AP1G2_HUMAN
ID AP1G2_HUMAN Reviewed; 785 AA.
AC O75843; D3DS51; O75504;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=AP-1 complex subunit gamma-like 2;
DE AltName: Full=Gamma2-adaptin;
DE Short=G2ad;
GN Name=AP1G2;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, NEGATIVE
RP INTERACTION WITH APB1, AND INTERACTION WITH AP1S1 AND AP1S2.
RC TISSUE=Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=9762922; DOI=10.1016/s0014-5793(98)01083-7;
RA Lewin D.A., Sheff D., Ooi C.E., Whitney J.A., Yamamoto E., Chicione L.M.,
RA Webster P., Bonifacino J.S., Mellman I.;
RT "Cloning, expression, and localization of a novel gamma-adaptin-like
RT molecule.";
RL FEBS Lett. 435:263-268(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH HBV MAJOR SURFACE ANTIGEN L (MICROBIAL INFECTION), AND
RP SUBCELLULAR LOCATION.
RX PubMed=11333915; DOI=10.1128/jvi.75.11.5343-5351.2001;
RA Hartmann-Stuehler C., Prange R.;
RT "Hepatitis B virus large envelope protein interacts with gamma2-adaptin, a
RT clathrin adaptor-related protein.";
RL J. Virol. 75:5343-5351(2001).
RN [5]
RP INTERACTION WITH RABEP1; CLINT1; NECAP1 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 [6]
RP FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, INTERACTION WITH HBV
RP CORE PROTEIN (MICROBIAL INFECTION) AND UBIQUITIN, AND MUTAGENESIS OF
RP LEU-369; ALA-372 AND SER-376.
RX PubMed=16867982; DOI=10.1074/jbc.m603517200;
RA Rost M., Mann S., Lambert C., Doring T., Thome N., Prange R.;
RT "Gamma-adaptin, a novel ubiquitin-interacting adaptor, and Nedd4 ubiquitin
RT ligase control hepatitis B virus maturation.";
RL J. Biol. Chem. 281:29297-29308(2006).
RN [7]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=17553870; DOI=10.1128/jvi.00479-07;
RA Lambert C., Doering T., Prange R.;
RT "Hepatitis B virus maturation is sensitive to functional inhibition of
RT ESCRT-III, Vps4, and gamma 2-adaptin.";
RL J. Virol. 81:9050-9060(2007).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP STRUCTURE BY NMR OF 662-785.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the alpha adaptin C2 domain from human adapter-
RT related protein complex 1 gamma 2 subunit.";
RL Submitted (JUL-2007) to the PDB data bank.
CC -!- FUNCTION: May function in protein sorting in late endosomes or
CC multivesucular bodies (MVBs). {ECO:0000269|PubMed:9733768}.
CC -!- FUNCTION: (Microbial infection) Involved in MVB-assisted maturation of
CC hepatitis B virus (HBV). {ECO:0000269|PubMed:16867982,
CC ECO:0000269|PubMed:17553870}.
CC -!- SUBUNIT: May interact with AP1S1/Sigma1A-adaptin and AP1S2/Sigma1B-
CC adaptin (PubMed:9733768). Probably does not interact with APB1
CC (PubMed:9733768). Interacts (via GAE domain) with RABEP1, NECAP1,
CC CLINT1 and AFTPH/aftiphilin (PubMed:14665628).
CC {ECO:0000269|PubMed:14665628, ECO:0000269|PubMed:9733768}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HBV major surface antigen
CC L. Interacts with HBV core protein C in a ubiquitin-dependent manner.
CC {ECO:0000269|PubMed:11333915, ECO:0000269|PubMed:16867982}.
CC -!- INTERACTION:
CC O75843; Q15276: RABEP1; NbExp=2; IntAct=EBI-373637, EBI-447043;
CC O75843; P03139-1: S; Xeno; NbExp=6; IntAct=EBI-373637, EBI-16065097;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:11333915, ECO:0000269|PubMed:9762922}; Peripheral
CC membrane protein; Cytoplasmic side {ECO:0000269|PubMed:11333915}.
CC Cytoplasmic vesicle membrane {ECO:0000269|PubMed:9733768}; Peripheral
CC membrane protein. Endosome membrane {ECO:0000269|PubMed:16867982};
CC Peripheral membrane protein. Note=Mainly localized to perinuclear
CC vesicular structures (PubMed:9733768). Colocalizes with HBV major
CC surface antigen L and HBV core protein C in CD63-containing
CC compartments (PubMed:16867982). Colocalizes with HBV major surface
CC antigen L to cis-Golgi-like structures (PubMed:11333915).
