AP1G2_MOUSE
ID AP1G2_MOUSE Reviewed; 791 AA.
AC O88512; Q2YDV3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=AP-1 complex subunit gamma-like 2;
DE AltName: Full=Gamma2-adaptin;
DE Short=G2ad;
GN Name=Ap1g2;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, and Spleen;
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).
CC -!- FUNCTION: May function in protein sorting in late endosomes or
CC multivesucular bodies (MVBs). Involved in MVB-assisted maturation of
CC hepatitis B virus (HBV). {ECO:0000250|UniProtKB:O75843}.
CC -!- SUBUNIT: May interact with AP1S1/Sigma1A-adaptin and AP1S2/Sigma1B-
CC adaptin (By similarity). Probably does not interact with APB1 (By
CC similarity). Interacts (via GAE domain) with RABEP1, NECAP1, CLINT1 and
CC AFTPH/aftiphilin (By similarity). Interacts with HBV major surface
CC antigen L. Interacts with HBV core protein C in a ubiquitin-dependent
CC manner. Binds ubiquitin. {ECO:0000250|UniProtKB:O75843}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O75843}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O75843}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O75843}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:O75843}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O75843}. Endosome membrane
CC {ECO:0000250|UniProtKB:O75843}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O75843}. Note=Mainly localized to perinuclear
CC vesicular structures. Colocalizes with HBV major surface antigen L and
CC HBV core protein C in CD63-containing compartments. Colocalizes with
CC HBV major surface antigen L to cis-Golgi-like structures.
CC {ECO:0000250|UniProtKB:O75843}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
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; AF068707; AAC67391.1; -; mRNA.
DR EMBL; CH466535; EDL36306.1; -; Genomic_DNA.
DR EMBL; CH466535; EDL36307.1; -; Genomic_DNA.
DR EMBL; BC108374; AAI08375.1; -; mRNA.
DR CCDS; CCDS36929.1; -.
DR RefSeq; NP_031481.2; NM_007455.5.
DR AlphaFoldDB; O88512; -.
DR SMR; O88512; -.
DR BioGRID; 198124; 2.
DR STRING; 10090.ENSMUSP00000043996; -.
DR iPTMnet; O88512; -.
DR PhosphoSitePlus; O88512; -.
DR EPD; O88512; -.
DR MaxQB; O88512; -.
DR PaxDb; O88512; -.
DR PeptideAtlas; O88512; -.
DR PRIDE; O88512; -.
DR ProteomicsDB; 296053; -.
DR Antibodypedia; 110; 68 antibodies from 16 providers.
DR DNASU; 11766; -.
DR Ensembl; ENSMUST00000036041; ENSMUSP00000043996; ENSMUSG00000040701.
DR Ensembl; ENSMUST00000170285; ENSMUSP00000128427; ENSMUSG00000040701.
DR GeneID; 11766; -.
DR KEGG; mmu:11766; -.
DR UCSC; uc007tyd.3; mouse.
DR CTD; 8906; -.
DR MGI; MGI:1328307; Ap1g2.
DR VEuPathDB; HostDB:ENSMUSG00000040701; -.
DR eggNOG; KOG1062; Eukaryota.
DR GeneTree; ENSGT00950000182838; -.
DR HOGENOM; CLU_003824_0_0_1; -.
DR InParanoid; O88512; -.
DR OMA; IDKRVGY; -.
DR OrthoDB; 250202at2759; -.
DR PhylomeDB; O88512; -.
DR TreeFam; TF300367; -.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR BioGRID-ORCS; 11766; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Ap1g2; mouse.
DR PRO; PR:O88512; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; O88512; protein.
DR Bgee; ENSMUSG00000040701; Expressed in duodenum and 157 other tissues.
DR ExpressionAtlas; O88512; baseline and differential.
DR Genevisible; O88512; MM.
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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005798; C:Golgi-associated vesicle; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; TAS:MGI.
DR GO; GO:0030133; C:transport vesicle; ISS: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; TAS: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 Cytoplasmic vesicle; Endosome; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..791
FT /note="AP-1 complex subunit gamma-like 2"
FT /id="PRO_0000193761"
FT DOMAIN 671..786
FT /note="GAE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00093"
FT CONFLICT 19
FT /note="K -> E (in Ref. 1; AAC67391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 791 AA; 87863 MW; 21F744FC8EEFB932 CRC64;
MVVHSLRLQD LIEEIRGAKT QAQEREVIQK ECAQIRASFR DGDPLQRHRQ LAKLLYVHML
GYPAHFGQME CLKLIASPRF TDKRVGYLGA MLLLDERHDS HLLITNSIKN DLSQGNQPVQ
GLALCTLSTM GSAEMCRDLA PEVEKLLLQP SPYVRKKAIL TAVHMIRKDP ELSGIFLPPC
TKLLRERHHG IQLGTVTLIT ELCERNPAAL RHFRKVVPQL VQILRTLVTT GYSTEHSISG
VSDPFLQVQI LRLLRILGRN HEESSETMND LLAQVATNTD TSRNAGNAVL LETVLTIMAI
HSAAGLRVLA VNILGRFLLN NDKNIRYVAL TSLLQLVQSD HSAVQRHRST VVECLQETDA
SLSRRALELS LALVNSSNVR AMMQELQAFL ESCPPDLRAD CASGILLAAE RFAPSKRWHI
DTILHVLTTA GAHVRDDAVA NLTQLIGEAE ELHTYSVRRL YSALAEDISQ QPLVQVAAWC
IGEYGDLLLE GNCEETEPFQ VEEEDVLALL EKVLQSHMSL PATRGYAITA LMKLSTRLRG
DNNRIRQVVS IYGSCVDLEL QQRAVEYNTL FQKYDHMRAA ILEKMPLVER GDPHVKEGGK
EKQTEAQPLE VTAPAPTEPQ ATKLLDLLDL LGDTSEPLSS GHAQHLPPQT PSPGEALIHL
LDLPCTPPPP APIPSVRVFE REGLQLDLSF MRPLETPALL LVTATTTNSS KEDVTHFVCQ
AAVPKSFQLQ LQAPSGNTIP AQGGLPITQV FRILNPNQAP LRLKLRLTYN HSGQPVQEIF
EVDNLPVETW Q
