AP4M_ARATH
ID AP4M_ARATH Reviewed; 451 AA.
AC Q9SB50;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=AP-4 complex subunit mu;
DE AltName: Full=Adaptor protein complex AP-4 subunit mu;
DE AltName: Full=Adaptor protein-4 mu-adaptin;
DE AltName: Full=Adaptor-related protein complex 4 subunit mu;
DE AltName: Full=At-muC-Ad;
DE AltName: Full=Mu4-adaptin;
GN Name=AP4M; Synonyms=CLH; OrderedLocusNames=At4g24550; ORFNames=F22K18.250;
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=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 [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 GENE FAMILY.
RX PubMed=14871308; DOI=10.1111/j.1365-313x.2003.01995.x;
RA Happel N., Hoening S., Neuhaus J.M., Paris N., Robinson D.G.,
RA Holstein S.E.;
RT "Arabidopsis muA-adaptin interacts with the tyrosine motif of the vacuolar
RT sorting receptor VSR-PS1.";
RL Plant J. 37:678-693(2004).
CC -!- FUNCTION: Subunit of novel type of clathrin- or non-clathrin-associated
CC protein coat involved in targeting proteins from the trans-Golgi
CC network (TGN) to the endosomal-lysosomal system. {ECO:0000250}.
CC -!- SUBUNIT: Adaptor protein complex 4 (AP-4) is a heterotetramer composed
CC of two large adaptins (epsilon-type subunit and beta-type subunit), a
CC medium adaptin (mu-type subunit) and a small adaptin (sigma-type
CC subunit). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000250}. Membrane, coated pit {ECO:0000250}. Note=Associated with
CC the trans-Golgi network. {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=Q9SB50-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the adaptor complexes medium subunit family.
CC {ECO:0000305}.
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DR EMBL; AL035356; CAA23008.1; -; Genomic_DNA.
DR EMBL; AL161561; CAB79365.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84924.1; -; Genomic_DNA.
DR EMBL; AY072171; AAL59993.1; -; mRNA.
DR PIR; T05579; T05579.
DR RefSeq; NP_194186.1; NM_118588.7. [Q9SB50-1]
DR AlphaFoldDB; Q9SB50; -.
DR SMR; Q9SB50; -.
DR STRING; 3702.AT4G24550.2; -.
DR iPTMnet; Q9SB50; -.
DR PaxDb; Q9SB50; -.
DR PRIDE; Q9SB50; -.
DR ProMEX; Q9SB50; -.
DR ProteomicsDB; 224555; -. [Q9SB50-1]
DR EnsemblPlants; AT4G24550.2; AT4G24550.2; AT4G24550. [Q9SB50-1]
DR GeneID; 828557; -.
DR Gramene; AT4G24550.2; AT4G24550.2; AT4G24550. [Q9SB50-1]
DR KEGG; ath:AT4G24550; -.
DR Araport; AT4G24550; -.
DR TAIR; locus:2121944; AT4G24550.
DR eggNOG; KOG0937; Eukaryota.
DR HOGENOM; CLU_026996_5_2_1; -.
DR InParanoid; Q9SB50; -.
DR OMA; NVCATIP; -.
DR PhylomeDB; Q9SB50; -.
DR PRO; PR:Q9SB50; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SB50; baseline and differential.
DR Genevisible; Q9SB50; AT.
DR GO; GO:0030124; C:AP-4 adaptor complex; IPI:TAIR.
DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0090160; P:Golgi to lysosome transport; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR001392; Clathrin_mu.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR028565; MHD.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR PIRSF; PIRSF005992; Clathrin_mu; 1.
DR PRINTS; PR00314; CLATHRINADPT.
DR SUPFAM; SSF49447; SSF49447; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS51072; MHD; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coated pit; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..451
FT /note="AP-4 complex subunit mu"
FT /id="PRO_0000424264"
FT DOMAIN 184..450
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
SQ SEQUENCE 451 AA; 50946 MW; C0981463B622AD36 CRC64;
MMISQFFVLS QRGDNIVFRD YRAEVPKGST ETFFRKVKFW KEDGNAEAPP IFNVDGVNYF
HVKVVGLYFV ATTRVNVSPS LVLELLQRIA RVIKDYLGVL NEDSFRKNFV LVYELLDEVI
DFGYVQTTST EVLKSYIFNE PIVVSPARLQ PIDPAAIFTQ GAKRMPGTAV TKSVVANDPG
GRRREEIFVD IIEKISVTFS SSGYILTSEI DGTIQMKSYL SGNPEIRLAL NEDLNIGRGG
RSVYDYRSSS GSGVILDDCN FHESVRLDSF DSDRTLSLVP PDGEFPVMNY RMTQEFKPPF
HVNTLIEEAG RLKAEVIIKI RAEFPSDIIA NTITVQMPLP NYTSRASFEL EPGAAGQRTD
FKESNKMLEW NLKKIVGGGE HTLRAKLTFS QEFHGNITKE AGPVSMTFTI PMYNVSKLQV
KYLQIAKKSS SYNPYRWVRY VTQANSYVAR I