AP1G1_PONAB
ID AP1G1_PONAB Reviewed; 822 AA.
AC Q5R5M2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Gamma-adaptin;
DE AltName: Full=Gamma1-adaptin;
DE AltName: Full=Golgi adaptor HA1/AP1 adaptin subunit gamma-1;
GN Name=AP1G1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250|UniProtKB:O43747}.
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) (By similarity).
CC Interacts (via GAE domain) with RABEP1 (By similarity). Interacts with
CC EPS15 (By similarity). Interacts with SYNRG/gamma-synergin (By
CC similarity). Interacts (via GAE domain) with AP1AR (via coiled-coil
CC domain) (By similarity). Interacts with CLN3 (via dileucine motif);
CC this interaction facilitates lysosomal targeting (By similarity).
CC Interacts (via GAE domain) with AFTPH/aftiphilin; the interaction is
CC required to recruit AFTPH/aftiphilin to the perinuclear region of the
CC cell (By similarity). {ECO:0000250|UniProtKB:O43747,
CC ECO:0000250|UniProtKB:P22892}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:O43747}.
CC Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC {ECO:0000250|UniProtKB:O43747}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O43747}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O43747}. Cytoplasm
CC {ECO:0000250|UniProtKB:O43747}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:O43747}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250|UniProtKB:O43747}. Membrane, clathrin-coated pit
CC {ECO:0000250|UniProtKB:O43747}. Note=Component of the coat surrounding
CC the cytoplasmic face of coated vesicles located at the Golgi complex
CC (By similarity). Co-localizes with AFTPH/aftiphilin in the cytoplasm
CC (By similarity). {ECO:0000250|UniProtKB:O43747}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; CR860835; CAH92944.1; -; mRNA.
DR RefSeq; NP_001126734.1; NM_001133262.1.
DR AlphaFoldDB; Q5R5M2; -.
DR BMRB; Q5R5M2; -.
DR SMR; Q5R5M2; -.
DR STRING; 9601.ENSPPYP00000008496; -.
DR PRIDE; Q5R5M2; -.
DR GeneID; 100173736; -.
DR KEGG; pon:100173736; -.
DR CTD; 164; -.
DR eggNOG; KOG1062; Eukaryota.
DR InParanoid; Q5R5M2; -.
DR OrthoDB; 250202at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0030121; C:AP-1 adaptor complex; IEA:InterPro.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
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 2: Evidence at transcript level;
KW Coated pit; Cytoplasm; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..822
FT /note="AP-1 complex subunit gamma-1"
FT /id="PRO_0000328678"
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"
SQ SEQUENCE 822 AA; 91321 MW; 7E507FE096741667 CRC64;
MPAPIRLREL IRTIRTARTQ AEEREMIQKE CAAIRSSFRE EDNTYRCRNV AKLLYMHMLG
YPAHFGQLEC LKLIASQKFT DKRIGYLGAM LLLDERQDVH LLMTNCIKND LNHSTQFVQG
LALCTLGCMG SSEMCRDLAG EVEKLLKTSN SYLRKKAALC AVHVIRKVPE LMEMFLPATK
NLLNEKNHGV LHTSVVLLTE MCERSPDMPA HFRKLVPQLV RILKNLIMSG YSPEHDVSGI
SDPFLQVRIL RLLRILGRND DDSSEAMNDI LAQVATNTET SKNVGNAILY ETVLTIMDIK
SESGLRVLAI NILGRFLLNN DKNIRYVALT SLLKTVRTDH NTVQRHRSTI VDCLKDLDVS
IKRRAMELSF ALVNGNNIRG MMKELLYFLD SCEPEFKADC ASGIFLAAEK YAPSKRWHID
TIMRVLTTAG SYVRDDAVPN LIQLITNSVE MHAYTVQRLY KAILGDYSQQ PLVQVAAWCI
GEYGDLLVSG QCEEEGPIQV 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
