ID   SC5AA_HUMAN             Reviewed;         596 AA.
AC   A0PJK1; A8MUC9; B4DPI0; B7WPR4; Q6P5X0; Q8IXM4; Q96LQ1;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Sodium/mannose cotransporter SLC5A10 {ECO:0000305|PubMed:22212718, ECO:0000305|PubMed:24573086};
DE   AltName: Full=Sodium/glucose cotransporter 5;
DE            Short=Na(+)/glucose cotransporter 5;
DE   AltName: Full=Solute carrier family 5 member 10;
GN   Name=SLC5A10; Synonyms=SGLT5 {ECO:0000303|PubMed:24573086};
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 [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC   TISSUE=Kidney;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 3-596 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE
RP   SCALE MRNA] OF 6-596 (ISOFORM 1).
RC   TISSUE=Brain, and 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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-145 AND THR-148, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [5]
RP   FUNCTION (ISOFORMS 1 AND 2), TRANSPORT ACTIVITY (ISOFORM 1),
RP   BIOPHYSICOCHEMICAL PROPERTIES (ISOFORM 1), TISSUE SPECIFICITY (ISOFORMS 1;
RP   2; 4 AND 5), AND ALTERNATIVE SPLICING (ISOFORMS 1; 2; 4 AND 5).
RX   PubMed=22212718; DOI=10.1016/j.febslet.2011.12.027;
RA   Grempler R., Augustin R., Froehner S., Hildebrandt T., Simon E., Mark M.,
RA   Eickelmann P.;
RT   "Functional characterisation of human SGLT-5 as a novel kidney-specific
RT   sodium-dependent sugar transporter.";
RL   FEBS Lett. 586:248-253(2012).
RN   [6]
RP   FUNCTION (ISOFORM 1), AND TRANSPORT ACTIVITY (ISOFORM 1).
RX   PubMed=23451068; DOI=10.1371/journal.pone.0056681;
RA   Fukuzawa T., Fukazawa M., Ueda O., Shimada H., Kito A., Kakefuda M.,
RA   Kawase Y., Wada N.A., Goto C., Fukushima N., Jishage K., Honda K.,
RA   King G.L., Kawabe Y.;
RT   "SGLT5 reabsorbs fructose in the kidney but its deficiency paradoxically
RT   exacerbates hepatic steatosis induced by fructose.";
RL   PLoS ONE 8:e56681-e56681(2013).
RN   [7]
RP   FUNCTION (ISOFORM 1), TRANSPORT ACTIVITY (ISOFORM 1), AND ACTIVITY
RP   REGULATION (ISOFORM 1).
RX   PubMed=24573086; DOI=10.1152/ajpcell.00027.2014;
RA   Ghezzi C., Gorraitz E., Hirayama B.A., Loo D.D., Grempler R., Mayoux E.,
RA   Wright E.M.;
RT   "Fingerprints of hSGLT5 sugar and cation selectivity.";
RL   Am. J. Physiol. 306:C864-C870(2014).
CC   -!- FUNCTION: [Isoform 1]: Electrogenic Na+-coupled sugar symporter that
CC       actively transports D-mannose or D-fructose at the plasma membrane,
CC       with a Na+ to sugar coupling ratio of 1:1. Transporter activity is
CC       driven by a transmembrane Na+ electrochemical gradient set by the
CC       Na+/K+ pump. Exclusively recognizes sugar substrates having a pyranose
CC       ring with an axial hydroxyl group on carbon 2 (PubMed:24573086,
CC       PubMed:22212718, PubMed:23451068). Has likely evolved to enable renal
CC       reabsorption of D-mannose, an important constituent of oligosaccharide
CC       chains of glycoproteins. Contributes to dietary D-fructose reabsorption
CC       from glomerular filtrate across the brush border of the kidney
CC       (PubMed:22212718, PubMed:23451068). {ECO:0000269|PubMed:22212718,
CC       ECO:0000269|PubMed:23451068, ECO:0000269|PubMed:24573086}.
