AP1G1_HUMAN
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 03-AUG-2022, entry version 208.
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}.
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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; 99.
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; 43.
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 PhosphoSitePlus; O43747; -.
DR SwissPalm; O43747; -.
DR BioMuta; AP1G1; -.
DR EPD; O43747; -.
DR jPOST; O43747; -.
DR MassIVE; O43747; -.
DR MaxQB; O43747; -.
DR PaxDb; O43747; -.
DR PeptideAtlas; O43747; -.
DR PRIDE; O43747; -.
DR ProteomicsDB; 49146; -. [O43747-1]
DR ProteomicsDB; 49147; -. [O43747-2]
DR Antibodypedia; 3960; 258 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 CTD; 164; -.
DR DisGeNET; 164; -.
DR GeneCards; AP1G1; -.
DR HGNC; HGNC:555; AP1G1.
DR HPA; ENSG00000166747; Low tissue specificity.
DR MIM; 603533; gene.
DR MIM; 619467; phenotype.
DR MIM; 619548; phenotype.
DR neXtProt; NX_O43747; -.
DR OpenTargets; ENSG00000166747; -.
DR Orphanet; 88616; Autosomal recessive non-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; NEFKPVM; -.
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; 73 hits in 1079 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 202 other tissues.
DR ExpressionAtlas; O43747; baseline and differential.
DR Genevisible; O43747; HS.
DR GO; GO:0030121; C:AP-1 adaptor complex; IBA:GO_Central.
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; IC:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
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:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
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; 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; IC: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; IC:ComplexPortal.
DR GO; GO:0032438; P:melanosome organization; IC:ParkinsonsUK-UCL.
DR GO; GO:0060155; P:platelet dense granule organization; IC: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:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IC:ComplexPortal.
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; 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
