S17A5_HUMAN
ID S17A5_HUMAN Reviewed; 495 AA.
AC Q9NRA2; Q5SZ76; Q8NBR5; Q9UGH0;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Sialin;
DE AltName: Full=H(+)/nitrate cotransporter;
DE AltName: Full=H(+)/sialic acid cotransporter;
DE Short=AST;
DE AltName: Full=Membrane glycoprotein HP59;
DE AltName: Full=Solute carrier family 17 member 5;
DE AltName: Full=Vesicular H(+)/Aspartate-glutamate cotransporter;
GN Name=SLC17A5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11751519;
RA Fu C., Bardhan S., Cetateanu N.D., Wamil B.D., Wang Y., Yan H.-P., Shi E.,
RA Carter C., Venkov C., Yakes F.M., Page D.L., Lloyd R.S., Mernaugh R.L.,
RA Hellerqvist C.G.;
RT "Identification of a novel membrane protein, HP59, with therapeutic
RT potential as a target of tumor angiogenesis.";
RL Clin. Cancer Res. 7:4182-4194(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP VARIANT SD CYS-39, AND VARIANTS ISSD 268-SER--ASN-272 DEL; ARG-183 AND
RP ARG-334.
RX PubMed=10581036; DOI=10.1038/70585;
RA Verheijen F.W., Verbeek E., Aula N., Beerens C.E.M.T., Havelaar A.C.,
RA Joosse M., Peltonen L., Aula P., Galjaard H., Van der Spek P.J.,
RA Mancini G.M.S.;
RT "A new gene, encoding an anion transporter, is mutated in sialic acid
RT storage diseases.";
RL Nat. Genet. 23:462-465(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon;
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 [6]
RP FUNCTION, DILEUCINE MOTIF, AND MUTAGENESIS OF 22-LEU--LEU-23.
RX PubMed=15510212; DOI=10.1038/sj.emboj.7600464;
RA Morin P., Sagne C., Gasnier B.;
RT "Functional characterization of wild-type and mutant human sialin.";
RL EMBO J. 23:4560-4570(2004).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Placenta;
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [8]
RP TOPOLOGY, AND MUTAGENESIS OF PHE-179.
RX PubMed=20424173; DOI=10.1074/jbc.m110.130716;
RA Courville P., Quick M., Reimer R.J.;
RT "Structure-function studies of the SLC17 transporter sialin identify
RT crucial residues and substrate-induced conformational changes.";
RL J. Biol. Chem. 285:19316-19323(2010).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND VARIANT SD CYS-39.
RX PubMed=21781115; DOI=10.1111/j.1471-4159.2011.07388.x;
RA Miyaji T., Omote H., Moriyama Y.;
RT "Functional characterization of vesicular excitatory amino acid transport
RT by human sialin.";
RL J. Neurochem. 119:1-5(2011).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22778404; DOI=10.1073/pnas.1116633109;
RA Qin L., Liu X., Sun Q., Fan Z., Xia D., Ding G., Ong H.L., Adams D.,
RA Gahl W.A., Zheng C., Qi S., Jin L., Zhang C., Gu L., He J., Deng D.,
RA Ambudkar I.S., Wang S.;
RT "Sialin (SLC17A5) functions as a nitrate transporter in the plasma
RT membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:13434-13439(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP VARIANTS SD CYS-39 AND GLU-136, AND VARIANTS ISSD 268-SER--ASN-272 DEL;
RP ARG-183; ARG-334 AND VAL-371.
RX PubMed=10947946; DOI=10.1086/303077;
RA Aula N., Salomaeki P., Timonen R., Verheijen F., Mancini G.M.S.,
RA Maensson J.-E., Aula P., Peltonen L.;
RT "The spectrum of SLC17A5-gene mutations resulting in free sialic acid-
RT storage diseases indicates some genotype-phenotype correlation.";
RL Am. J. Hum. Genet. 67:832-840(2000).
RN [13]
RP VARIANT SD CYS-39.
RX PubMed=12794687; DOI=10.1002/ajmg.a.10246;
RA Martin R.A., Slaugh R., Natowicz M., Pearlman K., Orvisky E.,
RA Krasnewich D., Kleta R., Huizing M., Gahl W.A.;
RT "Sialic acid storage disease of the Salla phenotype in American monozygous
RT twin female sibs.";
RL Am. J. Med. Genet. A 120:23-27(2003).
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. {ECO:0000269|PubMed:10581036,
CC ECO:0000269|PubMed:11751519, ECO:0000269|PubMed:15510212,
CC ECO:0000269|PubMed:21781115, ECO:0000269|PubMed:22778404}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22778404};
CC Multi-pass membrane protein {ECO:0000269|PubMed:22778404}. Cytoplasmic
CC vesicle, secretory vesicle, synaptic vesicle membrane
CC {ECO:0000269|PubMed:21781115}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21781115}. Lysosome membrane
CC {ECO:0000269|PubMed:17897319}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17897319}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRA2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRA2-2; Sequence=VSP_010482, VSP_010483;
CC -!- TISSUE SPECIFICITY: Found in fetal lung and small intestine, and at
CC lower level in fetal skin and muscle. In the adult, detected in
CC placenta, kidney and pancreas. Abundant in the endothelial cells of
CC tumors from ovary, colon, breast and lung, but is not detected in
CC endothelial cells from the corresponding normal tissues.
