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Folate transporter 1 (FOLT) (Intestinal folate carrier 1) (IFC-1) (Placental folate transporter) (Reduced folate carrier protein) (RFC) (Solute carrier family 19 member 1)

 S19A1_HUMAN             Reviewed;         591 AA.
P41440; B2R7U8; B7Z8C3; E9PFY4; O00553; O60227; Q13026; Q9BTX8;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 3.
12-SEP-2018, entry version 157.
RecName: Full=Folate transporter 1;
Short=FOLT;
AltName: Full=Intestinal folate carrier 1;
Short=IFC-1;
AltName: Full=Placental folate transporter;
AltName: Full=Reduced folate carrier protein;
Short=RFC;
AltName: Full=Solute carrier family 19 member 1;
Name=SLC19A1; Synonyms=FLOT1, RFC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-27.
TISSUE=Placenta;
PubMed=7826387; DOI=10.1006/bbrc.1995.1096;
Prasad P.D., Ramamoorthy S., Leibach F.H., Ganapathy V.;
"Molecular cloning of the human placental folate transporter.";
Biochem. Biophys. Res. Commun. 206:681-687(1995).
[2]
SEQUENCE REVISION TO 490-527.
Prasad P.D.;
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-27.
PubMed=7615551; DOI=10.1074/jbc.270.29.17468;
Wong S.C., Proefke A., Bhushan A., Matherly L.H.;
"Isolation of human cDNAs that restore methotrexate sensitivity and
reduced folate carrier activity in methotrexate transport-defective
Chinese hamster ovary cells.";
J. Biol. Chem. 270:17468-17475(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-27.
TISSUE=Testis;
PubMed=7641195;
Moscow J.A., Gong M., He R., Sgagias M.K., Dixon K.H., Anzick S.L.,
Meltzer P.S., Cowan K.H.;
"Isolation of a gene encoding a human reduced folate carrier (RFC1)
and analysis of its expression in transport-deficient, methotrexate-
resistant human breast cancer cells.";
Cancer Res. 55:3790-3794(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lymphoma;
PubMed=7852378; DOI=10.1074/jbc.270.7.2987;
Williams F.M., Flintoff W.F.;
"Isolation of a human cDNA that complements a mutant hamster cell
defective in methotrexate uptake.";
J. Biol. Chem. 270:2987-2992(1995).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-27.
TISSUE=Liver;
Tolner B.M., Roy K., Sirotnak F.M.;
"Structural analysis of the human RFC1 gene encoding a folate
transporter and alternatively spliced transcripts with 5' end
heterogeneity.";
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Small intestine;
PubMed=9041240; DOI=10.1053/gast.1997.v112.pm9041240;
Nguyen T.T., Dyer D.L., Dunning D.D., Rubin S.A., Grant K.E.,
Said H.M.;
"Human intestinal folate transport: cloning, expression, and
distribution of complementary RNA.";
Gastroenterology 112:783-791(1997).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Thymus, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
ARG-27.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
TOPOLOGY.
PubMed=10347183; DOI=10.1074/jbc.274.23.16269;
Ferguson P.L., Flintoff W.F.;
"Topological and functional analysis of the human reduced folate
carrier by hemagglutinin epitope insertion.";
J. Biol. Chem. 274:16269-16278(1999).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND SER-503, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-225, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Transporter for the intake of folate. Uptake of folate
in human placental choriocarcinoma cells occurs by a novel
mechanism called potocytosis which functionally couples three
components, namely the folate receptor, the folate transporter,
and a V-type H(+)-pump.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P41440-1; Sequence=Displayed;
Name=2;
IsoId=P41440-2; Sequence=VSP_042891;
Note=No experimental confirmation available.;
Name=3;
IsoId=P41440-3; Sequence=VSP_044497;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Placenta, liver, and to a much smaller extent,
in lung.
-!- PTM: Heavily glycosylated.
-!- SIMILARITY: Belongs to the reduced folate carrier (RFC)
transporter (TC 2.A.48) family. {ECO:0000305}.
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EMBL; U15939; AAA98442.1; -; mRNA.
