AP3BA_ARATH
ID AP3BA_ARATH Reviewed; 987 AA.
AC Q9M2T1; Q93YS9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=AP3-complex subunit beta-A;
DE AltName: Full=Adaptor protein complex AP-3 subunit beta-A;
DE AltName: Full=Adaptor-related protein complex 3 subunit beta-A;
DE AltName: Full=Beta-3B-adaptin;
DE AltName: Full=Clathrin assembly protein complex 3 beta-A large chain;
DE AltName: Full=Protein-affected trafficking 2;
GN Name=AP3BA; Synonyms=PAT2; OrderedLocusNames=At3g55480;
GN ORFNames=T22E16.140;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
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 [4]
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 [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=19884248; DOI=10.1093/pcp/pcp137;
RA Niihama M., Takemoto N., Hashiguchi Y., Tasaka M., Morita M.T.;
RT "ZIP genes encode proteins involved in membrane trafficking of the TGN-
RT PVC/vacuoles.";
RL Plant Cell Physiol. 50:2057-2068(2009).
RN [6]
RP MUTANT PAT2, DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20729380; DOI=10.1105/tpc.110.075424;
RA Feraru E., Paciorek T., Feraru M.I., Zwiewka M., De Groodt R., De Rycke R.,
RA Kleine-Vehn J., Friml J.;
RT "The AP-3 beta adaptin mediates the biogenesis and function of lytic
RT vacuoles in Arabidopsis.";
RL Plant Cell 22:2812-2824(2010).
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, AND COMPONENT OF THE AP-3 COMPLEX.
RX PubMed=21670741; DOI=10.1038/cr.2011.99;
RA Zwiewka M., Feraru E., Moeller B., Hwang I., Feraru M.I., Kleine-Vehn J.,
RA Weijers D., Friml J.;
RT "The AP-3 adaptor complex is required for vacuolar function in
RT Arabidopsis.";
RL Cell Res. 21:1711-1722(2011).
CC -!- FUNCTION: Part of the AP-3 complex, an adaptor-related complex which
CC seems to be clathrin-associated. The complex is associated with the
CC Golgi region as well as more peripheral structures. It facilitates the
CC budding of vesicles from the Golgi membrane and may be directly
CC involved in trafficking to the vacuole. It also function in maintaining
CC the identity of lytic vacuoles and in regulating the transition between
CC storage and lytic vacuoles. {ECO:0000269|PubMed:20729380,
CC ECO:0000269|PubMed:21670741}.
CC -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is a heterotetramer composed
CC of two large adaptins (delta-type subunit and beta-type subunit), a
CC medium adaptin (mu-type subunit) and a small adaptin (sigma-type
CC subunit).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20729380}. Golgi
CC apparatus {ECO:0000269|PubMed:20729380}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:20729380}; Peripheral membrane protein
CC {ECO:0000269|PubMed:20729380}; Cytoplasmic side
CC {ECO:0000269|PubMed:20729380}. Note=Component of the coat surrounding
CC the cytoplasmic face of coated vesicles located at the Golgi complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9M2T1-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: No obvious phenotype except defective lytic
CC vacuoles with altered morphology and accumulation of proteins.
CC {ECO:0000269|PubMed:19884248, ECO:0000269|PubMed:20729380,
CC ECO:0000269|PubMed:21670741}.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB75906.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL132975; CAB75906.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79390.1; -; Genomic_DNA.
DR EMBL; AY059780; AAL24128.1; -; mRNA.
DR PIR; T47687; T47687.
DR RefSeq; NP_567022.1; NM_115406.5. [Q9M2T1-1]
DR AlphaFoldDB; Q9M2T1; -.
DR SMR; Q9M2T1; -.
DR BioGRID; 10030; 2.
DR STRING; 3702.AT3G55480.2; -.
DR PaxDb; Q9M2T1; -.
DR EnsemblPlants; AT3G55480.1; AT3G55480.1; AT3G55480. [Q9M2T1-1]
DR GeneID; 824714; -.
DR Gramene; AT3G55480.1; AT3G55480.1; AT3G55480. [Q9M2T1-1]
DR KEGG; ath:AT3G55480; -.
DR Araport; AT3G55480; -.
DR eggNOG; KOG1060; Eukaryota.
DR InParanoid; Q9M2T1; -.
DR PhylomeDB; Q9M2T1; -.
DR PRO; PR:Q9M2T1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2T1; baseline and differential.
DR Genevisible; Q9M2T1; AT.
DR GO; GO:0030123; C:AP-3 adaptor complex; IEA:InterPro.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR026740; AP3_beta.
DR InterPro; IPR029390; AP3B_C.
DR InterPro; IPR026739; AP_beta.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR PANTHER; PTHR11134; PTHR11134; 1.
DR PANTHER; PTHR11134:SF1; PTHR11134:SF1; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF14796; AP3B1_C; 1.
DR SMART; SM01355; AP3B1_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Golgi apparatus;
KW Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1..987
FT /note="AP3-complex subunit beta-A"
FT /id="PRO_0000397851"
FT REGION 586..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 398
FT /note="H -> R (in Ref. 3; AAL24128)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="E -> G (in Ref. 3; AAL24128)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 987 AA; 108650 MW; AFFB1BC0099AD86D CRC64;
MAGIRLHVIA PLALAAVSKC ARDPAVYVRR CAANALPKLH DLRLEEHASA IEELVGILLN
DHSPGVVGAA AAAFTSICPN NFKLIGKNYK KLCQILPDVE EWGQILLIGT LLRYVVARHG
LVRESLMLSI HGTNSNGFCE KDGLGRDLTL DKEDGGKSDS FDVNLVSLVS KCYIQGPDEY
LSRSSCTDTV SSAFDTKETT SIAHNEDVKI LLQCTSPLLW SNNSAVVLAA AGVQWIMAPL
EDVKKIVKPL LFLLRSSSAS KYVVLCNILV FAKAVPSLFA PHFENFFICS SDAYQVKAYK
LEMLSLIATT SSIASILREF EDYIKDPDRR FAADTVAAIG LCAKRLMTIP TTCLDGLLAL
VRQESFAGDF ESADGEAGVL VQAVMSIQTM IERDPLRHEK VLIQLFRSLD SIKVAAARAT
IIWMVGVYCS LGHIIPRMLT TITKYLAWSF KSEASETKLQ ILNTIAKVLI SAEAGDFHML
KRIVVYVFEL GEYDLSYDIR DRTRFLKKLL SCKLASHEPA EDSVASQENI AAHVVEHVFG
RKLKSVSPIT LHNRFYLPGS LSQIVLHAAP GYEPLPKPCS FVYEEQDQLS DLDKQREAAA
DLDGSEESSE TGDENGSSDY DSESSNGSDF SSEGDERTVS NDANDPAAPL IQISETSVSA
DQEELRSRRA LDLWLDDQPS TSNQTPSALN SNQSSYAKIS IGDVGSRVKP KSYSLVDPGN
GSGLKVDYAF LSEVSNVSPL HVCVEVLFEN SSAEPILEVN LEDEESMKVA DSSEQTLVGK
ANASYNNIPT LIPMEEISCL EPHQSTKRLI QVRFHHHLLP MRLTLHYNEK KVPVKLRPDL
GYLVKPFSMS IEEFLATESR LPGMFEYSRR CTFDDHVKDS RTENGKDKFL SICESITLKV
LSNSNLHLVS VDLPVANSLE DATGLRLRFS SKILSSEIPL LITITVEGKC TEVLNLTVKI
NCEETVFGLN LLNRIANFMV EPSSSAT
