ID A0A0S3R8L6_PHAAN Unreviewed; 631 AA.
AC A0A0S3R8L6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Auxin efflux carrier component {ECO:0000256|RuleBase:RU362108};
GN Name=Vigan.01G485000 {ECO:0000313|EMBL:BAT76794.1};
GN ORFNames=VIGAN_01485000 {ECO:0000313|EMBL:BAT76794.1};
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:BAT76794.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT76794.1, 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362108}.
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DR EMBL; AP015034; BAT76794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3R8L6; -.
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:SF4; AUXIN EFFLUX CARRIER COMPONENT 2; 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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT TRANSMEM 42..59
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT TRANSMEM 71..89
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT TRANSMEM 101..120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT TRANSMEM 518..537
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT TRANSMEM 549..571
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT TRANSMEM 609..628
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362108"
FT REGION 336..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 68643 MW; 712787D247849C54 CRC64;
MITIKDIYDV FAAIVPLYVA MILAYGSVRW WKIFTPDQCS GINRFVAVFA VPLLSFHFIS
SNDPYAMNYH FIAADSLQKV VILGALFLWN TFTKHGSLDW TITLFSLSTL PNTLVMGIPL
LKAMYGDFSG SLMVQIVVLQ SVIWYTLMLF LFEYRGAKLL ITEQFPETAG SITSFRVDSD
VVSLNGREPL QTDAEIGEDG KLHVVVKRSA ASSMISSFNK SHLTSMTPRA SNLTGVEIYS
VQSSREPTPR ASSFNQTDFY AMFASKAPSP KHGYTNSFQS NSGIGDVYSL QSSKGATPRT
SNFEEEMLKM HKKRGGRSMS GELFNGGLVS SYPPPNPMFS GSTSAGGLKK KDSTGGSAAP
NKELHMFVWS SSASPVSEGN LRHAVNRAAS TDFGTVDPSK AVPHETIASK AVQELIENMS
PGRRGSGEKE LEMDEGAKYP TSGSPYTCQK KVDIEGNANK NQQMPPASVM TRLILIMVWR
KLIRNPNTYS SLLGLTWSLV SFRWHIEMPT IVKGSISILS DAGLGMAMFS LGLFMALQPK
IIACGKSVAA FSMAVRFLTG PAVIAATSIG IGLRGVLLHV AIVQAALPQG IVPFVFAKEY
NLHADILSTA VIFGMLIALP ITILYYVLLG L
//