CC -!- TISSUE SPECIFICITY: Expressed in all but one (skeletal muscle) tissues
CC examined.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
CC -!- CAUTION: Does not appear to be a subunit of the clathrin-associated
CC adaptor protein complex 1 (AP-1). {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC67390.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB015318; BAA33390.1; -; mRNA.
DR EMBL; AF068706; AAC67390.1; ALT_FRAME; mRNA.
DR EMBL; CH471078; EAW66132.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66134.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66138.1; -; Genomic_DNA.
DR CCDS; CCDS9602.1; -.
DR RefSeq; NP_003908.1; NM_003917.4.
DR RefSeq; XP_005268229.1; XM_005268172.3.
DR RefSeq; XP_005268230.1; XM_005268173.3.
DR PDB; 2E9G; NMR; -; A=662-785.
DR PDB; 2YMT; X-ray; 1.80 A; A=665-785.
DR PDB; 3ZHF; X-ray; 1.70 A; A=665-785.
DR PDB; 4BCX; X-ray; 2.00 A; A=665-785.
DR PDBsum; 2E9G; -.
DR PDBsum; 2YMT; -.
DR PDBsum; 3ZHF; -.
DR PDBsum; 4BCX; -.
DR AlphaFoldDB; O75843; -.
DR BMRB; O75843; -.
DR SMR; O75843; -.
DR BioGRID; 114420; 76.
DR CORUM; O75843; -.
DR DIP; DIP-31185N; -.
DR IntAct; O75843; 27.
DR MINT; O75843; -.
DR STRING; 9606.ENSP00000312442; -.
DR GlyGen; O75843; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75843; -.
DR PhosphoSitePlus; O75843; -.
DR BioMuta; AP1G2; -.
DR EPD; O75843; -.
DR jPOST; O75843; -.
DR MassIVE; O75843; -.
DR MaxQB; O75843; -.
DR PaxDb; O75843; -.
DR PeptideAtlas; O75843; -.
DR PRIDE; O75843; -.
DR ProteomicsDB; 50225; -.
DR Antibodypedia; 110; 68 antibodies from 16 providers.
DR DNASU; 8906; -.
DR Ensembl; ENST00000308724.9; ENSP00000312442.5; ENSG00000213983.12.
DR Ensembl; ENST00000397120.8; ENSP00000380309.3; ENSG00000213983.12.
DR GeneID; 8906; -.
DR KEGG; hsa:8906; -.
DR MANE-Select; ENST00000397120.8; ENSP00000380309.3; NM_003917.5; NP_003908.1.
DR UCSC; uc001wkl.4; human.
DR CTD; 8906; -.
DR DisGeNET; 8906; -.
DR GeneCards; AP1G2; -.
DR HGNC; HGNC:556; AP1G2.
DR HPA; ENSG00000213983; Low tissue specificity.
DR MIM; 603534; gene.
DR neXtProt; NX_O75843; -.
DR OpenTargets; ENSG00000213983; -.
DR PharmGKB; PA24846; -.
DR VEuPathDB; HostDB:ENSG00000213983; -.
DR eggNOG; KOG1062; Eukaryota.
DR GeneTree; ENSGT00950000182838; -.
DR HOGENOM; CLU_003824_0_0_1; -.
DR InParanoid; O75843; -.
DR OMA; IDKRVGY; -.
DR OrthoDB; 250202at2759; -.
DR PhylomeDB; O75843; -.
DR TreeFam; TF300367; -.
DR PathwayCommons; O75843; -.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR SignaLink; O75843; -.
DR BioGRID-ORCS; 8906; 38 hits in 1079 CRISPR screens.
DR ChiTaRS; AP1G2; human.
DR EvolutionaryTrace; O75843; -.
DR GeneWiki; AP1G2; -.
DR GenomeRNAi; 8906; -.
DR Pharos; O75843; Tbio.
DR PRO; PR:O75843; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O75843; protein.
DR Bgee; ENSG00000213983; Expressed in right hemisphere of cerebellum and 177 other tissues.
DR ExpressionAtlas; O75843; baseline and differential.
DR Genevisible; O75843; HS.
DR GO; GO:0030121; C:AP-1 adaptor complex; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005798; C:Golgi-associated vesicle; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IDA:UniProtKB.
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:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; NAS:UniProtKB.
