/nsb808; RA Nogi T., Shiba Y., Kawasaki M., Shiba T., Matsugaki N., Igarashi N., RA Suzuki M., Kato R., Takatsu H., Nakayama K., Wakatsuki S.; RT "Structural basis for the accessory protein recruitment by the gamma- RT adaptin ear domain."; RL Nat. Struct. Biol. 9:527-531(2002). RN [14] RP VARIANTS USRISD GLN-15; GLN-35; TRP-35 AND ARG-817, CHARACTERIZATION OF RP VARIANTS USRISD GLN-15; GLN-35; TRP-35 AND ARG-817, VARIANTS USRISR HIS-243 RP AND VAL-366, CHARACTERIZATION OF VARIANTS USRISR HIS-243 AND VAL-366, RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN USRISD, AND INVOLVEMENT IN RP USRISR. RX PubMed=34102099; DOI=10.1016/j.ajhg.2021.05.007; RG UCLA Clinical Genomics Center; RA Usmani M.A., Ahmed Z.M., Magini P., Pienkowski V.M., Rasmussen K.J., RA Hernan R., Rasheed F., Hussain M., Shahzad M., Lanpher B.C., Niu Z., RA Lim F.Y., Pippucci T., Ploski R., Kraus V., Matuszewska K., Palombo F., RA Kianmahd J., Martinez-Agosto J.A., Lee H., Colao E., Motazacker M.M., RA Brigatti K.W., Puffenberger E.G., Riazuddin S.A., Gonzaga-Jauregui C., RA Chung W.K., Wagner M., Schultz M.J., Seri M., Kievit A.J.A., Perrotti N., RA Wassink-Ruiter J.S.K., van Bokhoven H., Riazuddin S., Riazuddin S.; RT "De novo and bi-allelic variants in AP1G1 cause neurodevelopmental disorder RT with developmental delay, intellectual disability, and epilepsy."; RL Am. J. Hum. Genet. 108:1330-1341(2021). 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 (PubMed:15758025). {ECO:0000269|PubMed:15758025, CC ECO:0000269|PubMed:34102099}. 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:34102099). CC Interacts (via GAE domain) with RABEP1 (PubMed:12773381, CC PubMed:14665628, PubMed:12042876). Interacts with SYNRG/gamma-synergin CC (PubMed:12042876). Interacts with EPS15 (By similarity). Interacts (via CC GAE domain) with AP1AR (via coiled-coil domain) (PubMed:15775984). CC Interacts with CLN3 (via dileucine motif); this interaction facilitates CC lysosomal targeting (PubMed:15598649). Interacts (via GAE domain) with CC AFTPH/aftiphilin; the interaction is required to recruit CC AFTPH/aftiphilin to the perinuclear region of the cell CC (PubMed:14665628, PubMed:15758025). {ECO:0000250|UniProtKB:P22892, CC ECO:0000269|PubMed:12042876, ECO:0000269|PubMed:12773381, CC ECO:0000269|PubMed:14665628, ECO:0000269|PubMed:15598649, CC ECO:0000269|PubMed:15758025, ECO:0000269|PubMed:15775984, CC ECO:0000269|PubMed:34102099}. CC -!- INTERACTION: CC O43747; Q15276: RABEP1; NbExp=2; IntAct=EBI-447609, EBI-447043; CC O43747-2; Q6PD74: AAGAB; NbExp=4; IntAct=EBI-10185819, EBI-719906; CC O43747-2; P56377: AP1S2; NbExp=4; IntAct=EBI-10185819, EBI-1054374; CC O43747-2; P54253: ATXN1; NbExp=3; IntAct=EBI-10185819, EBI-930964; CC O43747-2; Q96S82: UBL7; NbExp=6; IntAct=EBI-10185819, EBI-348604; CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:12773381}. CC Cytoplasmic vesicle, clathrin-coated vesicle membrane CC {ECO:0000269|PubMed:12773381}; Peripheral membrane protein CC {ECO:0000269|PubMed:12773381}; Cytoplasmic side CC {ECO:0000269|PubMed:12773381}. Cytoplasm {ECO:0000269|PubMed:15758025}. CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:15758025, CC ECO:0000269|PubMed:34102099}. Cytoplasmic vesicle, clathrin-coated CC vesicle {ECO:0000269|PubMed:15758025}. Membrane, clathrin-coated pit CC {ECO:0000269|PubMed:34102099}. Note=Component of the coat surrounding CC the cytoplasmic face of coated vesicles located at the Golgi complex CC (PubMed:12773381). Co-localizes with AFTPH/aftiphilin in the cytoplasm CC (PubMed:15758025). {ECO:0000269|PubMed:12773381, CC ECO:0000269|PubMed:15758025}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O43747-1; Sequence=Displayed; CC Name=2; CC IsoId=O43747-2; Sequence=VSP_040133; CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- DISEASE: Usmani-Riazuddin syndrome, autosomal dominant (USRISD) CC [MIM:619467]: A neurodevelopmental disorder characterized by global CC developmental delay with impaired intellectual development and speech CC delay, hypotonia, and behavioral abnormalities. More variable CC additional features may include seizures and distal limb anomalies. CC {ECO:0000269|PubMed:34102099}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Usmani-Riazuddin syndrome, autosomal recessive (USRISR) CC [MIM:619548]: A neurodevelopmental disorder characterized by global CC developmental delay with impaired intellectual development and speech CC delay, hypotonia, spasticity, and behavioral abnormalities. More CC variable additional features may include seizures, scoliosis, and joint CC laxity. {ECO:0000269|PubMed:34102099}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y12226; CAA72902.1; -; mRNA. DR EMBL; AJ224112; CAA11832.1; -; Genomic_DNA. DR EMBL; AJ224113; CAA11832.1; JOINED; Genomic_DNA. DR EMBL; AJ224114; CAA11832.1; JOINED; Genomic_DNA. DR EMBL; AB015317; BAA33389.1; -; mRNA. DR EMBL; AC009097; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC010653; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL050025; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AL110198; CAB53673.1; -; mRNA. DR CCDS; CCDS32480.1; -. [O43747-1] DR CCDS; CCDS45522.1; -. [O43747-2] DR RefSeq; NP_001025178.1; NM_001030007.1. [O43747-2] DR RefSeq; NP_001119.3; NM_001128.5. [O43747-1] DR PDB; 1IU1; X-ray; 1.80 A; A/B=677-822. DR PDBsum; 1IU1; -. DR AlphaFoldDB; O43747; -. DR BMRB; O43747; -. DR SMR; O43747; -. DR BioGRID; 106673; 135. DR ComplexPortal; CPX-5047; Ubiquitous AP-1 Adaptor complex, sigma1a variant. DR ComplexPortal; CPX-5048; Ubiquitous AP-1 Adaptor complex, sigma1b variant. DR ComplexPortal; CPX-5049; Ubiquitous AP-1 Adaptor complex, sigma1c variant. DR ComplexPortal; CPX-5050; Endothelial AP-1 Adaptor complex, sigma1a variant. DR CORUM; O43747; -. DR IntAct; O43747; 46. DR MINT; O43747; -. DR STRING; 9606.ENSP00000377148; -. DR TCDB; 9.B.278.1.1; the organellar-targeting adaptor protein complex (o-apc) family. DR GlyGen; O43747; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O43747; -. DR MetOSite; O43747; -. DR PhosphoSitePlus; O43747; -. DR SwissPalm; O43747; -. DR BioMuta; AP1G1; -. DR EPD; O43747; -. DR jPOST; O43747; -. DR MassIVE; O43747; -. DR MaxQB; O43747; -. DR PaxDb; 9606-ENSP00000377148; -. DR PeptideAtlas; O43747; -. DR ProteomicsDB; 49146; -. [O43747-1] DR ProteomicsDB; 49147; -. [O43747-2] DR Pumba; O43747; -. DR Antibodypedia; 3960; 305 antibodies from 34 providers. DR DNASU; 164; -. DR Ensembl; ENST00000299980.9; ENSP00000299980.4; ENSG00000166747.13. [O43747-1] DR Ensembl; ENST00000393512.7; ENSP00000377148.3; ENSG00000166747.13. [O43747-2] DR Ensembl; ENST00000569748.5; ENSP00000454523.1; ENSG00000166747.13. [O43747-1] DR GeneID; 164; -. DR KEGG; hsa:164; -. DR MANE-Select; ENST00000299980.9; ENSP00000299980.4; NM_001128.6; NP_001119.3. DR UCSC; uc010cgg.4; human. [O43747-1] DR AGR; HGNC:555; -. DR CTD; 164; -. DR DisGeNET; 164; -. DR GeneCards; AP1G1; -. DR