AP1G_DICDI
ID AP1G_DICDI Reviewed; 895 AA.
AC Q8I8U2; Q54T69;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=AP-1 complex subunit gamma;
DE AltName: Full=Adaptor protein complex AP-1 subunit gamma;
DE AltName: Full=Adaptor-related protein complex 1 subunit gamma;
DE AltName: Full=Clathrin assembly protein complex 1 gamma large chain;
DE AltName: Full=Gamma1-adaptin;
GN Name=ap1g1; Synonyms=aptC; ORFNames=DDB_G0281957;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12802059; DOI=10.1091/mbc.e02-10-0627;
RA Lefkir Y., de Chassey B., Dubois A., Bogdanovic A., Brady R.J.,
RA Destaing O., Bruckert F., O'Halloran T.J., Cosson P., Letourneur F.;
RT "The AP-1 clathrin-adaptor is required for lysosomal enzymes sorting and
RT biogenesis of the contractile vacuole complex in Dictyostelium cells.";
RL Mol. Biol. Cell 14:1835-1851(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP INTERACTION WITH RHGA, AND MUTAGENESIS OF ARG-871 AND LYS-873.
RX PubMed=16478785; DOI=10.1242/jcs.02808;
RA Mercanti V., Blanc C., Lefkir Y., Cosson P., Letourneur F.;
RT "Acidic clusters target transmembrane proteins to the contractile vacuole
RT in Dictyostelium cells.";
RL J. Cell Sci. 119:837-845(2006).
CC -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that
CC plays a role in protein sorting in the trans-Golgi network (TGN) and
CC endosomes. The AP complexes mediate the recruitment of clathrin to
CC membranes and the recognition of sorting signals within the cytosolic
CC tails of transmembrane cargo molecules. Also involved in early steps of
CC phagocytosis and macropinocytosis.
CC -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC of two large adaptins (gamma-type subunit and beta-type subunit), a
CC medium adaptin (mu-type subunit) and a small adaptin (sigma-type
CC subunit) (By similarity). Interacts with rhgA. {ECO:0000250,
CC ECO:0000269|PubMed:16478785}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network. Cytoplasmic
CC vesicle, clathrin-coated vesicle membrane {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; AY144597; AAN41659.1; -; mRNA.
DR EMBL; AAFI02000044; EAL66400.1; -; Genomic_DNA.
DR RefSeq; XP_640382.1; XM_635290.1.
DR AlphaFoldDB; Q8I8U2; -.
DR SMR; Q8I8U2; -.
DR STRING; 44689.DDB0214928; -.
DR PaxDb; Q8I8U2; -.
DR PRIDE; Q8I8U2; -.
DR EnsemblProtists; EAL66400; EAL66400; DDB_G0281957.
DR GeneID; 8623337; -.
DR KEGG; ddi:DDB_G0281957; -.
DR dictyBase; DDB_G0281957; ap1g1.
DR eggNOG; KOG1062; Eukaryota.
DR HOGENOM; CLU_003824_0_0_1; -.
DR InParanoid; Q8I8U2; -.
DR OMA; NEFKPVM; -.
DR PhylomeDB; Q8I8U2; -.
DR Reactome; R-DDI-432720; Lysosome Vesicle Biogenesis.
DR PRO; PR:Q8I8U2; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0030121; C:AP-1 adaptor complex; IDA:dictyBase.
DR GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0140312; F:cargo adaptor activity; IBA:GO_Central.
DR GO; GO:0035615; F:clathrin adaptor activity; IDA:dictyBase.
DR GO; GO:0030276; F:clathrin binding; IPI:dictyBase.
DR GO; GO:0006895; P:Golgi to endosome transport; IDA:dictyBase.
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 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; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..895
FT /note="AP-1 complex subunit gamma"
FT /id="PRO_0000328679"
FT REPEAT 130..166
FT /note="HEAT 1"
FT REPEAT 167..205
FT /note="HEAT 2"
FT REPEAT 211..256
FT /note="HEAT 3"
FT REPEAT 301..339
FT /note="HEAT 4"
FT REPEAT 341..376
FT /note="HEAT 5"
FT DOMAIN 775..893
FT /note="GAE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00093"
FT REGION 591..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 871
FT /note="R->Q: Decrease in the interaction with rhgA."
FT /evidence="ECO:0000269|PubMed:16478785"
FT MUTAGEN 873
FT /note="K->Q: Decrease in the interaction with rhgA."
FT /evidence="ECO:0000269|PubMed:16478785"
SQ SEQUENCE 895 AA; 99625 MW; E57EA316FEA6FD84 CRC64;
MSSKLRDLIK TVRSCKTAAE ERSQIAKESA LIRTAMKEED LESRQRNVAK LLYIHMLGYP
TQFGQMECLK LIVSPSYADK RIGYLGLMLL LDEKQEVLLL ATNCIRGDIM NSNQFIVGVS
LCAFGNICST AMARDISPEI EKVISHSNPY IRKKAALCAI RVLRKVPDLT ENYIPKIKAL
LSERNHAVIL TALTLIIEIC EMDSTQIIHF KKMVPQLVRI LKSLTSSGYL PEHDIGGVTD
PFLQVKILRL LRILGQNDPE ASDAMNDILA QVSTNTDSTK NVGNAILYEC VQTIMTIESE
NGLKVMAINI LGRFLLNRDN NIRYVALNTL SRVVNTDIQA VQRHRNTIVE CLKDPDVSIR
CRALDLIYSL VTESNIRVLV RELLNFLLIA DAQFKSELVA KLCIVTEKYA PNKRWQIDTI
LRVMSIAGNF IPDEVPSNLI QLISSTPELS SYAVQKLYLA LKQDITQQPL TQVGLWCIGE
YGDLLVADKS QLPKDEDGLS LNVSEQAVID IIDLIFRHAT TTQATRQYSL TSLAKLSSRF
SQSSLQRIKT MIDNYKQNIN LELQQRACEY STLFDFDKKA SILDRMPPIE KQEESPHIGN
KNIPTQTPPQ QHYQQQQQQP QQQSSQFGSI LDGLDSPTQS SANSGNNNNN NNKQGGNAMS
LLEDIFGSAP TPTSNGNMNN NNNMNNMNNN MNNNYAMGGM GMNNNNNNSM GGMMNNNNNN
NNNNNNNNNN NKSQASALLD IMGDLQLTPT PQQPQSQSQQ ALSPTNQTSV LQPVPQPLTF
LVYQKHGLNI SYECSKPQPN NLSLTNINMV ITNTGSSPIT NFSLQAAVPK YLKIQLLAPS
STVIPPNNSG EVTQVSKVLN SQQGQKPILL RLKLDFQING QPFSDVPDTP LPSLF
