AUXI1_ARATH
ID AUXI1_ARATH Reviewed; 904 AA.
AC Q9SU08; Q8RXD0;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Auxilin-related protein 1 {ECO:0000305};
DE AltName: Full=Auxilin-like protein 1 {ECO:0000303|PubMed:11701884};
GN Name=AUXI1 {ECO:0000305};
GN OrderedLocusNames=At4g12780 {ECO:0000312|Araport:AT4G12780};
GN ORFNames=T20K18.130 {ECO:0000312|EMBL:CAB40995.1};
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] OF 397-904.
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 INTERACTION WITH SH3P1, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11701884; DOI=10.2307/3871590;
RA Lam B.C.-H., Sage T.L., Bianchi F., Blumwald E.;
RT "Role of SH3 domain-containing proteins in clathrin-mediated vesicle
RT trafficking in Arabidopsis.";
RL Plant Cell 13:2499-2512(2001).
CC -!- FUNCTION: Promotes uncoating of clathrin-coated vesicles. May interact
CC directly with clathrin. {ECO:0000269|PubMed:11701884}.
CC -!- SUBUNIT: Interacts with SH3P1. {ECO:0000269|PubMed:11701884}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11701884};
CC Peripheral membrane protein {ECO:0000269|PubMed:11701884}. Golgi
CC apparatus, trans-Golgi network {ECO:0000269|PubMed:11701884}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:11701884}. Cytoplasmic
CC vesicle {ECO:0000269|PubMed:11701884}.
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=Q9SU08-1; Sequence=Displayed;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL91223.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB40995.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78320.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049640; CAB40995.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161534; CAB78320.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83179.1; -; Genomic_DNA.
DR EMBL; AY081334; AAL91223.1; ALT_INIT; mRNA.
DR EMBL; BT009679; AAP81797.1; -; mRNA.
DR PIR; T06636; T06636.
DR RefSeq; NP_193014.5; NM_117347.7. [Q9SU08-1]
DR AlphaFoldDB; Q9SU08; -.
DR SMR; Q9SU08; -.
DR BioGRID; 12187; 3.
DR STRING; 3702.AT4G12780.1; -.
DR iPTMnet; Q9SU08; -.
DR PaxDb; Q9SU08; -.
DR PRIDE; Q9SU08; -.
DR EnsemblPlants; AT4G12780.1; AT4G12780.1; AT4G12780. [Q9SU08-1]
DR GeneID; 826890; -.
DR Gramene; AT4G12780.1; AT4G12780.1; AT4G12780. [Q9SU08-1]
DR KEGG; ath:AT4G12780; -.
DR Araport; AT4G12780; -.
DR TAIR; locus:2135778; AT4G12780.
DR eggNOG; KOG0431; Eukaryota.
DR InParanoid; Q9SU08; -.
DR OrthoDB; 319959at2759; -.
DR PhylomeDB; Q9SU08; -.
DR PRO; PR:Q9SU08; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SU08; baseline and differential.
DR Genevisible; Q9SU08; AT.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0072318; P:clathrin coat disassembly; IBA:GO_Central.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IPI:TAIR.
DR GO; GO:1900186; P:negative regulation of clathrin-dependent endocytosis; IDA:TAIR.
DR GO; GO:0045806; P:negative regulation of endocytosis; IDA:TAIR.
DR GO; GO:0045926; P:negative regulation of growth; IDA:TAIR.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR036869; J_dom_sf.
DR SUPFAM; SSF46565; SSF46565; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Chaperone; Coiled coil;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW Reference proteome.
FT CHAIN 1..904
FT /note="Auxilin-related protein 1"
FT /id="PRO_0000395459"
FT DOMAIN 619..640
FT /note="R"
FT DOMAIN 839..904
FT /note="J"
FT REGION 46..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 456..663
FT /evidence="ECO:0000255"
FT COILED 762..804
FT /evidence="ECO:0000255"
FT COMPBIAS 55..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 904 AA; 99853 MW; 98AB9B88A7F0B808 CRC64;
MDDFTGLLAR DFGLKPQGKS APMASQSNSS AADFNTFASS YSFATAAGKK SDSLPVFDDP
GRDGDDLLFK DVFSGPPPPK YGSSSGDSRS PSAPAFDYDA MFKEPKSKSA SSMPVYDKPV
YDDEDVFESI PELKIPSTSS QSARFENVFS SISSSPTKHR KQNSSPFDDL MGNNLGKKGA
DSDREEKGSS IFDDLIPGFG RTSSPPSKRT TSETTNQSEK APYRTAETSS NVEEDPFVVL
EESESTPREP SRTDPLDDIG KFNSRKTDHS SVHGGVFVDI DPLDNLGKPG PDMNSKGKSH
LRPPGNISGS QSPPVESPGS YHSKKVSFED FLEPHNMSTP PPTNSNGSFE SSDDVWLTVS
EIPLFTQPTS APPPTRPPPP RPTRPIKKKV NEPSIPTSAY HSHVPSSGRA SVNSPTASQM
DELDDFSIGR NQTAANGYPD PSSGEDSDVF STAAASAAAM KDAMDKAEAK FRHAKERREK
ENLKASRSRE GDHTENYDSR ERELREKQVR LDRERAEREA EMEKAQEREK EEREREQKRI
ERERERLVAR QAVERATREA RERAATEAHA KVQRAAVGKA TDARERAERA AVQRAHAEAR
ERAAAGARDK AAKAAAEARE KAEKAAAEAK ERANAEAREK ETRVRAERAA VERAAAEARG
RAAAQAKAKQ QQENTNDLDS FFSSISRPNS APRQRTNPLD PFQDSWNKGG SFESSRESLR
VPPGQPENLR KTSSVTNIVD DLSSIFGASA SQSGGFQDVD GETEERRRAR LERHQRTQER
AAKALAEKNE RDLQVQREQV EKDRIGVTLD VEIKRWGAGK EGNLRALLST LQYVLWPECG
WQPVSLTDLI TAASVKKVYR KATLCIHPDK VQQKGANLQQ KYIAEKVFDM LKEAWNKFNS
EELF