CC   -!- FUNCTION: [Isoform 2]: Appears to have no transporter activity.
CC       {ECO:0000269|PubMed:22212718}.
CC   -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC       Reaction=D-mannose(out) + Na(+)(out) = D-mannose(in) + Na(+)(in);
CC         Xref=Rhea:RHEA:72907, ChEBI:CHEBI:4208, ChEBI:CHEBI:29101;
CC         Evidence={ECO:0000269|PubMed:22212718, ECO:0000269|PubMed:24573086};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72908;
CC         Evidence={ECO:0000250|UniProtKB:Q5SWY8};
CC   -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC       Reaction=D-fructopyranose(out) + Na(+)(out) = D-fructopyranose(in) +
CC         Na(+)(in); Xref=Rhea:RHEA:72915, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:37714; Evidence={ECO:0000269|PubMed:22212718,
CC         ECO:0000269|PubMed:23451068};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72916;
CC         Evidence={ECO:0000250|UniProtKB:Q5SWY8};
CC   -!- ACTIVITY REGULATION: [Isoform 1]: Inhibited by phlorizin.
CC       {ECO:0000269|PubMed:24573086}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 1]:
CC       Kinetic parameters:
CC         KM=0.45 mM for D-mannose {ECO:0000269|PubMed:22212718};
CC         KM=0.62 mM for D-fructopyranose {ECO:0000269|PubMed:22212718};
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q5SWY8}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=IF2;
CC         IsoId=A0PJK1-1; Sequence=Displayed;
CC       Name=2; Synonyms=IF3;
CC         IsoId=A0PJK1-2; Sequence=VSP_029417;
CC       Name=3;
CC         IsoId=A0PJK1-3; Sequence=VSP_029416, VSP_029417, VSP_029418,
CC                                  VSP_029419;
CC       Name=4; Synonyms=IF1;
CC         IsoId=A0PJK1-4; Sequence=VSP_029418;
CC       Name=5; Synonyms=IF4;
CC         IsoId=A0PJK1-5; Sequence=VSP_045061;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed at high levels in kidney.
CC       Very low expression is detected in testes.
CC       {ECO:0000269|PubMed:22212718}.
CC   -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in kidney.
CC       {ECO:0000269|PubMed:22212718}.
CC   -!- TISSUE SPECIFICITY: [Isoform 2]: The most abundant isoform expressed in
CC       kidney. {ECO:0000269|PubMed:22212718}.
CC   -!- TISSUE SPECIFICITY: [Isoform 4]: Expressed in kidney.
CC       {ECO:0000269|PubMed:22212718}.
CC   -!- TISSUE SPECIFICITY: [Isoform 5]: Expressed in kidney.
CC       {ECO:0000269|PubMed:22212718}.
CC   -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB71619.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK057946; BAB71619.1; ALT_SEQ; mRNA.
DR   EMBL; AK298345; BAG60592.1; -; mRNA.
DR   EMBL; AC003957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC034380; AAH34380.1; -; mRNA.
DR   EMBL; BC039868; AAH39868.1; -; mRNA.
DR   EMBL; BC062617; AAH62617.1; -; mRNA.
DR   CCDS; CCDS11201.2; -. [A0PJK1-4]
DR   CCDS; CCDS42275.1; -. [A0PJK1-1]
DR   CCDS; CCDS59277.1; -. [A0PJK1-5]
DR   CCDS; CCDS59278.1; -. [A0PJK1-2]
DR   CCDS; CCDS74008.1; -. [A0PJK1-3]
DR   RefSeq; NP_001035915.1; NM_001042450.2. [A0PJK1-1]
DR   RefSeq; NP_001257577.1; NM_001270648.1. [A0PJK1-2]
DR   RefSeq; NP_001257578.1; NM_001270649.1. [A0PJK1-5]
DR   RefSeq; NP_001269346.1; NM_001282417.1. [A0PJK1-3]
DR   RefSeq; NP_689564.3; NM_152351.4. [A0PJK1-4]
DR   AlphaFoldDB; A0PJK1; -.
