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Q8BN82 (S17A5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sialin
Alternative name(s):
H(+)/nitrate cotransporter
H(+)/sialic acid cotransporter
Short name=AST
Solute carrier family 17 member 5
Vesicular H(+)/Aspartate-glutamate cotransporter
Gene names
Name:Slc17a5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transports glucuronic acid and free sialic acid out of the lysosome after it is cleaved from sialoglycoconjugates undergoing degradation, this is required for normal CNS myelination. Mediates aspartate and glutamate membrane potential-dependent uptake into synaptic vesicles and synaptic-like microvesicles. Also functions as an electrogenic 2NO3-/H+ cotransporter in the plasma membrane of salivary gland acinar cells, mediating the physiological nitrate efflux, 25% of the circulating nitrate ions is typically removed and secreted in saliva By similarity. Ref.4

Subcellular location

Cell membrane By similarity; Multi-pass membrane protein. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane By similarity. Lysosome membrane By similarity; Multi-pass membrane protein.

Sequence similarities

Belongs to the major facilitator superfamily. Sodium/anion cotransporter family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BN82-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8BN82-2)

The sequence of this isoform differs from the canonical sequence as follows:
     98-123: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8BN82-3)

The sequence of this isoform differs from the canonical sequence as follows:
     176-238: GVTFPAMHAM...VFYLFGIVGI → KYPPPGCYVS...YELDLRLLSF
     239-495: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 495495Sialin
PRO_0000220948

Regions

Topological domain1 – 4141Cytoplasmic Potential
Transmembrane42 – 6221Helical; Potential
Topological domain63 – 10947Lumenal Potential
Transmembrane110 – 13021Helical; Potential
Topological domain131 – 1366Cytoplasmic Potential
Transmembrane137 – 15721Helical; Potential
Topological domain1581Lumenal Potential
Transmembrane159 – 17921Helical; Potential
Topological domain180 – 20021Cytoplasmic Potential
Transmembrane201 – 22121Helical; Potential
Topological domain222 – 2276Lumenal Potential
Transmembrane228 – 24821Helical; Potential
Topological domain249 – 27830Cytoplasmic Potential
Transmembrane279 – 29921Helical; Potential
Topological domain300 – 32829Lumenal Potential
Transmembrane329 – 34921Helical; Potential
Topological domain350 – 36516Cytoplasmic Potential
Transmembrane366 – 38621Helical; Potential
Topological domain387 – 3915Lumenal Potential
Transmembrane392 – 41221Helical; Potential
Topological domain413 – 42311Cytoplasmic Potential
Transmembrane424 – 44421Helical; Potential
Topological domain445 – 45713Lumenal Potential
Transmembrane458 – 47821Helical; Potential
Topological domain479 – 49517Cytoplasmic Potential
Motif22 – 232Dileucine internalization motif By similarity

Amino acid modifications

Glycosylation711N-linked (GlcNAc...) Potential
Glycosylation771N-linked (GlcNAc...) Potential
Glycosylation951N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence98 – 12326Missing in isoform 2.
VSP_010484
Alternative sequence176 – 23863GVTFP…GIVGI → KYPPPGCYVSSYARHVVFLG SPSGKKQASYHFLCGSTAWD SDLTSSFRNNMLLYELDLRL LSF in isoform 3.
VSP_010485
Alternative sequence239 – 495257Missing in isoform 3.
VSP_010486

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 7, 2004. Version 2.
Checksum: 6009661215D26437

FASTA49554,369
        10         20         30         40         50         60 
MRPLLRGPAG NDDEESSDST PLLPGARQTE AAPVCCSARY NLAILAFCGF FVLYALRVNL 

        70         80         90        100        110        120 
SVALVDMVDS NTTLTDNRTS KECAEHSAPI KVHHNHTGKK YKWDAETQGW ILGSFFYGYI 

