S17A5_MOUSE
ID S17A5_MOUSE Reviewed; 495 AA.
AC Q8BN82; Q3TE25;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Sialin;
DE AltName: Full=H(+)/nitrate cotransporter;
DE AltName: Full=H(+)/sialic acid cotransporter;
DE Short=AST;
DE AltName: Full=Solute carrier family 17 member 5;
DE AltName: Full=Vesicular H(+)/Aspartate-glutamate cotransporter;
GN Name=Slc17a5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Eye, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP FUNCTION.
RX PubMed=20007460; DOI=10.1523/jneurosci.3005-09.2009;
RA Prolo L.M., Vogel H., Reimer R.J.;
RT "The lysosomal sialic acid transporter sialin is required for normal CNS
RT myelination.";
RL J. Neurosci. 29:15355-15365(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transports glucuronic acid and free sialic acid out of the
CC lysosome after it is cleaved from sialoglycoconjugates undergoing
CC degradation, this is required for normal CNS myelination. Mediates
CC aspartate and glutamate membrane potential-dependent uptake into
CC synaptic vesicles and synaptic-like microvesicles. Also functions as an
CC electrogenic 2NO(3)(-)/H(+) cotransporter in the plasma membrane of
CC salivary gland acinar cells, mediating the physiological nitrate
CC efflux, 25% of the circulating nitrate ions is typically removed and
CC secreted in saliva (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:20007460}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NRA2};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NRA2}. Cytoplasmic
CC vesicle, secretory vesicle, synaptic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9NRA2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9NRA2}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q9NRA2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9NRA2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BN82-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BN82-2; Sequence=VSP_010484;
CC Name=3;
CC IsoId=Q8BN82-3; Sequence=VSP_010485, VSP_010486;
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion
CC cotransporter family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK029102; BAC26298.1; -; mRNA.
DR EMBL; AK087395; BAC39859.1; -; mRNA.
DR EMBL; AK169868; BAE41423.1; -; mRNA.
DR EMBL; BC058785; AAH58785.1; -; mRNA.
DR CCDS; CCDS23364.1; -. [Q8BN82-1]
DR CCDS; CCDS72283.1; -. [Q8BN82-2]
DR RefSeq; NP_001263381.1; NM_001276452.1. [Q8BN82-2]
DR RefSeq; NP_766361.1; NM_172773.3. [Q8BN82-1]
DR AlphaFoldDB; Q8BN82; -.
DR SMR; Q8BN82; -.
DR STRING; 10090.ENSMUSP00000056182; -.
DR GlyGen; Q8BN82; 3 sites.
DR iPTMnet; Q8BN82; -.
DR PhosphoSitePlus; Q8BN82; -.
DR MaxQB; Q8BN82; -.
DR PaxDb; Q8BN82; -.
DR PeptideAtlas; Q8BN82; -.
DR PRIDE; Q8BN82; -.
DR ProteomicsDB; 255444; -. [Q8BN82-1]
DR ProteomicsDB; 255445; -. [Q8BN82-2]
DR ProteomicsDB; 255446; -. [Q8BN82-3]
DR Antibodypedia; 31449; 114 antibodies from 27 providers.
DR DNASU; 235504; -.
DR Ensembl; ENSMUST00000052441; ENSMUSP00000056182; ENSMUSG00000049624. [Q8BN82-1]
DR Ensembl; ENSMUST00000117645; ENSMUSP00000113003; ENSMUSG00000049624. [Q8BN82-2]
DR GeneID; 235504; -.
DR KEGG; mmu:235504; -.
DR UCSC; uc009quo.2; mouse. [Q8BN82-1]
DR UCSC; uc009qup.2; mouse. [Q8BN82-3]
DR UCSC; uc012gxg.2; mouse. [Q8BN82-2]
DR CTD; 26503; -.
DR MGI; MGI:1924105; Slc17a5.
DR VEuPathDB; HostDB:ENSMUSG00000049624; -.
DR eggNOG; KOG2532; Eukaryota.
DR GeneTree; ENSGT00940000160370; -.
DR HOGENOM; CLU_001265_5_0_1; -.
DR InParanoid; Q8BN82; -.
DR OMA; RVVTTWF; -.
DR OrthoDB; 619250at2759; -.
DR PhylomeDB; Q8BN82; -.
DR TreeFam; TF313535; -.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR Reactome; R-MMU-428643; Organic anion transporters.
DR BioGRID-ORCS; 235504; 8 hits in 76 CRISPR screens.
DR ChiTaRS; Slc17a5; mouse.
DR PRO; PR:Q8BN82; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BN82; protein.
DR Bgee; ENSMUSG00000049624; Expressed in epithelium of small intestine and 219 other tissues.
DR Genevisible; Q8BN82; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015136; F:sialic acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0006820; P:anion transport; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0015739; P:sialic acid transport; ISO:MGI.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid transport; Cell membrane;
KW Cytoplasmic vesicle; Glycoprotein; Lysosome; Membrane; Reference proteome;
KW Symport; Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..495
FT /note="Sialin"
FT /id="PRO_0000220948"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..109
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..227
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..328
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..391
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..457
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 22..23
FT /note="Dileucine internalization motif"
FT /evidence="ECO:0000250"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 98..123
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010484"
FT VAR_SEQ 176..238
FT /note="GVTFPAMHAMWSSWAPPLERSKLLTISYAGAQLGTVISLPLSGIICYYMNWT
FT YVFYLFGIVGI -> KYPPPGCYVSSYARHVVFLGSPSGKKQASYHFLCGSTAWDSDLT
FT SSFRNNMLLYELDLRLLSF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010485"
FT VAR_SEQ 239..495
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010486"
SQ SEQUENCE 495 AA; 54369 MW; 6009661215D26437 CRC64;
MRPLLRGPAG NDDEESSDST PLLPGARQTE AAPVCCSARY NLAILAFCGF FVLYALRVNL
SVALVDMVDS NTTLTDNRTS KECAEHSAPI KVHHNHTGKK YKWDAETQGW ILGSFFYGYI
VTQIPGGYIA SRVGGKLLLG LGILGTSVFT LFTPLAADLG VVTLVVLRAL EGLGEGVTFP
AMHAMWSSWA PPLERSKLLT ISYAGAQLGT VISLPLSGII CYYMNWTYVF YLFGIVGIVW
FILWMWIVSD TPETHKTISH YEKEYIVSSL KNQLSSQKVV PWGSILKSLP LWAIVVAHFS
YNWSFYTLLT LLPTYMKEIL RFNVQENGFL SALPYFGCWL CMILCGQAAD YLRVKWNFST
ISVRRIFSLV GMVGPAVFLV AAGFIGCDYS LAVAFLTIST TLGGFASSGF SINHLDIAPS
YAGILLGITN TFATIPGMTG PIIAKSLTPD NTIREWQTVF CIAAAINVFG AIFFTLFAKG
EVQSWALSDH HGHRN
