AP1G1_ARATH
ID AP1G1_ARATH Reviewed; 876 AA.
AC Q84K16; O81227; Q9LRA3; Q9XFS0;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=AP-1 complex subunit gamma-1;
DE AltName: Full=Adaptor protein complex AP-1 large 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 Short=At-g-Ad;
DE Short=At-gamma-Ad;
DE AltName: Full=Gamma-adaptin 1;
GN Name=GAMMA-ADR; OrderedLocusNames=At1g23900; ORFNames=T23E23.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RA Schledzewski K., LaBrie S.T., Crawford N.M., Brinkmann H., Mendel R.R.;
RT "Molecular cloning and sequencing of the gamma-adaptin 1 gene of
RT Arabidopsis thaliana.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, AND REVIEW.
RX PubMed=11598180; DOI=10.1091/mbc.12.10.2907;
RA Boehm M., Bonifacino J.S.;
RT "Adaptins: the final recount.";
RL Mol. Biol. Cell 12:2907-2920(2001).
RN [6]
RP INTERACTION WITH DRP2A.
RX PubMed=12207647; DOI=10.1046/j.1365-313x.2002.01377.x;
RA Lam B.C.-H., Sage T.L., Bianchi F., Blumwald E.;
RT "Regulation of ADL6 activity by its associated molecular network.";
RL Plant J. 31:565-576(2002).
RN [7]
RP INTERACTION WITH EPSIN1.
RX PubMed=16905657; DOI=10.1105/tpc.105.039123;
RA Song J., Lee M.H., Lee G.-J., Yoo C.M., Hwang I.;
RT "Arabidopsis EPSIN1 plays an important role in vacuolar trafficking of
RT soluble cargo proteins in plant cells via interactions with clathrin, AP-1,
RT VTI11, and VSR1.";
RL Plant Cell 18:2258-2274(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND COMPONENT OF THE AP-1 COMPLEX.
RX PubMed=23543752; DOI=10.1093/pcp/pct048;
RA Teh O.K., Shimono Y., Shirakawa M., Fukao Y., Tamura K., Shimada T.,
RA Hara-Nishimura I.;
RT "The AP-1 mu adaptin is required for KNOLLE localization at the cell plate
RT to mediate cytokinesis in Arabidopsis.";
RL Plant Cell Physiol. 54:838-847(2013).
CC -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that
CC plays a role in protein sorting at the trans-Golgi network and early
CC endosomes (TGN/EE). The AP complexes mediate both the recruitment of
CC clathrin to membranes and the recognition of sorting signals within the
CC cytosolic tails of transmembrane cargo molecules (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 and beta-type subunit), a
CC medium adaptin (mu-type subunit) and a small adaptin (sigma-type
CC subunit) (Probable). Binds to EPSIN1 (PubMed:16905657). Interacts with
CC DRP2A/ADL6 (via C-terminus) (PubMed:12207647).
CC {ECO:0000269|PubMed:12207647, ECO:0000269|PubMed:16905657,
CC ECO:0000305}.
CC -!- INTERACTION:
CC Q84K16; Q8VY07: EPSIN1; NbExp=2; IntAct=EBI-1163115, EBI-1162785;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasmic
CC vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF87139.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF061286; AAC28338.1; -; mRNA.
DR EMBL; AF124524; AAD28247.1; -; Genomic_DNA.
DR EMBL; AJ133777; CAB39730.1; -; mRNA.
DR EMBL; AC002423; AAF87139.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30448.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30449.1; -; Genomic_DNA.
DR EMBL; BT004307; AAO42305.1; -; mRNA.
DR EMBL; BT005557; AAO63977.1; -; mRNA.
DR PIR; T51951; T51951.
DR RefSeq; NP_173802.1; NM_102238.2.
DR RefSeq; NP_849701.1; NM_179370.4.
DR AlphaFoldDB; Q84K16; -.
DR SMR; Q84K16; -.
DR BioGRID; 24239; 14.
DR IntAct; Q84K16; 4.
DR STRING; 3702.AT1G23900.2; -.
DR PaxDb; Q84K16; -.
DR PRIDE; Q84K16; -.
DR ProteomicsDB; 240597; -.
DR EnsemblPlants; AT1G23900.1; AT1G23900.1; AT1G23900.
DR EnsemblPlants; AT1G23900.2; AT1G23900.2; AT1G23900.
DR GeneID; 839001; -.
DR Gramene; AT1G23900.1; AT1G23900.1; AT1G23900.
DR Gramene; AT1G23900.2; AT1G23900.2; AT1G23900.
DR KEGG; ath:AT1G23900; -.