       130        140        150        160        170        180 
VTQIPGGYIA SRVGGKLLLG LGILGTSVFT LFTPLAADLG VVTLVVLRAL EGLGEGVTFP 

       190        200        210        220        230        240 
AMHAMWSSWA PPLERSKLLT ISYAGAQLGT VISLPLSGII CYYMNWTYVF YLFGIVGIVW 

       250        260        270        280        290        300 
FILWMWIVSD TPETHKTISH YEKEYIVSSL KNQLSSQKVV PWGSILKSLP LWAIVVAHFS 

       310        320        330        340        350        360 
YNWSFYTLLT LLPTYMKEIL RFNVQENGFL SALPYFGCWL CMILCGQAAD YLRVKWNFST 

       370        380        390        400        410        420 
ISVRRIFSLV GMVGPAVFLV AAGFIGCDYS LAVAFLTIST TLGGFASSGF SINHLDIAPS 

       430        440        450        460        470        480 
YAGILLGITN TFATIPGMTG PIIAKSLTPD NTIREWQTVF CIAAAINVFG AIFFTLFAKG 

       490 
EVQSWALSDH HGHRN 

« Hide

Isoform 2 [UniParc].

Checksum: B48BCF204A2D6008
Show »

FASTA46951,301
Isoform 3 [UniParc].

Checksum: 95222793B0E39762
Show »

FASTA23825,879

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Strain: C57BL/6J and NOD.
Tissue: Eye and Skin.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Olfactory epithelium.
[3]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[4]"The lysosomal sialic acid transporter sialin is required for normal CNS myelination."
Prolo L.M., Vogel H., Reimer R.J.
J. Neurosci. 29:15355-15365(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK029102 mRNA. Translation: BAC26298.1.
AK087395 mRNA. Translation: BAC39859.1.
AK169868 mRNA. Translation: BAE41423.1.
BC058785 mRNA. Translation: AAH58785.1.
CCDSCCDS23364.1. [Q8BN82-1]
CCDS72283.1. [Q8BN82-2]
RefSeqNP_001263381.1. NM_001276452.1. [Q8BN82-2]
NP_766361.1. NM_172773.3. [Q8BN82-1]
UniGeneMm.46932.

3D structure databases

ProteinModelPortalQ8BN82.
SMRQ8BN82. Positions 114-142.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8BN82.

Proteomic databases

PRIDEQ8BN82.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000052441; ENSMUSP00000056182; ENSMUSG00000049624. [Q8BN82-1]
ENSMUST00000117645; ENSMUSP00000113003; ENSMUSG00000049624. [Q8BN82-2]
ENSMUST00000119213; ENSMUSP00000113340; ENSMUSG00000049624. [Q8BN82-3]
GeneID235504.
KEGGmmu:235504.
UCSCuc009quo.1. mouse. [Q8BN82-1]
uc009qup.1. mouse. [Q8BN82-3]
uc012gxg.1. mouse. [Q8BN82-2]

Organism-specific databases

CTD26503.
MGIMGI:1924105. Slc17a5.

Phylogenomic databases

eggNOGCOG0477.
GeneTreeENSGT00640000091442.
HOGENOMHOG000230811.
HOVERGENHBG008834.
InParanoidQ8BN82.
KOK12301.
OMAKHKRISH.
OrthoDBEOG789C9Z.
PhylomeDBQ8BN82.
TreeFamTF313535.

Gene expression databases

BgeeQ8BN82.
GenevestigatorQ8BN82.

Family and domain databases

InterProIPR011701. MFS.
IPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
[Graphical view]
PfamPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMSSF103473. SSF103473. 2 hits.
PROSITEPS50850. MFS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLC17A5. mouse.
NextBio382720.
PROQ8BN82.
SOURCESearch...

Entry information

Entry nameS17A5_MOUSE
AccessionPrimary (citable) accession number: Q8BN82
Secondary accession number(s): Q3TE25
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: July 9, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot