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2.A.17.3.7 The root dipeptide/tripeptide transporter, PTRI (Komarova et al., 2008). Transport is electrogenic and dependent on protons. Leak currents are inhibited by Phe-Ala when this peptide binds at the active site with high affinity (Hammes et al., 2010).
Accession Number:	Q9M390
Protein Name:	Peptide transport-like protein
Length:	570
Molecular Weight:	64034.00
Species:	Arabidopsis thaliana (Mouse-ear cress) [3702]
Number of TMSs:	11
Location¹ / Topology² / Orientation³:	Cell membrane¹ / Multi-pass membrane protein²
Substrate	tripeptide, dipeptide

RefSeq:	NP_190982.1
Entrez Gene ID:	824581
Pfam:	PF00854
KEGG:	ath:AT3G54140
Gene Ontology GO:0016021 C:integral to membrane GO:0005886 C:plasma membrane GO:0042936 F:dipeptide transporter activity GO:0042937 F:tripeptide transporter activity GO:0042938 P:dipeptide transport GO:0006807 P:nitrogen compound metabolic process GO:0015031 P:protein transport GO:0042939 P:tripeptide transport
References (4) [1] “Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.” Salanoubat M.et.al. 11130713 [2] “Empirical analysis of transcriptional activity in the Arabidopsis genome.” Yamada K.et.al. 14593172 [3] “AtPTR1, a plasma membrane peptide transporter expressed during seed germination and in vascular tissue of Arabidopsis.” Dietrich D.et.al. 15500465 [4] “AtPTR1 and AtPTR5 transport dipeptides in planta.” Komarova N.Y.et.al. 18753286

UniProt (Universal Protein Resource)
CDD Search (Conserved Domain Database)

Predict TMSs (Predict number of transmembrane segments)

FASTA formatted sequence

1:	MEEKDVYTQD GTVDIHKNPA NKEKTGNWKA CRFILGNECC ERLAYYGMGT NLVNYLESRL 
61:	NQGNATAANN VTNWSGTCYI TPLIGAFIAD AYLGRYWTIA TFVFIYVSGM TLLTLSASVP 
121:	GLKPGNCNAD TCHPNSSQTA VFFVALYMIA LGTGGIKPCV SSFGADQFDE NDENEKIKKS 
181:	SFFNWFYFSI NVGALIAATV LVWIQMNVGW GWGFGVPTVA MVIAVCFFFF GSRFYRLQRP 
241:	GGSPLTRIFQ VIVAAFRKIS VKVPEDKSLL FETADDESNI KGSRKLVHTD NLKFFDKAAV 
301:	ESQSDSIKDG EVNPWRLCSV TQVEELKSII TLLPVWATGI VFATVYSQMS TMFVLQGNTM 
361:	DQHMGKNFEI PSASLSLFDT VSVLFWTPVY DQFIIPLARK FTRNERGFTQ LQRMGIGLVV 
421:	SIFAMITAGV LEVVRLDYVK THNAYDQKQI HMSIFWQIPQ YLLIGCAEVF TFIGQLEFFY 
481:	DQAPDAMRSL CSALSLTTVA LGNYLSTVLV TVVMKITKKN GKPGWIPDNL NRGHLDYFFY 
541:	LLATLSFLNF LVYLWISKRY KYKKAVGRAH

2.A.17.3.7
The root dipeptide/tripeptide transporter, PTRI (Komarova et al., 2008). Transport is electrogenic and dependent on protons. Leak currents are inhibited by Phe-Ala when this peptide binds at the active site with high affinity (Hammes et al., 2010).

Cross database links:

Gene Ontology

References (4)

External Searches:

Analyze:

2.A.17.3.7The root dipeptide/tripeptide transporter, PTRI (Komarova et al., 2008). Transport is electrogenic and dependent on protons. Leak currents are inhibited by Phe-Ala when this peptide binds at the active site with high affinity (Hammes et al., 2010).

Cross database links:

Gene Ontology

References (4)

External Searches:

Analyze:

2.A.17.3.7
The root dipeptide/tripeptide transporter, PTRI (Komarova et al., 2008). Transport is electrogenic and dependent on protons. Leak currents are inhibited by Phe-Ala when this peptide binds at the active site with high affinity (Hammes et al., 2010).