DR Araport; AT1G23900; -.
DR TAIR; locus:2199897; AT1G23900.
DR eggNOG; KOG1062; Eukaryota.
DR HOGENOM; CLU_003824_0_0_1; -.
DR InParanoid; Q84K16; -.
DR OMA; WHLDTMI; -.
DR OrthoDB; 250202at2759; -.
DR PhylomeDB; Q84K16; -.
DR PRO; PR:Q84K16; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84K16; baseline and differential.
DR Genevisible; Q84K16; AT.
DR GO; GO:0030121; C:AP-1 adaptor complex; ISS:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
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; IEA:InterPro.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:TAIR.
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..876
FT /note="AP-1 complex subunit gamma-1"
FT /id="PRO_0000397852"
FT REPEAT 97..135
FT /note="HEAT 1"
FT REPEAT 136..173
FT /note="HEAT 2"
FT REPEAT 248..284
FT /note="HEAT 3"
FT REPEAT 308..345
FT /note="HEAT 4"
FT REPEAT 346..382
FT /note="HEAT 5"
FT REPEAT 384..417
FT /note="HEAT 6"
FT REPEAT 418..454
FT /note="HEAT 7"
FT REPEAT 506..545
FT /note="HEAT 8"
FT REPEAT 560..599
FT /note="HEAT 9"
FT DOMAIN 756..873
FT /note="GAE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00093"
FT CONFLICT 466
FT /note="S -> A (in Ref. 1; AAC28338/AAD28247)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="S -> L (in Ref. 1; AAC28338/AAD28247)"
FT /evidence="ECO:0000305"
FT CONFLICT 548..552
FT /note="ERIKD -> VRIKG (in Ref. 1; AAC28338/AAD28247)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="A -> V (in Ref. 1; CAB39730)"
FT /evidence="ECO:0000305"
FT CONFLICT 652
FT /note="T -> A (in Ref. 1; AAC28338/AAD28247/CAB39730)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="G -> R (in Ref. 1; CAB39730)"
FT /evidence="ECO:0000305"
FT CONFLICT 719
FT /note="D -> Y (in Ref. 1; AAC28338/AAD28247)"
FT /evidence="ECO:0000305"
FT CONFLICT 820
FT /note="S -> N (in Ref. 1; AAC28338/AAD28247)"
FT /evidence="ECO:0000305"
FT CONFLICT 825
FT /note="L -> P (in Ref. 1; AAC28338/AAD28247)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 876 AA; 96469 MW; 3607846F5AACE546 CRC64;
MNPFSSGTRL RDMIRAIRAC KTAAEERAVV RKECADIRAL INEDDPHDRH RNLAKLMFIH
MLGYPTHFGQ MECLKLIASP GFPEKRIGYL GLMLLLDERQ EVLMLVTNSL KQDLNHSNQY
VVGLALCALG NICSAEMARD LAPEVERLIQ FRDPNIRKKA ALCSTRIIRK VPDLAENFVN
AAASLLKEKH HGVLITGVQL CYELCTINDE ALEYFRTKCT EGLIKTLRDI TNSAYQPEYD
VAGITDPFLH IRLLRLLRVL GQGDADASDL MTDILAQVAT KTESNKNAGN AVLYECVETI
MAIEDTNSLR VLAINILGRF LSNRDNNIRY VALNMLMKAI TFDDQAVQRH RVTILECVKD
PDASIRKRAL ELVTLLVNEN NVTQLTKELI DYLEISDEDF KEDLSAKICF IVEKFSPEKL
WYIDQMLKVL CEAGKFVKDD VWHALIVVIS NASELHGYTV RALYKSVLTY SEQETLVRVA
VWCIGEYGDL LVNNVGMLGI EDPITVTESD AVDVIEDAIT RHNSDSTTKA MALVALLKLS
SRFPSISERI KDIIVKQKGS LLLEMQQRAI EYNSIVDRHK NIRSSLVDRM PVLDEATFNV
RRAGSFPASV STMAKPSVSL QNGVEKLPVA PLVDLLDLDS DDIMAAPSPS GTDFLQDLLG
VDLGSSSAQY GATQAPKAGT DLLLDILSIG TPSPAQNSTS SIGLLSIADV NNNPSIALDT
LSSPAPPHVA TTSSTGMFDL LDGLSPSPSK EATNGPAYAP IVAYESSSLK IEFTFSKTPG
NLQTTNVQAT FTNLSPNTFT DFIFQAAVPK FLQLHLDPAS SNTLLASGSG AITQNLRVTN
SQQGKKSLVM RMRIGYKLNG KDVLEEGQVS NFPRGL