DR   SMR; A0PJK1; -.
DR   BioGRID; 125922; 6.
DR   STRING; 9606.ENSP00000379008; -.
DR   DrugCentral; A0PJK1; -.
DR   TCDB; 2.A.21.3.15; the solute:sodium symporter (sss) family.
DR   GlyCosmos; A0PJK1; 2 sites, No reported glycans.
DR   GlyGen; A0PJK1; 2 sites.
DR   iPTMnet; A0PJK1; -.
DR   PhosphoSitePlus; A0PJK1; -.
DR   BioMuta; SLC5A10; -.
DR   jPOST; A0PJK1; -.
DR   MassIVE; A0PJK1; -.
DR   PaxDb; 9606-ENSP00000379008; -.
DR   PeptideAtlas; A0PJK1; -.
DR   ProteomicsDB; 4787; -.
DR   ProteomicsDB; 57; -. [A0PJK1-1]
DR   ProteomicsDB; 58; -. [A0PJK1-2]
DR   ProteomicsDB; 59; -. [A0PJK1-3]
DR   ProteomicsDB; 60; -. [A0PJK1-4]
DR   Antibodypedia; 13581; 111 antibodies from 26 providers.
DR   DNASU; 125206; -.
DR   Ensembl; ENST00000317977.10; ENSP00000324346.6; ENSG00000154025.16. [A0PJK1-3]
DR   Ensembl; ENST00000395643.6; ENSP00000379005.2; ENSG00000154025.16. [A0PJK1-2]
DR   Ensembl; ENST00000395645.4; ENSP00000379007.3; ENSG00000154025.16. [A0PJK1-1]
DR   Ensembl; ENST00000395647.6; ENSP00000379008.2; ENSG00000154025.16. [A0PJK1-4]
DR   Ensembl; ENST00000417251.6; ENSP00000401875.2; ENSG00000154025.16. [A0PJK1-5]
DR   GeneID; 125206; -.
DR   KEGG; hsa:125206; -.
DR   MANE-Select; ENST00000395645.4; ENSP00000379007.3; NM_001042450.4; NP_001035915.1.
DR   UCSC; uc002gur.3; human. [A0PJK1-1]
DR   AGR; HGNC:23155; -.
DR   CTD; 125206; -.
DR   DisGeNET; 125206; -.
DR   GeneCards; SLC5A10; -.
DR   HGNC; HGNC:23155; SLC5A10.
DR   HPA; ENSG00000154025; Tissue enriched (kidney).
DR   MIM; 618636; gene.
DR   neXtProt; NX_A0PJK1; -.
DR   OpenTargets; ENSG00000154025; -.
DR   PharmGKB; PA134940254; -.
DR   VEuPathDB; HostDB:ENSG00000154025; -.
DR   eggNOG; KOG2349; Eukaryota.
DR   GeneTree; ENSGT00940000159416; -.
DR   HOGENOM; CLU_018808_9_2_1; -.
DR   InParanoid; A0PJK1; -.
DR   OMA; LFGGMWS; -.
DR   OrthoDB; 74094at2759; -.
DR   PhylomeDB; A0PJK1; -.
DR   TreeFam; TF352855; -.
DR   PathwayCommons; A0PJK1; -.
DR   Reactome; R-HSA-189200; Cellular hexose transport.
DR   BioGRID-ORCS; 125206; 21 hits in 1146 CRISPR screens.
DR   ChiTaRS; SLC5A10; human.
DR   GenomeRNAi; 125206; -.
DR   Pharos; A0PJK1; Tbio.
DR   PRO; PR:A0PJK1; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; A0PJK1; Protein.
DR   Bgee; ENSG00000154025; Expressed in kidney epithelium and 90 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0140930; F:fructose:sodium symporter activity; IDA:UniProtKB.
