ID   APBLA_ARATH             Reviewed;         841 AA.
AC   Q9LDK9;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Beta-adaptin-like protein A;
DE            Short=At-bA-Ad;
DE            Short=At-betaA-Ad;
DE   AltName: Full=AP complex subunit beta-A;
DE   AltName: Full=Adaptor protein complex AP subunit beta-A;
DE   AltName: Full=Beta-adaptin A;
DE   AltName: Full=Clathrin assembly protein complex beta large chain A;
GN   Name=BETAA-AD; OrderedLocusNames=At5g11490; ORFNames=F15N18.80;
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 [MRNA].
RC   STRAIN=cv. Columbia;
RA   Holstein S.E.H., Happel N.;
RT   "Isolation of clathrin-coated vesicle beta-adaptin homologs from
RT   Arabidopsis thaliana.";
RL   (er) Plant Gene Register PGR00-028(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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   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   INTERACTION WITH AHK2.
RX   PubMed=18642946; DOI=10.1021/pr0703831;
RA   Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T., Heyl A.;
RT   "Toward an interaction map of the two-component signaling pathway of
RT   Arabidopsis thaliana.";
RL   J. Proteome Res. 7:3649-3660(2008).
CC   -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex that
CC       plays a role in protein sorting in the late-Golgi/trans-Golgi network
CC       (TGN) and/or endosomes. The AP complexes mediate both the recruitment
CC       of clathrin to membranes and the recognition of sorting signals within
CC       the cytosolic tails of transmembrane cargo molecules (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Adaptor protein complexes are heterotetramers composed of two
CC       large adaptins (beta-type subunit and alpha-type or delta-type or
CC       epsilon-type or gamma-type subunit), a medium adaptin (mu-type subunit)
CC       and a small adaptin (sigma-type subunit) (By similarity). Interacts
CC       with AHK2. {ECO:0000250, ECO:0000269|PubMed:18642946}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Golgi apparatus,
CC       trans-Golgi network {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated
CC       vesicle membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Associated with the
CC       trans-Golgi network. Component of the coat surrounding the cytoplasmic
CC       face of coated vesicles located at the Golgi complex (By similarity).
CC       {ECO:0000250}.
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=Q9LDK9-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AF216385; AAF61671.1; -; mRNA.
DR   EMBL; AL163815; CAB87709.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91685.1; -; Genomic_DNA.
DR   PIR; T48508; T48508.
DR   RefSeq; NP_196710.1; NM_121187.4. [Q9LDK9-1]
DR   AlphaFoldDB; Q9LDK9; -.
DR   SMR; Q9LDK9; -.
DR   BioGRID; 16299; 2.
DR   IntAct; Q9LDK9; 1.
DR   STRING; 3702.AT5G11490.2; -.
DR   iPTMnet; Q9LDK9; -.
DR   PaxDb; Q9LDK9; -.
DR   PRIDE; Q9LDK9; -.
DR   ProteomicsDB; 244423; -. [Q9LDK9-1]
DR   EnsemblPlants; AT5G11490.1; AT5G11490.1; AT5G11490. [Q9LDK9-1]
DR   GeneID; 831021; -.
DR   Gramene; AT5G11490.1; AT5G11490.1; AT5G11490. [Q9LDK9-1]
DR   KEGG; ath:AT5G11490; -.
DR   Araport; AT5G11490; -.
DR   eggNOG; KOG1061; Eukaryota.
DR   HOGENOM; CLU_006320_4_5_1; -.
DR   InParanoid; Q9LDK9; -.
DR   OMA; ANCMHAL; -.
DR   PhylomeDB; Q9LDK9; -.
DR   PRO; PR:Q9LDK9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LDK9; baseline and differential.
DR   Genevisible; Q9LDK9; AT.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR   GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
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   Gene3D; 3.30.310.10; -; 1.
DR   InterPro; IPR026739; AP_beta.
DR   InterPro; IPR016342; AP_complex_bsu_1_2_4.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR015151; B-adaptin_app_sub_C.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR012295; TBP_dom_sf.
DR   PANTHER; PTHR11134; PTHR11134; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF09066; B2-adapt-app_C; 1.
DR   PIRSF; PIRSF002291; AP_complex_beta; 1.
DR   SMART; SM01020; B2-adapt-app_C; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..841
FT                   /note="Beta-adaptin-like protein A"
FT                   /id="PRO_0000397848"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          650..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        655..671
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   841 AA;  93266 MW;  89906E3AB705711C CRC64;
     MAPPAASQRY PSPSQPSGKS EVSDLKTQLR QLAGSRAPGV DDSKRDLYKK VISYMTIGID
     VSSVFGEMVM CSATSDIVLK KMCYLYVGNY AKGNPDLSLL TINFLQRDCK DEDPMIRGLA
     LRSLCSLRVP NLVEYLVGPL GSGLKDNNSY VRTIAVTGVL KLYHISPSTC IDADFPATLK
     SLMLHDSDAQ VVANCLSALQ EIWSLEASHS EEACREKESL LSKPVIYYFL NRIKEFNEWA
     QCLILELAVK YVPSDSNDIF DIMNLLEDRL QHANGAVVLA TVKVFLQLTL SMTDVHQQVY
     ERIKSPLLTL VSSGSPEQSY AILSHLHLLV VRAPFIFAAD YKHFYCQYNE PSYVKKLKLE
     MLTAVANESN TYEIVTELCE YAANVDIAIA RESIRAVGKI ALQQYDVNAI VDRLLQFLEM
     EKDYVTAETL VLVKDLLRKY PQWSHDCISV VGGISSKNIQ EPKAKAALIW MLGEYAQDMS
     DAPYVLENLI ENWEEEHSAE VRLHLLTAAM KCFFKRAPET QKALGTALAA GIADFHQDVH
     DRALFYYRVL QYDVHVAERV VSPPKQAVSV FADTQSSEIK DRVFDEFNSL SVIYQKPSYM
     FTDKEHRGPF EFSDEVGNIS ITPEASSDIV PAQQYEANDK DLLLGIDEKD ENKGVSNNNG
     SAYTAPSLES SSNITSQMQE LAISGPATSA TTPQSFGFDD LFGLGLSTAP APTPSPPLLK
     LNARAALDPG AFQQKWRQLP ISLTQECSVN PQGIAALTVP QSLIKHMQSH SIHCIASGGQ
     SPNFKFFFFA QKESEPSNYL TECIINTSSA KAQIKVKADE QSTCQAFTTV FETALSKFGM
     P