CC {ECO:0000269|PubMed:10581036, ECO:0000269|PubMed:11751519}.
CC -!- DISEASE: Salla disease (SD) [MIM:604369]: Sialic acid storage disease
CC (SASD). SASDs are autosomal recessive neurodegenerative disorders
CC characterized by hypotonia, cerebellar ataxia and intellectual
CC disability. They are caused by a defect in the metabolism of sialic
CC acid which results in increased urinary excretion of unconjugated
CC sialic acid, specifically N-acetylneuraminic acid. Enlarged lysosomes
CC are seen on electron microscopic studies. Clinical symptoms of SD
CC present usually at age less than 1 year and progression is slow.
CC {ECO:0000269|PubMed:10581036, ECO:0000269|PubMed:10947946,
CC ECO:0000269|PubMed:12794687, ECO:0000269|PubMed:21781115}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Infantile sialic acid storage disorder (ISSD) [MIM:269920]:
CC Severe form of sialic acid storage disease. Affected newborns exhibit
CC visceromegaly, coarse features and failure to thrive immediately after
CC birth. These patients have a shortened life span, usually less than 2
CC years. {ECO:0000269|PubMed:10581036, ECO:0000269|PubMed:10947946}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion
CC cotransporter family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF97769.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF244577; AAF97769.1; ALT_INIT; mRNA.
DR EMBL; AJ387747; CAB62540.1; -; mRNA.
DR EMBL; AK075320; BAC11546.1; -; mRNA.
DR EMBL; AL121972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020961; AAH20961.1; -; mRNA.
DR CCDS; CCDS4981.1; -. [Q9NRA2-1]
DR RefSeq; NP_036566.1; NM_012434.4. [Q9NRA2-1]
DR AlphaFoldDB; Q9NRA2; -.
DR SMR; Q9NRA2; -.
DR BioGRID; 117710; 7.
DR IntAct; Q9NRA2; 2.
DR STRING; 9606.ENSP00000348019; -.
DR BindingDB; Q9NRA2; -.
DR ChEMBL; CHEMBL4630859; -.
DR TCDB; 2.A.1.14.10; the major facilitator superfamily (mfs).
DR GlyGen; Q9NRA2; 3 sites.
DR iPTMnet; Q9NRA2; -.
DR PhosphoSitePlus; Q9NRA2; -.
DR SwissPalm; Q9NRA2; -.
DR BioMuta; SLC17A5; -.
DR DMDM; 48428688; -.
DR EPD; Q9NRA2; -.
DR jPOST; Q9NRA2; -.
DR MassIVE; Q9NRA2; -.
DR MaxQB; Q9NRA2; -.
DR PaxDb; Q9NRA2; -.
DR PeptideAtlas; Q9NRA2; -.
DR PRIDE; Q9NRA2; -.
DR ProteomicsDB; 82321; -. [Q9NRA2-1]
DR ProteomicsDB; 82322; -. [Q9NRA2-2]
DR Antibodypedia; 31449; 114 antibodies from 27 providers.
DR DNASU; 26503; -.
DR Ensembl; ENST00000355773.6; ENSP00000348019.5; ENSG00000119899.13. [Q9NRA2-1]
DR GeneID; 26503; -.
DR KEGG; hsa:26503; -.
DR MANE-Select; ENST00000355773.6; ENSP00000348019.5; NM_012434.5; NP_036566.1.
DR UCSC; uc003phn.5; human. [Q9NRA2-1]
DR CTD; 26503; -.
DR DisGeNET; 26503; -.
DR GeneCards; SLC17A5; -.
DR GeneReviews; SLC17A5; -.
DR HGNC; HGNC:10933; SLC17A5.
DR HPA; ENSG00000119899; Tissue enriched (parathyroid).
DR MalaCards; SLC17A5; -.
DR MIM; 269920; phenotype.
DR MIM; 604322; gene.
DR MIM; 604369; phenotype.
DR neXtProt; NX_Q9NRA2; -.
DR OpenTargets; ENSG00000119899; -.
DR Orphanet; 309324; Free sialic acid storage disease, infantile form.
DR Orphanet; 309331; Intermediate severe Salla disease.
DR Orphanet; 309334; Salla disease.
DR PharmGKB; PA35824; -.
DR VEuPathDB; HostDB:ENSG00000119899; -.
DR eggNOG; KOG2532; Eukaryota.
DR GeneTree; ENSGT00940000160370; -.
DR HOGENOM; CLU_001265_5_0_1; -.
DR InParanoid; Q9NRA2; -.
DR OMA; RVVTTWF; -.
DR OrthoDB; 619250at2759; -.
DR PhylomeDB; Q9NRA2; -.