HGNC; HGNC:555; AP1G1. DR HPA; ENSG00000166747; Low tissue specificity. DR MalaCards; AP1G1; -. DR MIM; 603533; gene. DR MIM; 619467; phenotype. DR MIM; 619548; phenotype. DR neXtProt; NX_O43747; -. DR OpenTargets; ENSG00000166747; -. DR Orphanet; 528084; Non-specific syndromic intellectual disability. DR PharmGKB; PA24845; -. DR VEuPathDB; HostDB:ENSG00000166747; -. DR eggNOG; KOG1062; Eukaryota. DR GeneTree; ENSGT00950000182838; -. DR HOGENOM; CLU_003824_0_0_1; -. DR InParanoid; O43747; -. DR OMA; AICAMRI; -. DR OrthoDB; 25313at2759; -. DR PhylomeDB; O43747; -. DR TreeFam; TF300367; -. DR PathwayCommons; O43747; -. DR Reactome; R-HSA-164940; Nef mediated downregulation of MHC class I complex cell surface expression. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis. DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis. DR SignaLink; O43747; -. DR SIGNOR; O43747; -. DR BioGRID-ORCS; 164; 81 hits in 1162 CRISPR screens. DR ChiTaRS; AP1G1; human. DR EvolutionaryTrace; O43747; -. DR GeneWiki; AP1G1; -. DR GenomeRNAi; 164; -. DR Pharos; O43747; Tbio. DR PRO; PR:O43747; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; O43747; Protein. DR Bgee; ENSG00000166747; Expressed in buccal mucosa cell and 204 other cell types or tissues. DR ExpressionAtlas; O43747; baseline and differential. DR GO; GO:0030121; C:AP-1 adaptor complex; IBA:GO_Central. DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell. DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:MGI. DR GO; GO:0030665; C:clathrin-coated vesicle membrane; ISS:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005769; C:early endosome; NAS:ComplexPortal. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0098793; C:presynapse; IEA:Ensembl. DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central. DR GO; GO:0005518; F:collagen binding; IEA:Ensembl. DR GO; GO:0030742; F:GTP-dependent protein binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0019894; F:kinesin binding; IPI:UniProtKB. DR GO; GO:0031267; F:small GTPase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0110010; P:basolateral protein secretion; NAS:ComplexPortal. DR GO; GO:0035646; P:endosome to melanosome transport; IMP:ParkinsonsUK-UCL. DR GO; GO:0090160; P:Golgi to lysosome transport; IMP:UniProtKB. DR GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:1903232; P:melanosome assembly; NAS:ComplexPortal. DR GO; GO:0032438; P:melanosome organization; IC:ParkinsonsUK-UCL. DR GO; GO:0060155; P:platelet dense granule organization; NAS:ComplexPortal. DR GO; GO:0043323; P:positive regulation of natural killer cell degranulation; IMP:UniProtKB. DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IMP:UniProtKB. DR GO; GO:0016182; P:synaptic vesicle budding from endosome; IEA:Ensembl. DR GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl. DR GO; GO:0016192; P:vesicle-mediated transport; NAS:ComplexPortal. DR Gene3D; 2.60.40.1230; -; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 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 PANTHER; PTHR22780; ADAPTIN, ALPHA/GAMMA/EPSILON; 1. DR PANTHER; PTHR22780:SF26; AP-1 COMPLEX SUBUNIT GAMMA-1; 1. 