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2.A.43.1.4
Cystinosin homolog of 270 aas and 6 or 7 TMSs uses the proton gradient to drive cystine export from the lysosome into the cytoplasm. Löbel et al. 2022 presented the crystal structures of cystinosin from Arabidopsis thaliana in both apo and cystine bound states. They establish a mechanism for cystine recognition and proton coupled transport. Mutational mapping and functional characterisation of human cystinosin provided a framework for understanding the molecular impact of disease-causing mutations.

Accession Number:P57758
Protein Name:Cystinosin homolog
Length:270
Molecular Weight:31027.00
Species:Arabidopsis thaliana (Mouse-ear cress) [3702]
Number of TMSs:7
Location1 / Topology2 / Orientation3: Lysosome membrane1 / Multi-pass membrane protein2
Substrate hydron, cystine

Cross database links:

Entrez Gene ID: 834067   
KEGG: ath:AT5G40670   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005765 C:lysosomal membrane
GO:0005774 C:vacuolar membrane
GO:0006810 P:transport

References (2)

[1] “Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones.”  Sato S.et.al.   9628582
[2] “Empirical analysis of transcriptional activity in the Arabidopsis genome.”  Yamada K.et.al.   14593172

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MASWNSIPLE ISYEIVGWIA FASWSISFYP QLILNFRRRS VVGLNFDFVM LNLTKHSSYM 
61:	IYNVCLYFSP VIQKQYFDTY GDKEMIPVAA NDVAFSIHAV VMTAVTLFQI FIYERGPQKV 
121:	SRLAIGIVVV VWGFAAICFF IALPTHSWLW LISIFNSIQV FMTCVKYIPQ AKMNFTRKST 
181:	VGWSIGNILL DFTGGLANYL QMVIQSIDQN SWKNFYGNMG KTLLSLISIF FDILFMFQHY 
241:	VLYPEKKVSK SPETGEESNE PLIDSSHEHV