DR TreeFam; TF313535; -.
DR PathwayCommons; Q9NRA2; -.
DR Reactome; R-HSA-4085001; Sialic acid metabolism.
DR Reactome; R-HSA-428643; Organic anion transporters.
DR Reactome; R-HSA-5619035; Defective SLC17A5 causes Salla disease (SD) and ISSD.
DR SignaLink; Q9NRA2; -.
DR BioGRID-ORCS; 26503; 8 hits in 1069 CRISPR screens.
DR ChiTaRS; SLC17A5; human.
DR GeneWiki; HP59; -.
DR GeneWiki; SLC17A5; -.
DR GenomeRNAi; 26503; -.
DR Pharos; Q9NRA2; Tbio.
DR PRO; PR:Q9NRA2; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NRA2; protein.
DR Bgee; ENSG00000119899; Expressed in corpus epididymis and 186 other tissues.
DR Genevisible; Q9NRA2; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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; IDA:MGI.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; TAS:ProtInc.
DR GO; GO:0015136; F:sialic acid transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015538; F:sialic acid:proton symporter activity; TAS:Reactome.
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:0006811; P:ion transport; TAS:Reactome.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0015739; P:sialic acid transport; IDA: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; Disease variant; Glycoprotein; Lysosome; Membrane;
KW Phosphoprotein; Reference proteome; Symport; Synapse; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..495
FT /note="Sialin"
FT /id="PRO_0000220947"
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..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..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..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 22..23
FT /note="Dileucine internalization motif"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
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 274..276
FT /note="LSS -> AGV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_010482"
FT VAR_SEQ 278..495
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_010483"
FT VARIANT 39
FT /note="R -> C (in SD; completely devoid of aspartate and
FT glutamate transport activity, but retains appreciable H(+)/
FT sialic acid cotransport activity, frequent mutation in
FT Finland; dbSNP:rs80338794)"
FT /evidence="ECO:0000269|PubMed:10581036,
FT ECO:0000269|PubMed:10947946, ECO:0000269|PubMed:12794687,
FT ECO:0000269|PubMed:21781115"
FT /id="VAR_018684"
FT VARIANT 136
FT /note="K -> E (in SD; dbSNP:rs80338795)"
FT /evidence="ECO:0000269|PubMed:10947946"
FT /id="VAR_018685"
FT VARIANT 183
FT /note="H -> R (in ISSD; dbSNP:rs119491109)"
FT /evidence="ECO:0000269|PubMed:10581036,
FT ECO:0000269|PubMed:10947946"
FT /id="VAR_018686"
FT VARIANT 268..272
FT /note="Missing (in ISSD)"
FT /evidence="ECO:0000269|PubMed:10581036,
FT ECO:0000269|PubMed:10947946"
FT /id="VAR_018687"
FT VARIANT 296
FT /note="V -> I (in dbSNP:rs16883930)"
FT /id="VAR_034746"
FT VARIANT 334
FT /note="P -> R (in ISSD; dbSNP:rs119491110)"
FT /evidence="ECO:0000269|PubMed:10581036,
FT ECO:0000269|PubMed:10947946"
FT /id="VAR_018688"
FT VARIANT 371
FT /note="G -> V (in ISSD; dbSNP:rs777862172)"
FT /evidence="ECO:0000269|PubMed:10947946"
FT /id="VAR_018689"
FT MUTAGEN 22..23
FT /note="LL->GG: Targeted to plasma membrane; sialic acid
FT uptake strongly activated at acidic pH."
FT /evidence="ECO:0000269|PubMed:15510212"
FT MUTAGEN 179
FT /note="F->C: 15 fold increase in affinity for glucuronic
FT acid."
FT /evidence="ECO:0000269|PubMed:20424173"
SQ SEQUENCE 495 AA; 54640 MW; 5C6C154B3E93A19E CRC64;
MRSPVRDLAR NDGEESTDRT PLLPGAPRAE AAPVCCSARY NLAILAFFGF FIVYALRVNL
SVALVDMVDS NTTLEDNRTS KACPEHSAPI KVHHNQTGKK YQWDAETQGW ILGSFFYGYI
ITQIPGGYVA SKIGGKMLLG FGILGTAVLT LFTPIAADLG VGPLIVLRAL EGLGEGVTFP
AMHAMWSSWA PPLERSKLLS ISYAGAQLGT VISLPLSGII CYYMNWTYVF YFFGTIGIFW
FLLWIWLVSD TPQKHKRISH YEKEYILSSL RNQLSSQKSV PWVPILKSLP LWAIVVAHFS
YNWTFYTLLT LLPTYMKEIL RFNVQENGFL SSLPYLGSWL CMILSGQAAD NLRAKWNFST
LCVRRIFSLI GMIGPAVFLV AAGFIGCDYS LAVAFLTIST TLGGFCSSGF SINHLDIAPS
YAGILLGITN TFATIPGMVG PVIAKSLTPD NTVGEWQTVF YIAAAINVFG AIFFTLFAKG
EVQNWALNDH HGHRH