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; Cytoplasmic vesicle; Endosome; Golgi apparatus;
KW Host-virus interaction; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..785
FT /note="AP-1 complex subunit gamma-like 2"
FT /id="PRO_0000193760"
FT DOMAIN 665..780
FT /note="GAE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00093"
FT REGION 369..379
FT /note="Essential for ubiquitin-binding"
FT REGION 592..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 377
FT /note="S -> F (in dbSNP:rs12897422)"
FT /id="VAR_024363"
FT MUTAGEN 369
FT /note="L->G: Greatly diminishes interaction with ubiquitin;
FT when associated with G-372."
FT /evidence="ECO:0000269|PubMed:16867982"
FT MUTAGEN 372
FT /note="A->G: Greatly diminishes interaction with ubiquitin;
FT when associated with G-369."
FT /evidence="ECO:0000269|PubMed:16867982"
FT MUTAGEN 372
FT /note="A->G: Greatly diminishes interaction with ubiquitin;
FT when associated with G-376."
FT /evidence="ECO:0000269|PubMed:16867982"
FT MUTAGEN 376
FT /note="S->G: Greatly diminishes interaction with ubiquitin;
FT when associated with G-372."
FT /evidence="ECO:0000269|PubMed:16867982"
FT CONFLICT 204..206
FT /note="ERS -> GRN (in Ref. 2; AAC67390)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="A -> C (in Ref. 2; AAC67390)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="A -> D (in Ref. 2; AAC67390)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="K -> T (in Ref. 2; AAC67390)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="T -> S (in Ref. 2; AAC67390)"
FT /evidence="ECO:0000305"
FT CONFLICT 439..441
FT /note="VAN -> AGHT (in Ref. 2; AAC67390)"
FT /evidence="ECO:0000305"
FT STRAND 670..675
FT /evidence="ECO:0007829|PDB:3ZHF"
FT STRAND 678..685
FT /evidence="ECO:0007829|PDB:3ZHF"
FT STRAND 693..702
FT /evidence="ECO:0007829|PDB:3ZHF"
FT STRAND 704..706
FT /evidence="ECO:0007829|PDB:3ZHF"
FT STRAND 708..716
FT /evidence="ECO:0007829|PDB:3ZHF"
FT STRAND 721..725
FT /evidence="ECO:0007829|PDB:3ZHF"
FT STRAND 731..733
FT /evidence="ECO:0007829|PDB:2E9G"
FT TURN 735..737
FT /evidence="ECO:0007829|PDB:3ZHF"
FT STRAND 741..748
FT /evidence="ECO:0007829|PDB:3ZHF"
FT STRAND 758..765
FT /evidence="ECO:0007829|PDB:3ZHF"
FT STRAND 768..775
FT /evidence="ECO:0007829|PDB:3ZHF"
FT HELIX 781..783
FT /evidence="ECO:0007829|PDB:3ZHF"
SQ SEQUENCE 785 AA; 87117 MW; C189192C9811111C CRC64;
MVVPSLKLQD LIEEIRGAKT QAQEREVIQK ECAHIRASFR DGDPVHRHRQ LAKLLYVHML
GYPAHFGQME CLKLIASSRF TDKRVGYLGA MLLLDERHDA HLLITNSIKN DLSQGIQPVQ
GLALCTLSTM GSAEMCRDLA PEVEKLLLQP SPYVRKKAIL TAVHMIRKVP ELSSVFLPPC
AQLLHERHHG ILLGTITLIT ELCERSPAAL RHFRKVVPQL VHILRTLVTM GYSTEHSISG
VSDPFLQVQI LRLLRILGRN HEESSETMND LLAQVATNTD TSRNAGNAVL FETVLTIMDI
RSAAGLRVLA VNILGRFLLN SDRNIRYVAL TSLLRLVQSD HSAVQRHRPT VVECLRETDA
SLSRRALELS LALVNSSNVR AMMQELQAFL ESCPPDLRAD CASGILLAAE RFAPTKRWHI
DTILHVLTTA GTHVRDDAVA NLTQLIGGAQ ELHAYSVRRL YNALAEDISQ QPLVQVAAWC
IGEYGDLLLA GNCEEIEPLQ VDEEEVLALL EKVLQSHMSL PATRGYALTA LMKLSTRLCG
DNNRIRQVVS IYGSCLDVEL QQRAVEYDTL FRKYDHMRAA ILEKMPLVER DGPQADEEAK
ESKEAAQLSE AAPVPTEPQA SQLLDLLDLL DGASGDVQHP PHLDPSPGGA LVHLLDLPCV
PPPPAPIPDL KVFEREGVQL NLSFIRPPEN PALLLITITA TNFSEGDVTH FICQAAVPKS
LQLQLQAPSG NTVPARGGLP ITQLFRILNP NKAPLRLKLR LTYDHFHQSV QEIFEVNNLP
VESWQ