EMBL; U19720; AAC50180.1; -; mRNA.
EMBL; S78996; AAB35058.1; -; mRNA.
EMBL; U17566; AAA74914.1; -; mRNA.
EMBL; U92873; AAC26162.1; -; Genomic_DNA.
EMBL; U92869; AAC26162.1; JOINED; Genomic_DNA.
EMBL; U92870; AAC26162.1; JOINED; Genomic_DNA.
EMBL; U92871; AAC26162.1; JOINED; Genomic_DNA.
EMBL; U92872; AAC26162.1; JOINED; Genomic_DNA.
EMBL; AF004354; AAB61417.1; -; mRNA.
EMBL; AK303168; BAH13909.1; -; mRNA.
EMBL; AK313125; BAG35945.1; -; mRNA.
EMBL; AL163302; CAB90483.1; ALT_SEQ; Genomic_DNA.
EMBL; BX322561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471079; EAX09331.1; -; Genomic_DNA.
EMBL; BC003068; AAH03068.1; -; mRNA.
CCDS; CCDS13725.1; -. [P41440-1]
CCDS; CCDS56217.1; -. [P41440-2]
CCDS; CCDS56218.1; -. [P41440-3]
PIR; I38924; I38924.
PIR; I52728; I52728.
RefSeq; NP_001192135.1; NM_001205206.1. [P41440-3]
RefSeq; NP_001192136.1; NM_001205207.1. [P41440-2]
RefSeq; NP_919231.1; NM_194255.2. [P41440-1]
RefSeq; XP_011528002.1; XM_011529700.2. [P41440-1]
RefSeq; XP_011528003.1; XM_011529701.2. [P41440-1]
RefSeq; XP_011528004.1; XM_011529702.2. [P41440-1]
RefSeq; XP_011528005.1; XM_011529703.2. [P41440-1]
RefSeq; XP_011528006.1; XM_011529704.2. [P41440-1]
RefSeq; XP_016883935.1; XM_017028446.1. [P41440-3]
UniGene; Hs.736903; -.
UniGene; Hs.84190; -.
ProteinModelPortal; P41440; -.
BioGrid; 112461; 6.
IntAct; P41440; 4.
STRING; 9606.ENSP00000308895; -.
BindingDB; P41440; -.
ChEMBL; CHEMBL4833; -.
DrugBank; DB00563; Methotrexate.
DrugBank; DB06813; Pralatrexate.
GuidetoPHARMACOLOGY; 1014; -.
TCDB; 2.A.48.1.1; the reduced folate carrier (rfc) family.
iPTMnet; P41440; -.
PhosphoSitePlus; P41440; -.
SwissPalm; P41440; -.
BioMuta; SLC19A1; -.
DMDM; 12643280; -.
EPD; P41440; -.
MaxQB; P41440; -.
PaxDb; P41440; -.
PeptideAtlas; P41440; -.
PRIDE; P41440; -.
ProteomicsDB; 55462; -.
ProteomicsDB; 55463; -. [P41440-2]
DNASU; 6573; -.
Ensembl; ENST00000311124; ENSP00000308895; ENSG00000173638. [P41440-1]
Ensembl; ENST00000380010; ENSP00000369347; ENSG00000173638. [P41440-3]
Ensembl; ENST00000485649; ENSP00000441772; ENSG00000173638. [P41440-2]
GeneID; 6573; -.
KEGG; hsa:6573; -.
UCSC; uc002zhl.3; human. [P41440-1]
CTD; 6573; -.
DisGeNET; 6573; -.
EuPathDB; HostDB:ENSG00000173638.18; -.
GeneCards; SLC19A1; -.
HGNC; HGNC:10937; SLC19A1.
HPA; HPA024802; -.
MalaCards; SLC19A1; -.
MIM; 600424; gene.
neXtProt; NX_P41440; -.
OpenTargets; ENSG00000173638; -.
Orphanet; 306574; Methotrexate dose selection.
PharmGKB; PA327; -.
eggNOG; KOG3810; Eukaryota.
eggNOG; ENOG410XT34; LUCA.
