ID A0A0S3R304_PHAAN Unreviewed; 653 AA.
AC A0A0S3R304;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Auxin efflux carrier component {ECO:0000256|RuleBase:RU362108};
GN Name=Vigan.01G269800 {ECO:0000313|EMBL:BAT74919.1};
GN ORFNames=VIGAN_01269800 {ECO:0000313|EMBL:BAT74919.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT74919.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT74919.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
CC -!- FUNCTION: May act as a component of the auxin efflux carrier.
CC {ECO:0000256|RuleBase:RU362108}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362108}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362108}.
CC -!- SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.1) family.
CC {ECO:0000256|ARBA:ARBA00009177, ECO:0000256|RuleBase:RU362108}.
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DR EMBL; AP015034; BAT74919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3R304; -.
DR Proteomes; UP000291084; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0060918; P:auxin transport; IEA:UniProt.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-UniRule.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR InterPro; IPR014024; Auxin_eff_plant.
DR InterPro; IPR004776; Mem_transp_PIN-like.
DR NCBIfam; TIGR00946; 2a69; 1.
DR PANTHER; PTHR31752; AUXIN EFFLUX CARRIER COMPONENT 1B-RELATED; 1.
DR PANTHER; PTHR31752:SF18; AUXIN EFFLUX CARRIER COMPONENT 4; 1.
DR Pfam; PF03547; Mem_trans; 1.
PE 3: Inferred from homology;
KW Auxin signaling pathway {ECO:0000256|ARBA:ARBA00023294,
KW ECO:0000256|RuleBase:RU362108};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362108};
KW Reference proteome {ECO:0000313|Proteomes:UP000291084};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362108};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362108}; Transport {ECO:0000256|RuleBase:RU362108}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT TRANSMEM 40..59
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT TRANSMEM 71..92
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT TRANSMEM 104..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT TRANSMEM 511..528
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT TRANSMEM 540..559
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT TRANSMEM 571..593
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT TRANSMEM 626..650
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT REGION 275..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 653 AA; 70761 MW; 3AAD91329476FC0B CRC64;
MISWTDLYTV LTAVIPLYVA MILAYGSVRW WKIFSPDQCS GINRFVAIFA VPLLSFHFIS
SNNPYAMNFR FIAADTLQKI IMLFALAIWT NFTANGSLEW MITIFSLSTL PNTLVMGIPL
LIAMYGDYSG QLMVQVVVLQ CIIWYTLLLF LFEYRGAKLL IMEQFPETAA SIVSFKVDSD
VVSLDGRDFL ETDAEVGDDG KLHVTVRKSN ASRRSFMMTP RPSNLTGAEI YSLSSSRNPT
PRGSNFNHAD FYSMMGYAPR HSNFGAADLY SVQSTSRGVT PRPSNFEENS APAPQAISSP
RFGFYPAVQT VPSAYPAPNP EFSSGLTKSV SKNSQTQPQP QSQPQAPAQA PQVAQPPNSS
SKASHDAKEL HMFVWSSSAS PVSEAGGLHV FSGADFGASD QSGRSDQGAK EIRMLVADEH
PQNGEANKAT AEGEFRGEDL KFPGKEGEQA EEEAEKAGAA GPNKLGSSST AELHPKSGVG
VAGKHMPPAS VMTRLILIMV WRKLIRNPNT YSSLIGVIWS LVAFRWHVHM PKIIEKSISI
LSDAGLGMAM FSLGLFMALQ PNIIACGNSV ATFAMAVRFL TGPAVMAAAS IAVGLRGTLL
RVAIVQAALP QGIVPFVFAK EYNVHPAILS TGVIFGMLIA LPITLVYYIL LGL
//
