APBLB_ARATH
ID APBLB_ARATH Reviewed; 894 AA.
AC Q9SUS3; Q9M650;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Beta-adaptin-like protein B;
DE Short=At-bB-Ad;
DE Short=At-betaB-Ad;
DE AltName: Full=AP complex subunit beta-B;
DE AltName: Full=Adaptor protein complex AP subunit beta-B;
DE AltName: Full=Beta-adaptin B;
DE AltName: Full=Clathrin assembly protein complex beta large chain B;
GN Name=BETAB-AD; OrderedLocusNames=At4g11380; ORFNames=F8L21.170;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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 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).
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=Q9SUS3-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; AF216386; AAF61672.1; -; mRNA.
DR EMBL; AL096882; CAB51422.1; -; Genomic_DNA.
DR EMBL; AL161531; CAB81239.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83003.1; -; Genomic_DNA.
DR EMBL; AY093155; AAM13154.1; -; mRNA.
DR EMBL; BT010362; AAQ56805.1; -; mRNA.
DR EMBL; AK227093; BAE99145.1; -; mRNA.
DR PIR; T13029; T13029.
DR RefSeq; NP_192877.1; NM_117209.5. [Q9SUS3-1]
DR AlphaFoldDB; Q9SUS3; -.
DR SMR; Q9SUS3; -.
DR BioGRID; 12040; 18.
DR STRING; 3702.AT4G11380.2; -.
DR iPTMnet; Q9SUS3; -.
DR PaxDb; Q9SUS3; -.
DR PRIDE; Q9SUS3; -.
DR EnsemblPlants; AT4G11380.1; AT4G11380.1; AT4G11380. [Q9SUS3-1]
DR GeneID; 826741; -.
DR Gramene; AT4G11380.1; AT4G11380.1; AT4G11380. [Q9SUS3-1]
DR KEGG; ath:AT4G11380; -.
DR Araport; AT4G11380; -.
DR eggNOG; KOG1061; Eukaryota.
DR HOGENOM; CLU_006320_2_1_1; -.
DR InParanoid; Q9SUS3; -.
DR OMA; NPPEVQW; -.
DR PhylomeDB; Q9SUS3; -.
DR PRO; PR:Q9SUS3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUS3; baseline and differential.
DR Genevisible; Q9SUS3; 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: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; 2.60.40.1150; -; 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; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR013037; Clathrin_b-adaptin_app_Ig-like.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR11134; PTHR11134; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR Pfam; PF09066; B2-adapt-app_C; 1.
DR PIRSF; PIRSF002291; AP_complex_beta; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SMART; SM01020; B2-adapt-app_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..894
FT /note="Beta-adaptin-like protein B"
FT /id="PRO_0000397849"
FT REGION 597..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..637
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 604
FT /note="A -> R (in Ref. 1; AAF61672)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 894 AA; 99372 MW; 469B8650F370CBCF CRC64;
MSGHDSKYFS TTKKGEIPEL KEELNSQYKD KRKDAVKKVI AAMTVGKDVS SLFTDVVNCM
QTENLELKKL VYLYLINYAK SQPDLAILAV NTFVKDSQDP NPLIRALAVR TMGCIRVDKI
TEYLCDPLQK CLKDDDPYVR KTAAICVAKL FDINAELVED RGFLEALKDL ISDNNPMVVA
NAVAALAEIQ ENSSSPIFEI NSTTLTKLLT ALNECTEWGQ VFILDALSKY KAADPREAEN
IVERVTPRLQ HANCAVVLSA VKMILQQMEL ITSTDVIRNL CKKMAPPLVT LLSAEPEIQY
VALRNINLIV QKRPTILAHE IKVFFCKYND PIYVKMEKLE IMIKLASDRN IDQVLLEFKE
YATEVDVDFV RKAVRAIGRC AIKLERAAER CISVLLELIK IKVNYVVQEA IIVIKDIFRR
YPNTYESIIA TLCESLDTLD EPEAKASMIW IIGEYAERID NADELLESFL ENFPEEPAQV
QLQLLTATVK LFLKKPTEGP QQMIQVVLNN ATVETDNPDL RDRAYIYWRL LSTDPEAAKD
VVLAEKPVIS DDSNQLDPSL LDELLTNIST LSSVYHKPPE AFVTRLKTTV QKTEDEDFAE
GSEAGYSSSN PVDSAASPPG NIPQPSGRQP APAVPAPVPD LLGDLMGLDN AAIVPVDDPI
TQSGPPLPVV VPASSGQGLQ ISAQLSRKDG QVFYSMLFEN NSQSVLDGFM IQFNKNTFGL
AAAGSLQIPP LHPATSARTM LPMVLFQNMS AGPPSSLLQV AVKNNQQPVW YFTDKIILHA
LFGEDGRMER GTFLETWRSL PDSNEVLKEF PGITITSVES TIELLTAFNM FFIAKRKNGN
QDVIYLSAKD PRDVPFLIEL TAMVGQPGLK CAVKTPTPEI APLFFEALEL LFKA