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; ARM repeat; 1. DR SUPFAM; SSF49348; Clathrin adaptor appendage domain; 1. DR PROSITE; PS50180; GAE; 1. DR Genevisible; O43747; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Coated pit; Cytoplasm; KW Cytoplasmic vesicle; Disease variant; Golgi apparatus; KW Intellectual disability; Membrane; Protein transport; Reference proteome; KW Transport. FT CHAIN 1..822 FT /note="AP-1 complex subunit gamma-1" FT /id="PRO_0000193758" FT DOMAIN 702..817 FT /note="GAE" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00093" FT REGION 597..628 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 213 FT /note="R -> RKNE (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9653655" FT /id="VSP_040133" FT VARIANT 15 FT /note="R -> Q (in USRISD; does not rescue morphological FT defects in a zebrafish animal model)" FT /evidence="ECO:0000269|PubMed:34102099" FT /id="VAR_086350" FT VARIANT 35 FT /note="R -> Q (in USRISD; does not rescue morphological FT defects in a zebrafish animal model)" FT /evidence="ECO:0000269|PubMed:34102099" FT /id="VAR_086351" FT VARIANT 35 FT /note="R -> W (in USRISD; does not rescue morphological FT defects in a zebrafish animal model)" FT /evidence="ECO:0000269|PubMed:34102099" FT /id="VAR_086352" FT VARIANT 195 FT /note="V -> G (in dbSNP:rs36037071)" FT /id="VAR_048194" FT VARIANT 243 FT /note="P -> H (in USRISR; does not fully rescue FT morphological defects in a zebrafish animal model; affects FT trafficking of transferrin from early to recycling FT endosomes; no effect on subcellular location in the FT perinuclear region; does not affect interaction with AP-1 FT complex subunits AP1B1, AP1M1 and AP1S1)" FT /evidence="ECO:0000269|PubMed:34102099" FT /id="VAR_086353" FT VARIANT 366 FT /note="M -> V (in USRISR; does not fully rescue FT morphological defects in a zebrafish animal model; affects FT trafficking of transferrin from recycling endosomes to FT plasma membrane; no effect on subcellular location in the FT perinuclear region; does not affect interaction with AP-1 FT complex subunits AP1B1, AP1M1 and AP1S1)" FT /evidence="ECO:0000269|PubMed:34102099" FT /id="VAR_086354" FT VARIANT 685 FT /note="P -> H (in dbSNP:rs904763)" FT /evidence="ECO:0000269|PubMed:9733768" FT /id="VAR_013572" FT VARIANT 817 FT /note="P -> R (in USRISD; does not fully rescue FT morphological defects in a zebrafish animal model)" FT /evidence="ECO:0000269|PubMed:34102099" FT /id="VAR_086355" FT CONFLICT 61 FT /note="Y -> N (in Ref. 1; CAA11832)" FT /evidence="ECO:0000305" FT CONFLICT 141 FT /note="E -> K (in Ref. 1; CAA11832)" FT /evidence="ECO:0000305" FT CONFLICT 154 FT /note="R -> K (in Ref. 1; CAA11832)" FT /evidence="ECO:0000305" FT CONFLICT 174..175 FT /note="MF -> NV (in Ref. 1; CAA11832)" FT /evidence="ECO:0000305" FT STRAND 707..712 FT /evidence="ECO:0007829|PDB:1IU1" FT STRAND 715..723 FT /evidence="ECO:0007829|PDB:1IU1" FT STRAND 730..739 FT /evidence="ECO:0007829|PDB:1IU1" FT STRAND 741..743 FT /evidence="ECO:0007829|PDB:1IU1" FT STRAND 745..753 FT /evidence="ECO:0007829|PDB:1IU1" FT STRAND 758..762 FT /evidence="ECO:0007829|PDB:1IU1" FT HELIX 772..774 FT /evidence="ECO:0007829|PDB:1IU1" FT STRAND 778..785 FT /evidence="ECO:0007829|PDB:1IU1" FT STRAND 795..802 FT /evidence="ECO:0007829|PDB:1IU1" FT STRAND 805..812 FT /evidence="ECO:0007829|PDB:1IU1" FT HELIX 818..820 FT /evidence="ECO:0007829|PDB:1IU1" SQ SEQUENCE 822 AA; 91351 MW; 42EF40223DFBA5E9 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 TTNGPTEIVQ TNGETEPAPL ETKPPPSGPQ PTSQANDLLD LLGGNDITPV IPTAPTSKPS SAGGELLDLL GDINLTGAPA AAPAPASVPQ ISQPPFLLDG LSSQPLFNDI AAGIPSITAY SKNGLKIEFT FERSNTNPSV TVITIQASNS TELDMTDFVF QAAVPKTFQL QLLSPSSSIV PAFNTGTITQ VIKVLNPQKQ QLRMRIKLTY NHKGSAMQDL AEVNNFPPQS WQ //