ID A0A1S3V6I3_VIGRR Unreviewed; 491 AA.
AC A0A1S3V6I3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Auxin transporter-like protein 2 {ECO:0000313|RefSeq:XP_014513951.1};
GN Name=LOC106772219 {ECO:0000313|RefSeq:XP_014513951.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014513951.1};
RN [1] {ECO:0000313|RefSeq:XP_014513951.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014513951.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Carrier protein involved in proton-driven auxin influx.
CC Mediates the formation of auxin gradient from developing leaves (site
CC of auxin biosynthesis) to tips by contributing to the loading of auxin
CC in vascular tissues and facilitating acropetal (base to tip) auxin
CC transport within inner tissues of the root apex, and basipetal (tip to
CC base) auxin transport within outer tissues of the root apex (By
CC similarity). May be involved in lateral roots and nodules formation.
CC {ECO:0000256|ARBA:ARBA00003124}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC Amino acid/auxin permease (AAAP) (TC 2.A.18.1) subfamily.
CC {ECO:0000256|ARBA:ARBA00005590}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014513951.1; XM_014658465.2.
DR AlphaFoldDB; A0A1S3V6I3; -.
DR STRING; 3916.A0A1S3V6I3; -.
DR GeneID; 106772219; -.
DR KEGG; vra:106772219; -.
DR OrthoDB; 454873at2759; -.
DR Proteomes; UP000087766; Chromosome 8.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR013057; AA_transpt_TM.
DR PANTHER; PTHR48017:SF255; AUXIN TRANSPORTER PROTEIN 1; 1.
DR PANTHER; PTHR48017; OS05G0424000 PROTEIN-RELATED; 1.
DR Pfam; PF01490; Aa_trans; 1.
PE 3: Inferred from homology;
KW Amino-acid transport {ECO:0000256|ARBA:ARBA00022970};
KW Auxin signaling pathway {ECO:0000256|ARBA:ARBA00023294};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW Symport {ECO:0000256|ARBA:ARBA00022847};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022970}.
FT TRANSMEM 85..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 49..442
FT /note="Amino acid transporter transmembrane"
FT /evidence="ECO:0000259|Pfam:PF01490"
SQ SEQUENCE 491 AA; 55184 MW; CCB367F31C0CFF4B CRC64;
METMLPQKQA EEAIVASLNE TESEVGGVRE EEKELQDHSG FSIKNLLWHG GSVWDAWFSC
ASNQVAQVLL TLPCSFSQLG MLSGILLQIF YGIMGSWTAY LISVLYMEYR ARKEKENVSF
KNHVIQWFEV LDGLLGPYWK AVGLAFNCTF LLFGSVIQLI ACASNIYYIN DHLDKRTWTY
IFGACCATSV FIPSFHNYRI WSFLGLGMTT YTAWYLAIAA LVHGQAENVT HTGPTKLVLY
FTGATNILYT FGGHAVTVEI MHAMWKPQKF KYIYLMATLY VFTLTIPSAA AVYWAFGDEL
LNHSNAFSLL PKNGFRDTAV ILMLIHQFIT FGFACTPLYF VWEKVIGMHD TKSICLRALA
RLPVVIPIWF FAIIFPFFGP INSAVGALLV SFTVYIIPAT AHMLTYRKAS ARQNAAEKPP
FFMPSWTAMY VFNAFIVVWV LVVGFGFGGW ASMSNFIKQI DNFGLFAKCY QCKGPAPPAM
AAAPPPHHHN H
//
