ID A0A1S3BGQ7_CUCME Unreviewed; 459 AA.
AC A0A1S3BGQ7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=GABA transporter 1-like {ECO:0000313|RefSeq:XP_008446788.1};
GN Name=LOC103489411 {ECO:0000313|RefSeq:XP_008446788.1};
GN Synonyms=103489411 {ECO:0000313|EnsemblPlants:MELO3C012372.2.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008446788.1};
RN [1] {ECO:0000313|Proteomes:UP000089565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [2] {ECO:0000313|EnsemblPlants:MELO3C012372.2.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2023) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_008446788.1}
RP IDENTIFICATION.
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_008446788.1; XM_008448566.2.
DR EnsemblPlants; MELO3C012372.2.1; MELO3C012372.2.1; MELO3C012372.2.
DR GeneID; 103489411; -.
DR Gramene; MELO3C012372.2.1; MELO3C012372.2.1; MELO3C012372.2.
DR KEGG; cmo:103489411; -.
DR eggNOG; KOG1303; Eukaryota.
DR InParanoid; A0A1S3BGQ7; -.
DR OrthoDB; 1112843at2759; -.
DR Proteomes; UP000089565; Unplaced.
DR Proteomes; UP000596662; Unplaced.
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:SF38; AMINO ACID TRANSPORTER TRANSMEMBRANE DOMAIN-CONTAINING PROTEIN; 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:UP000089565};
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 73..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 419..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 41..442
FT /note="Amino acid transporter transmembrane"
FT /evidence="ECO:0000259|Pfam:PF01490"
SQ SEQUENCE 459 AA; 49825 MW; 62CB310ECD71EF09 CRC64;
MGILAPISGA DQAAADKEKG GALVQPTAEL DAGALFVLKS RGSWWHCGYH LTTSIVAPAL
LSLPFAFRLL GWVGGSICLL LGGVVTFYAY LLLSLVLEHH AMQGSRLLRF RDMATYILGP
KWAIFYVGPI QFGVCYGSVV AGILIGGQNL KYIYVLCNPE GEMQLYQFII IFGTLMLILA
QIPSFHSLRH INLVSLTLSL AYSASATAAS LILGYSKNAP PRDYSLQGSP VSQLFNAFNG
ISVIATTYAC GMLPEIQATL VAPVKGKMFK GLCLCYTVIA VTFLSVGISG YWTFGNEAMG
TVLSNFMAHN SLPSWLLIIT NIFCFLQVSA VAGTYLQPTN EVFEKIFADP NKNQFSMRNI
VPRLISRSLS VVVAIIIGAM LPFFGDLMAL IGAFGFIPLD FIMPMIFYNA TFKPSKHSLI
YWVNTLIVAV SSVLAIIGGV ASIRQIVLDA KEYRLFANV
//
