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2.A.1.14.10
Lysosomal sialate transporter (Salla disease and infantile sialate storage disease protein (Morin et al., 2004)). Also transports glucuronic acid and aspartate. Structure-function studies have identify crucial residues and substrate-induced conformational changes (Courville et al., 2010). Also called SLC17A5. The substrate binding pocket has been identified based on modeling studies (Pietrancosta et al., 2012).  NAAG (N-acetylaspartylglutamate) an abundant neuropeptide in the vertebrate nervous system that is released from synaptic terminals in a calcium-dependent manner and acts as an agonist at the type II metabotropic glutamate receptor mGluR3, is transported into synaptic vesicles before it is secreted. Lodder-Gadaczek et al. 2013 demonstrate that vesicular uptake of NAAG and the related peptide NAAG2 (N-acetylaspartylglutamylglutamate) is mediated by sialin (SLC17A5). Sialin is probably the only vesicular transporter for NAAG and NAAG2, because transport of both peptides was not detectable in vesicles isolated from sialin-deficient mice.  Sialin also transports nitrate in the plasma membrane of salivary glands (Qin et al. 2012).

Accession Number:Q9NRA2
Protein Name:Sialin
Length:495
Molecular Weight:54640.00
Species: [9606]
Number of TMSs:12
Location1 / Topology2 / Orientation3: Lysosome membrane1 / Multi-pass membrane protein2
Substrate Sialic acid

Cross database links:

COG0477
Genevestigator: Q9NRA2 Q9NRA2
HEGENOM: HBG561587 HOG000230811
RefSeq: NP_036566.1   
Entrez Gene ID: 26503   
Pfam: PF07690   
OMIM: 236750  phenotype
269920  phenotype
604322  gene
604369  phenotype
KEGG: hsa:26503    hsa:26503   

Gene Ontology

GO:0005887 C:integral to plasma membrane
GO:0005765 C:lysosomal membrane
GO:0005624 C:membrane fraction
GO:0005351 F:sugar:hydrogen symporter activity
GO:0006820 P:anion transport
GO:0055085 P:transmembrane transport
GO:0016023 C:cytoplasmic membrane-bounded vesicle
GO:0015136 F:sialic acid transmembrane transporter activity

References (15)

[1] “Identification of a novel membrane protein, HP59, with therapeutic potential as a target of tumor angiogenesis.”  Fu C.et.al.   11751519
[2] “A new gene, encoding an anion transporter, is mutated in sialic acid storage diseases.”  Verheijen F.W.et.al.   10581036
[3] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[4] “The DNA sequence and analysis of human chromosome 6.”  Mungall A.J.et.al.   14574404
[5] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[6] “The spectrum of SLC17A5-gene mutations resulting in free sialic acid-storage diseases indicates some genotype-phenotype correlation.”  Aula N.et.al.   10947946
[7] “Sialic acid storage disease of the Salla phenotype in American monozygous twin female sibs.”  Martin R.A.et.al.   12794687
[8] “Identification of a novel membrane protein, HP59, with therapeutic potential as a target of tumor angiogenesis.”  Fu C.et.al.   11751519
[9] “A new gene, encoding an anion transporter, is mutated in sialic acid storage diseases.”  Verheijen F.W.et.al.   10581036
[10] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[11] “The DNA sequence and analysis of human chromosome 6.”  Mungall A.J.et.al.   14574404
[12] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[13] “Integral and associated lysosomal membrane proteins.”  Schroeder B.et.al.   17897319
[14] “The spectrum of SLC17A5-gene mutations resulting in free sialic acid-storage diseases indicates some genotype-phenotype correlation.”  Aula N.et.al.   10947946
[15] “Sialic acid storage disease of the Salla phenotype in American monozygous twin female sibs.”  Martin R.A.et.al.   12794687

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FASTA formatted sequence
1:	MRSPVRDLAR NDGEESTDRT PLLPGAPRAE AAPVCCSARY NLAILAFFGF FIVYALRVNL 
61:	SVALVDMVDS NTTLEDNRTS KACPEHSAPI KVHHNQTGKK YQWDAETQGW ILGSFFYGYI 
121:	ITQIPGGYVA SKIGGKMLLG FGILGTAVLT LFTPIAADLG VGPLIVLRAL EGLGEGVTFP 
181:	AMHAMWSSWA PPLERSKLLS ISYAGAQLGT VISLPLSGII CYYMNWTYVF YFFGTIGIFW 
241:	FLLWIWLVSD TPQKHKRISH YEKEYILSSL RNQLSSQKSV PWVPILKSLP LWAIVVAHFS 
301:	YNWTFYTLLT LLPTYMKEIL RFNVQENGFL SSLPYLGSWL CMILSGQAAD NLRAKWNFST 
361:	LCVRRIFSLI GMIGPAVFLV AAGFIGCDYS LAVAFLTIST TLGGFCSSGF SINHLDIAPS 
421:	YAGILLGITN TFATIPGMVG PVIAKSLTPD NTVGEWQTVF YIAAAINVFG AIFFTLFAKG 
481:	EVQNWALNDH HGHRH