AXR4_ARATH
ID AXR4_ARATH Reviewed; 473 AA.
AC Q9FZ33; Q944Q7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Protein AUXIN RESPONSE 4;
GN Name=AXR4; OrderedLocusNames=At1g54990; ORFNames=F14C21.51, T24C10.10;
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=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 FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16690816; DOI=10.1126/science.1122847;
RA Dharmasiri S., Swarup R., Mockaitis K., Dharmasiri N., Singh S.K.,
RA Kowalchyk M., Marchant A., Mills S., Sandberg G., Bennett M.J., Estelle M.;
RT "AXR4 is required for localization of the auxin influx facilitator AUX1.";
RL Science 312:1218-1220(2006).
CC -!- FUNCTION: Required for the auxin influx facilitator AUX1 polar
CC trafficking and its asymmetric localization within the plasma membrane.
CC Not involved in the PIN proteins localization.
CC {ECO:0000269|PubMed:16690816}.
CC -!- INTERACTION:
CC Q9FZ33; Q96247: AUX1; NbExp=5; IntAct=EBI-25514394, EBI-16935343;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16690816}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16690816}.
CC -!- TISSUE SPECIFICITY: Most abundant in root tissue, lesser amounts in
CC rosette leaves, stems and flowers and very little in mature siliques.
CC {ECO:0000269|PubMed:16690816}.
CC -!- DISRUPTION PHENOTYPE: Plants show reduced gravitropism, auxin-resistant
CC root growth and AUX1 accumulation in the endoplasmic reticulum.
CC {ECO:0000269|PubMed:16690816}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL11602.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC064840; AAG00878.1; -; Genomic_DNA.
DR EMBL; AC069144; AAG51115.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33170.1; -; Genomic_DNA.
DR EMBL; AY074334; AAL67030.1; -; mRNA.
DR EMBL; AY122984; AAM67517.1; -; mRNA.
DR EMBL; AF424608; AAL11602.1; ALT_INIT; mRNA.
DR PIR; D96591; D96591.
DR RefSeq; NP_564672.2; NM_104373.2.
DR AlphaFoldDB; Q9FZ33; -.
DR BioGRID; 27166; 2.
DR IntAct; Q9FZ33; 3.
DR STRING; 3702.AT1G54990.1; -.
DR ESTHER; arath-AXR4; 6_AlphaBeta_hydrolase.
DR PaxDb; Q9FZ33; -.
DR PRIDE; Q9FZ33; -.
DR ProteomicsDB; 240942; -.
DR EnsemblPlants; AT1G54990.1; AT1G54990.1; AT1G54990.
DR GeneID; 841941; -.
DR Gramene; AT1G54990.1; AT1G54990.1; AT1G54990.
DR KEGG; ath:AT1G54990; -.
DR Araport; AT1G54990; -.
DR TAIR; locus:2011000; AT1G54990.
DR eggNOG; ENOG502QUCP; Eukaryota.
DR HOGENOM; CLU_039117_0_0_1; -.
DR InParanoid; Q9FZ33; -.
DR OMA; DIAEWGG; -.
DR OrthoDB; 1362002at2759; -.
DR PhylomeDB; Q9FZ33; -.
DR PRO; PR:Q9FZ33; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZ33; baseline and differential.
DR Genevisible; Q9FZ33; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:TAIR.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..473
FT /note="Protein AUXIN RESPONSE 4"
FT /id="PRO_0000300097"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 119..283
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 52419 MW; D09124A11565BB23 CRC64;
MAIITEEEED PKTLNPPKNK PKDSDFTKSE STMKNPKPQS QNPFPFWFYF TVVVSLATII
FISLSLFSSQ NDPRSWFLSL PPALRQHYSN GRTIKVQVNS NESPIEVFVA ESGSIHTETV
VIVHGLGLSS FAFKEMIQSL GSKGIHSVAI DLPGNGFSDK SMVVIGGDRE IGFVARVKEV
YGLIQEKGVF WAFDQMIETG DLPYEEIIKL QNSKRRSFKA IELGSEETAR VLGQVIDTLG
LAPVHLVLHD SALGLASNWV SENWQSVRSV TLIDSSISPA LPLWVLNVPG IREILLAFSF
GFEKLVSFRC SKEMTLSDID AHRILLKGRN GREAVVASLN KLNHSFDIAQ WGNSDGINGI
PMQVIWSSEA SKEWSDEGQR VAKALPKAKF VTHSGSRWPQ ESKSGELADY ISEFVSLLPK
SIRRVAEEPI PEEVQKVLEE AKAGDDHDHH HGHGHAHAGY SDAYGLGEEW TTT