DR   GO; GO:0005412; F:glucose:sodium symporter activity; IBA:GO_Central.
DR   GO; GO:0140929; F:mannose:sodium symporter activity; IDA:UniProtKB.
DR   GO; GO:0015370; F:solute:sodium symporter activity; TAS:Reactome.
DR   GO; GO:0008645; P:hexose transmembrane transport; TAS:Reactome.
DR   CDD; cd11489; SLC5sbd_SGLT5; 1.
DR   Gene3D; 1.20.1730.10; Sodium/glucose cotransporter; 1.
DR   InterPro; IPR038377; Na/Glc_symporter_sf.
DR   InterPro; IPR001734; Na/solute_symporter.
DR   InterPro; IPR018212; Na/solute_symporter_CS.
DR   NCBIfam; TIGR00813; sss; 1.
DR   PANTHER; PTHR11819:SF128; SODIUM_GLUCOSE COTRANSPORTER 5; 1.
DR   PANTHER; PTHR11819; SOLUTE CARRIER FAMILY 5; 1.
DR   Pfam; PF00474; SSF; 1.
DR   PROSITE; PS00457; NA_SOLUT_SYMP_2; 1.
DR   PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
DR   Genevisible; A0PJK1; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Glycoprotein; Ion transport; Membrane;
KW   Phosphoprotein; Reference proteome; Sodium; Sodium transport;
KW   Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..596
FT                   /note="Sodium/mannose cotransporter SLC5A10"
FT                   /id="PRO_0000311211"
FT   TOPO_DOM        1..15
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..72
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..99
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        121..149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        171..173
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        195..200
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..264
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        286..300
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        322..355
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        377..409
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        431..443
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        444..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        465..471
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        472..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        493..513
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        514..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        535..575
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        576..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         141
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         145
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         148
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..56
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029416"
FT   VAR_SEQ         187..213
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029417"
FT   VAR_SEQ         327
FT                   /note="P -> PGAHVYEERHQVSVSRT (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029418"
FT   VAR_SEQ         328..363
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045061"
FT   VAR_SEQ         414
FT                   /note="R -> RTGIPSTPPAPQSRLSFLLPETPPLERYLLGLVVMDLW (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029419"
FT   VARIANT         522
FT                   /note="A -> V (in dbSNP:rs12604020)"
FT                   /id="VAR_052493"
SQ   SEQUENCE   596 AA;  64342 MW;  73D104A9F8065926 CRC64;
     MAANSTSDLH TPGTQLSVAD IIVITVYFAL NVAVGIWSSC RASRNTVNGY FLAGRDMTWW
     PIGASLFASS EGSGLFIGLA GSGAAGGLAV AGFEWNATYV LLALAWVFVP IYISSEIVTL
     PEYIQKRYGG QRIRMYLSVL SLLLSVFTKI SLDLYAGALF VHICLGWNFY LSTILTLGIT
     ALYTIAGGLA AVIYTDALQT LIMVVGAVIL TIKAFDQIGG YGQLEAAYAQ AIPSRTIANT
     TCHLPRTDAM HMFRDPHTGD LPWTGMTFGL TIMATWYWCT DQVIVQRSLS ARDLNHAKAG
     SILASYLKML PMGLIIMPGM ISRALFPDDV GCVVPSECLR ACGAEVGCSN IAYPKLVMEL
     MPIGLRGLMI AVMLAALMSS LTSIFNSSST LFTMDIWRRL RPRSGERELL LVGRLVIVAL
     IGVSVAWIPV LQDSNSGQLF IYMQSVTSSL APPVTAVFVL GVFWRRANEQ GAFWGLIAGL
     VVGATRLVLE FLNPAPPCGE PDTRPAVLGS IHYLHFAVAL FALSGAVVVA GSLLTPPPQS
     VQIENLTWWT LAQDVPLGTK AGDGQTPQKH AFWARVCGFN AILLMCVNIF FYAYFA
//