AP1G1_USTMA
ID AP1G1_USTMA Reviewed; 874 AA.
AC Q99128; A0A0D1CH08; Q4PGV3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=AP-1 complex subunit gamma-1;
DE AltName: Full=Clathrin assembly protein complex 1 gamma large chain;
DE AltName: Full=Clathrin assembly protein large gamma chain;
DE AltName: Full=Gamma-adaptin;
DE Short=Gamma-ADA;
GN Name=APL4; ORFNames=UMAG_00660;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IMI 103761;
RX PubMed=7557403; DOI=10.1016/0378-1119(95)00355-a;
RA Keon J.P.R., Jewitt S., Hargreaves J.A.;
RT "A gene encoding gamma-adaptin is required for apical extension growth in
RT Ustilago maydis.";
RL Gene 162:141-145(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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). Required
CC for apical growth extension. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA86825.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z46804; CAA86825.1; ALT_INIT; Genomic_DNA.
DR EMBL; CM003140; KIS72247.1; -; Genomic_DNA.
DR PIR; S49876; S49876.
DR RefSeq; XP_011386466.1; XM_011388164.1.
DR AlphaFoldDB; Q99128; -.
DR SMR; Q99128; -.
DR STRING; 5270.UM00660P0; -.
DR EnsemblFungi; KIS72247; KIS72247; UMAG_00660.
DR GeneID; 23561899; -.
DR KEGG; uma:UMAG_00660; -.
DR VEuPathDB; FungiDB:UMAG_00660; -.
DR eggNOG; KOG1062; Eukaryota.
DR HOGENOM; CLU_003824_0_0_1; -.
DR InParanoid; Q99128; -.
DR OrthoDB; 250202at2759; -.
DR Proteomes; UP000000561; Chromosome 1.
DR GO; GO:0030121; C:AP-1 adaptor complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0016482; P:cytosolic transport; IEA:UniProt.
DR GO; GO:0016197; P:endosomal transport; IEA:UniProt.
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 3: Inferred from homology;
KW Cytoplasmic vesicle; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..874
FT /note="AP-1 complex subunit gamma-1"
FT /id="PRO_0000193763"
FT DOMAIN 761..873
FT /note="GAE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00093"
FT CONFLICT 248
FT /note="S -> T (in Ref. 1; CAA86825)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 874 AA; 95075 MW; A8221F770B6DF007 CRC64;
MSTFFQKQQQ VAALDPRLGG LMASAGLYNL KALIKAIRSC KTLADERSLI QKESASIRTA
FKDEDPFARH NNIAKLLYIH MLGYPAHFGQ IECLKLVATP RFTDKRLGYL GIMLLLDENT
EVLTLVTNGL KNDMEHSNMY VCGLALCTFA NIASEEMSRD LCNEIEKLMG SSNTYIRRKA
AICAMRIVRK VPDLIDHFVD RTQQLLSDKN HGVLLCAVTL AIEICRQDDE ALTVYRRAVP
LLVQHLKSLV TTGYSPEHDV SGITDPFLQV KILRLLRILG KENAQASETM NDILAQVATN
TEASKNVGNS ILYETVLTIL EIDADNGLRV MAINILGKFL SNRDNNIRYV ALNTLSKVVS
MDTNAVQRHR NIILDCLRDG DISIRRRALE LSYALINESN VRVLTRELLS FLEVADNEFK
LGMTTQICLA AEKFAPNKRW HIDTVLRVLK LAGNYVREEI LSAFIRLVCH TPELQAYTVQ
KLFSGLHQDF SQESLTLAAV WVIGEFGDVL IQGGNFEDEE LVREVQPKDV VDLLSSVLDS
PYVNGLIRQF VLTSLAKLHT RLSDASQQSR IEQIIASFET SVEVEIQQRS VEFATLLKRS
DIRQGVLESM PPPEIKQTVL GTVSEAKPVG STRSDKDALL DLMGDEMPVT SGGGTGADNA
PSGATQQSTH DLLADIFGGG DMGGMPSAAP AASASAAQKP KSSVNDILGL FGDGASAPAA
AAQQAPTPAP AATSSYGGLD LLGGLGASSS ASTPAATPAS TVAKSHTVYT KHGLTITLTP
TTNPARPEIV HITARFTSAT SAISNINFQA AVPKTHKLQM QAISNSTVHP DSTETQPLRV
MVPPGAAVRL RLRIAFQVDG HSVQDQTDWA QPSA