OPT4_ARATH
ID OPT4_ARATH Reviewed; 729 AA.
AC Q9FME8; Q8LBQ6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Oligopeptide transporter 4;
DE Short=AtOPT4;
GN Name=OPT4; OrderedLocusNames=At5g64410; ORFNames=MSJ1.25;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, NOMENCLATURE, AND TISSUE SPECIFICITY.
RX PubMed=11788749; DOI=10.1104/pp.010332;
RA Koh S., Wiles A.M., Sharp J.S., Naider F.R., Becker J.M., Stacey G.;
RT "An oligopeptide transporter gene family in Arabidopsis.";
RL Plant Physiol. 128:21-29(2002).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-8, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17869214; DOI=10.1016/j.bbrc.2007.08.177;
RA Hem S., Rofidal V., Sommerer N., Rossignol M.;
RT "Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify
RT phosphorylation sites in secondary active transporters.";
RL Biochem. Biophys. Res. Commun. 363:375-380(2007).
CC -!- FUNCTION: Involved in the translocation of tetra- and pentapeptides
CC across the cellular membrane in an energy-dependent manner.
CC {ECO:0000269|PubMed:11788749}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, leaves, roots, and stems.
CC {ECO:0000269|PubMed:11788749}.
CC -!- SIMILARITY: Belongs to the oligopeptide OPT transporter (TC 2.A.67.1)
CC family. {ECO:0000305}.
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DR EMBL; AB008268; BAB09872.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97890.1; -; Genomic_DNA.
DR EMBL; AY099843; AAM20694.1; -; mRNA.
DR EMBL; BT000339; AAN15658.1; -; mRNA.
DR EMBL; AY087053; AAM64614.1; -; mRNA.
DR RefSeq; NP_201246.1; NM_125837.4.
DR AlphaFoldDB; Q9FME8; -.
DR BioGRID; 21804; 4.
DR STRING; 3702.AT5G64410.1; -.
DR iPTMnet; Q9FME8; -.
DR PaxDb; Q9FME8; -.
DR PRIDE; Q9FME8; -.
DR ProteomicsDB; 248818; -.
DR EnsemblPlants; AT5G64410.1; AT5G64410.1; AT5G64410.
DR GeneID; 836562; -.
DR Gramene; AT5G64410.1; AT5G64410.1; AT5G64410.
DR KEGG; ath:AT5G64410; -.
DR Araport; AT5G64410; -.
DR TAIR; locus:2173408; AT5G64410.
DR eggNOG; KOG2262; Eukaryota.
DR HOGENOM; CLU_004965_1_1_1; -.
DR InParanoid; Q9FME8; -.
DR OMA; LTWWAFL; -.
DR OrthoDB; 190227at2759; -.
DR PhylomeDB; Q9FME8; -.
DR PRO; PR:Q9FME8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FME8; baseline and differential.
DR Genevisible; Q9FME8; AT.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:TAIR.
DR GO; GO:0035673; F:oligopeptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR004648; Oligpept_transpt.
DR InterPro; IPR004813; OPT.
DR PANTHER; PTHR22601; PTHR22601; 1.
DR Pfam; PF03169; OPT; 1.
DR TIGRFAMs; TIGR00727; ISP4_OPT; 1.
DR TIGRFAMs; TIGR00728; OPT_sfam; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Peptide transport; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17869214"
FT CHAIN 2..729
FT /note="Oligopeptide transporter 4"
FT /id="PRO_0000213781"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 592..612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 640..660
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 673..693
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:17869214"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17869214"
FT CONFLICT 295
FT /note="F -> L (in Ref. 4; AAM64614)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="N -> K (in Ref. 4; AAM64614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 729 AA; 81793 MW; 2215E9D6FE6570DF CRC64;
MATADEFSDE DTSPIEEVRL TVTNTDDPTL PVWTFRMWFL GLISCSLLSF LNQFFSYRTE
PLVITQITVQ VATLPIGHFL AKVLPKTRFG LPGCGSARFS LNPGPFNMKE HVLISIFANA
GSAFGSGSAY AVGIITIIKA FYGRSISFIA GWLLIITTQV LGYGWAGLLR KYVVEPAHMW
WPSTLVQVSL FRALHEKDDQ RMTRAKFFVI ALVCSFGWYI VPGYLFTTLT SISWVCWAFP
RSVTAQQIGS GMRGLGLGAF TLDWTAVASF LFSPLISPFF AIANVFIGYV LLIYFVLPLA
YWGFDSYNAT RFPIFSSHLF TSVGNTYDIP AIVNDNFELD LAKYEQQGRI NLSMFFALTY
GLGFATIAST LTHVALFYGK EISERFRVSY KGKEDIHTRL MKRYKDIPSW WFYSMLAATL
LISLALCVFL NDEVQMPWWG LVFASAMAFV FTLPISIITA TTNQTPGLNI ITEYAMGLIY
PGRPIANVCF KVYGYMSMAQ AVSFLNDFKL GHYMKIPPRS MFLVQFIGTI LAGTINITVA
WWQLNSIKNI CQEELLPPNS PWTCPGDRVF FDASVIWGLV GPKRIFGSQG NYAAMNWFFL
GGALGPVIVW SLHKAFPKRS WIPLVNLPVL LGATAMMPPA TAVNYNSWIL VGTIFNLFVF
RYRKSWWQRY NYVLSAAMDA GVAFMAVLLY FSVGMEEKSL DWWGTRGEHC DLAKCPTARG
VIVDGCPVK
