ID A0A0A0KSP8_CUCSA Unreviewed; 422 AA.
AC A0A0A0KSP8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Amino acid transporter transmembrane domain-containing protein {ECO:0000259|Pfam:PF01490};
GN ORFNames=Csa_5G605130 {ECO:0000313|EMBL:KGN51919.1};
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN51919.1, ECO:0000313|Proteomes:UP000029981};
RN [1] {ECO:0000313|EMBL:KGN51919.1, ECO:0000313|Proteomes:UP000029981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX PubMed=19881527; DOI=10.1038/ng.475;
RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT "The genome of the cucumber, Cucumis sativus L.";
RL Nat. Genet. 41:1275-1281(2009).
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}.
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DR EMBL; CM002926; KGN51919.1; -; Genomic_DNA.
DR RefSeq; XP_004135455.1; XM_004135407.2.
DR AlphaFoldDB; A0A0A0KSP8; -.
DR EnsemblPlants; KGN51919; KGN51919; Csa_5G605130.
DR GeneID; 101204828; -.
DR Gramene; KGN51919; KGN51919; Csa_5G605130.
DR KEGG; csv:101204828; -.
DR eggNOG; KOG1303; Eukaryota.
DR OMA; LGIFMAP; -.
DR OrthoDB; 3425278at2759; -.
DR Proteomes; UP000029981; Chromosome 5.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR013057; AA_transpt_TM.
DR PANTHER; PTHR48017:SF109; AA_TRANS 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:UP000029981};
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 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 388..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..411
FT /note="Amino acid transporter transmembrane"
FT /evidence="ECO:0000259|Pfam:PF01490"
SQ SEQUENCE 422 AA; 46306 MW; 3503C224E139BEA4 CRC64;
MESQNQLPST QFLAKGTTFL RTCINGINAL SGVGILSIPF AISQGGWVSL ILLLMVAIIC
CYTASLLKHC MDANPLMVRT YTDIGGLAFG YKGRILVSVF VYLELYLVAV EFLILEGDNL
EKLFPSSSPL FGLKIGSLKV DEGMMNYKKM YMILSAVLIL PTTWVKNLGS LAYVSFGGVL
ASIVLVLCVG WIGATDGFGF NQRSDNDHHR VLNLHGLPTT ISLFVFCYCG HSVFPMLCNS
MKNRTQFSKV LMVCFVASTL SYGSMGILGY CMYGDNIKSQ VTLNLPLNKI STKLAIYTTL
INPITKYAAI TNPIAIAIED SLSPNFFITK KIAILIRTLL LITTLILALF IPFFAYVMAF
TGSFLSVTTS ILIPCLCYLK INKSAREFGW ELILILTILV LGIFIGVFGT CSSVNQIVKR
LS
//
