AP180_ARATH
ID AP180_ARATH Reviewed; 653 AA.
AC Q9ZVN6;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Clathrin coat assembly protein AP180;
DE Short=At-AP180;
DE AltName: Full=Clathrin coat-associated protein AP180;
GN Name=AP180; OrderedLocusNames=At1g05020; ORFNames=T7A14.11;
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=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 [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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 FUNCTION, INTERACTION WITH ALPHAC-AD, AND MUTAGENESIS OF 442-ASP--LEU-444;
RP 473-ASP--TRP-475 AND 608-ASP--PHE-610.
RX PubMed=15054111; DOI=10.1242/jcs.01062;
RA Barth M., Holstein S.E.;
RT "Identification and functional characterization of Arabidopsis AP180, a
RT binding partner of plant alphaC-adaptin.";
RL J. Cell Sci. 117:2051-2062(2004).
CC -!- FUNCTION: Adaptins are components of the adapter complexes which link
CC clathrin to receptors in coated vesicles. Clathrin-associated protein
CC complexes are believed to interact with the cytoplasmic tails of
CC membrane proteins, leading to their selection and concentration.
CC Binding of AP180 to clathrin triskelia promotes their assembly into 70-
CC 90 nm coats cages. {ECO:0000269|PubMed:15054111}.
CC -!- SUBUNIT: Interacts with ALPHAC-AD and clathrin.
CC {ECO:0000269|PubMed:15054111}.
CC -!- INTERACTION:
CC Q9ZVN6; Q8LPK4: ALPHAC-AD; NbExp=2; IntAct=EBI-2366853, EBI-2366827;
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250}.
CC Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250}. Note=Colocalized with clathrin in the Golgi
CC area. {ECO:0000250}.
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DR EMBL; AC005322; AAC97997.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27780.1; -; Genomic_DNA.
DR EMBL; AK117462; BAC42127.1; -; mRNA.
DR EMBL; BT005184; AAO50717.1; -; mRNA.
DR PIR; B86184; B86184.
DR RefSeq; NP_563726.1; NM_100381.3.
DR AlphaFoldDB; Q9ZVN6; -.
DR SMR; Q9ZVN6; -.
DR BioGRID; 24578; 4.
DR IntAct; Q9ZVN6; 4.
DR STRING; 3702.AT1G05020.1; -.
DR PaxDb; Q9ZVN6; -.
DR PRIDE; Q9ZVN6; -.
DR ProteomicsDB; 244975; -.
DR EnsemblPlants; AT1G05020.1; AT1G05020.1; AT1G05020.
DR GeneID; 839343; -.
DR Gramene; AT1G05020.1; AT1G05020.1; AT1G05020.
DR KEGG; ath:AT1G05020; -.
DR Araport; AT1G05020; -.
DR TAIR; locus:2205558; AT1G05020.
DR eggNOG; KOG0251; Eukaryota.
DR HOGENOM; CLU_014098_4_0_1; -.
DR InParanoid; Q9ZVN6; -.
DR OMA; DQYNPFL; -.
DR OrthoDB; 553740at2759; -.
DR PhylomeDB; Q9ZVN6; -.
DR PRO; PR:Q9ZVN6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZVN6; baseline and differential.
DR Genevisible; Q9ZVN6; AT.
DR GO; GO:0005905; C:clathrin-coated pit; IBA:GO_Central.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0032050; F:clathrin heavy chain binding; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0048268; P:clathrin coat assembly; IEA:InterPro.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR Gene3D; 1.20.58.150; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR014712; ANTH_dom_sf.
DR InterPro; IPR045192; AP180-like.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR PANTHER; PTHR22951; PTHR22951; 1.
DR Pfam; PF07651; ANTH; 1.
DR SMART; SM00273; ENTH; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
PE 1: Evidence at protein level;
KW Coated pit; Cytoplasmic vesicle; Endocytosis; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..653
FT /note="Clathrin coat assembly protein AP180"
FT /id="PRO_0000187071"
FT DOMAIN 28..165
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT REGION 170..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 442..444
FT /note="Required to promote clathrin assembly"
FT MOTIF 608..610
FT /note="ALPHAC-AD binding"
FT COMPBIAS 170..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 442..444
FT /note="DLL->AAA: Loss of clathrin assembly activity, but
FT normal clathrin binding."
FT /evidence="ECO:0000269|PubMed:15054111"
FT MUTAGEN 473..475
FT /note="DPW->AAA: Normal ALPHAC-AD binding."
FT /evidence="ECO:0000269|PubMed:15054111"
FT MUTAGEN 608..610
FT /note="DPF->AAA: Loss of ALPHAC-AD binding."
FT /evidence="ECO:0000269|PubMed:15054111"
SQ SEQUENCE 653 AA; 72172 MW; 6D6B9C9DFE47850A CRC64;
MPSKLKKAIG AVKDQTSISL AKVANGATGG GDLTTLEVAI LKATSHDEEV PIDDRLVTEI
LGIISSKKSH AASCAAAIGR RIGRTRNWIV ALKSLVLVLR IFQDGDPYFP REVLHAMKRG
AKILNLSSFR DDSNSCPWDF TAFVRTFALY LDERLDCFLT GKLQRRYTNR EQTGRISTNS
TTRSRFNPKA GIKSHEPAVR DMKPVMLLDK ITYWQKLLDR AIATRPTGDA KANRLVKMSL
YAVMQESFDL YRDISDGLAL LLDSFFHLQY QSCINAFQAC VRASKQFEEL NAFYDLSKSI
GIGRTSEYPS IQKISLELLE TLQEFLKDQS SFPASSGLYP SPNSFLPPPP SSKDSAVSSS
LDFGDSTIDT SERYSDYGSF RSTSLEDLMS RTEAGTSSPP MSCHSEPYGG GRDDPNGNNF
DTVSTKSLPN NPSVSASNLI LDLLSLDDVS NTAEAEDVED KKKQDDSKAE TFDPWEALML
RDDPKKKIET IEEEPSTAED HQRDSGNWLL ALEETATQVQ GNNSMAIVPF GLDDPMPAFQ
AATDQYNPFL EEPVAQLATA GEPMITFGGL ALTGFQPEPT FQVNVPDDFE PSSTPTFKAT
ETLPMKCDPF TTFESFGFGE TFSENGGVNQ QSVLQEQQIW LQNQKKIIAK HLS
