AP1G1_SCHPO
ID AP1G1_SCHPO Reviewed; 865 AA.
AC Q9UU81;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=AP-1 complex subunit gamma-1;
DE AltName: Full=Clathrin assembly protein complex 1 gamma-1 large chain;
DE AltName: Full=Clathrin assembly protein large gamma-1 chain;
DE AltName: Full=Gamma-adaptin;
GN Name=apl4; ORFNames=SPCP1E11.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Adaptins are components of the adaptor complexes which link
CC clathrin to receptors in coated vesicles. Clathrin-associated protein
CC complexes are believed to interact with the cytoplasmic tails of
CC membrane proteins, leading to their selection and concentration. The
CC AP-1 complex interacts directly with clathrin (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC of two large adaptins (gamma-type subunit apl4 and beta-type subunit
CC apl2), a medium adaptin (mu-type subunit apm1) and a small adaptin
CC (sigma-type subunit aps1). AP-1 interacts with clathrin (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}.
CC Note=Component of the coat surrounding the cytoplasmic face of coated
CC vesicles located at the Golgi complex. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; CU329672; CAB54865.1; -; Genomic_DNA.
DR PIR; T41685; T41685.
DR RefSeq; NP_588559.1; NM_001023546.2.
DR AlphaFoldDB; Q9UU81; -.
DR SMR; Q9UU81; -.
DR BioGRID; 275878; 8.
DR STRING; 4896.SPCP1E11.06.1; -.
DR iPTMnet; Q9UU81; -.
DR SwissPalm; Q9UU81; -.
DR MaxQB; Q9UU81; -.
DR PaxDb; Q9UU81; -.
DR PRIDE; Q9UU81; -.
DR EnsemblFungi; SPCP1E11.06.1; SPCP1E11.06.1:pep; SPCP1E11.06.
DR GeneID; 2539311; -.
DR KEGG; spo:SPCP1E11.06; -.
DR PomBase; SPCP1E11.06; apl4.
DR VEuPathDB; FungiDB:SPCP1E11.06; -.
DR eggNOG; KOG1062; Eukaryota.
DR HOGENOM; CLU_003824_0_0_1; -.
DR InParanoid; Q9UU81; -.
DR OMA; NEFKPVM; -.
DR PhylomeDB; Q9UU81; -.
DR Reactome; R-SPO-432720; Lysosome Vesicle Biogenesis.
DR PRO; PR:Q9UU81; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0030121; C:AP-1 adaptor complex; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005768; C:endosome; IDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
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:0099638; P:endosome to plasma membrane protein transport; IDA:PomBase.
DR GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:PomBase.
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 3: Inferred from homology;
KW Cytoplasmic vesicle; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..865
FT /note="AP-1 complex subunit gamma-1"
FT /id="PRO_0000193762"
FT DOMAIN 746..860
FT /note="GAE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00093"
FT REGION 665..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 865 AA; 96042 MW; 05BA43A15B61E84E CRC64;
MQTTHPKNLH LTCSGVERGF TNSPKTHPKM SSLKSFIKAV RASKTTAEEH TTILKESAQI
RKNIRQGSND MRMRRKNVAK LLYLFLLGEP THFGQIECLK LLSSSRFMDK RLGYLAAMLL
LDENQEVLTL LTNSLQNDLK SRDKFIVGLA LSAFGNVAGP ELARDLSNDI AELCSNHHNY
ISKKAVLCAL RVIQKEPDLE SLYIEKTDEL LHSKSHGVLM AALAFAISAC KINPSLISRF
ESQADDLIYR IRQLSTSTYS SEHNIGNISD PFLQVKILQF LSILGQNNPK IYDKMSDLLA
QVCTNTDSSR NAGNAILYQA VRTILDLNSD SSLRVLGVNI LAKFLGNRDN NTRYVALNML
KLVVNSEENA VQRHRSTILA CLNDVDSSIQ SRALELSTFL VNEANVRFMV RELLSFLDNV
SDELRGSTAQ YITEVTNAFA PNKRWHFDTL LRVFKSAGNF VSESTLSTFL RLIASAPELH
EYAVVKLYAA LKEDVSQEAL TLSAFWVIGE YGQMLLSPTM NFDDDQTLPH SVSESDIVDI
IEEVFNSVEA SRYIIVQYGL FALTKLSARL GSSSTASRID KIIYSYKRNK NTEVQQRSVE
FHLILNDSKL SKTILEPTPA PLPPPRTTPY QNAEQKLKAN KHVEKRVQES NELLDLIGLT
TPSVAEPLET PVDEMTQSPQ SSLSRAPSTS KKSHFEDILG LFASPAPSAQ PVDSLASSFA
SLDFNASASQ PSNNLSLLSS IPSTSKSYPP IVVFDKHDVT LTLVPSKEES TKTAVIEAKF
KNKNPMTRVE KIHLEVAVPK SQKLKIQPLR TTSMEPGGET SQTLRVHGPS GSQVKLRLRI
SVVRQGGSNT LDQVDFGKLP SDLLQ