GeneTree; ENSGT00510000046382; -.
HOGENOM; HOG000001583; -.
HOVERGEN; HBG054198; -.
InParanoid; P41440; -.
KO; K14609; -.
OMA; HILWNVV; -.
OrthoDB; EOG091G0BSJ; -.
PhylomeDB; P41440; -.
TreeFam; TF313684; -.
Reactome; R-HSA-196757; Metabolism of folate and pterines.
SIGNOR; P41440; -.
ChiTaRS; SLC19A1; human.
GeneWiki; SLC19A1; -.
GenomeRNAi; 6573; -.
PRO; PR:P41440; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000173638; Expressed in 183 organ(s), highest expression level in blood.
CleanEx; HS_FLOT1; -.
CleanEx; HS_RFC1; -.
CleanEx; HS_SLC19A1; -.
ExpressionAtlas; P41440; baseline and differential.
Genevisible; P41440; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:BHF-UCL.
GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0008518; F:folate:anion antiporter activity; IDA:BHF-UCL.
GO; GO:0005542; F:folic acid binding; IBA:GO_Central.
GO; GO:0008517; F:folic acid transmembrane transporter activity; ISS:BHF-UCL.
GO; GO:0015350; F:methotrexate transmembrane transporter activity; IBA:GO_Central.
GO; GO:1904447; P:folate import across plasma membrane; IDA:BHF-UCL.
GO; GO:0046655; P:folic acid metabolic process; TAS:Reactome.
GO; GO:0015884; P:folic acid transport; ISS:BHF-UCL.
GO; GO:0051958; P:methotrexate transport; IBA:GO_Central.
CDD; cd06174; MFS; 1.
InterPro; IPR002666; Folate_carrier.
InterPro; IPR020846; MFS_dom.
InterPro; IPR036259; MFS_trans_sf.
InterPro; IPR028339; RFC.
PANTHER; PTHR10686; PTHR10686; 1.
PANTHER; PTHR10686:SF12; PTHR10686:SF12; 1.
Pfam; PF01770; Folate_carrier; 1.
PIRSF; PIRSF028739; Folate_carrier; 1.
PIRSF; PIRSF500793; Folate_transporter_1; 1.
SUPFAM; SSF103473; SSF103473; 2.
TIGRFAMs; TIGR00806; rfc; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Folate-binding;
Glycoprotein; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 591 Folate transporter 1.
/FTId=PRO_0000178660.
TOPO_DOM 1 23 Cytoplasmic.
{ECO:0000305|PubMed:10347183}.
TRANSMEM 24 44 Helical. {ECO:0000305}.
TOPO_DOM 45 70 Extracellular.
{ECO:0000305|PubMed:10347183}.
TRANSMEM 71 89 Helical. {ECO:0000305}.
TOPO_DOM 90 95 Cytoplasmic.
{ECO:0000305|PubMed:10347183}.
TRANSMEM 96 116 Helical. {ECO:0000305}.
TOPO_DOM 117 123 Extracellular.
{ECO:0000305|PubMed:10347183}.
TRANSMEM 124 144 Helical. {ECO:0000305}.
TOPO_DOM 145 159 Cytoplasmic.
{ECO:0000305|PubMed:10347183}.
TRANSMEM 160 177 Helical. {ECO:0000305}.
TOPO_DOM 178 186 Extracellular.
{ECO:0000305|PubMed:10347183}.
TRANSMEM 187 203 Helical. {ECO:0000305}.
TOPO_DOM 204 259 Cytoplasmic.
{ECO:0000305|PubMed:10347183}.
TRANSMEM 260 287 Helical. {ECO:0000305}.
TOPO_DOM 288 309 Extracellular.
{ECO:0000305|PubMed:10347183}.
TRANSMEM 310 327 Helical. {ECO:0000305}.
TOPO_DOM 328 333 Cytoplasmic.
{ECO:0000305|PubMed:10347183}.
TRANSMEM 334 354 Helical. {ECO:0000305}.
TOPO_DOM 355 360 Extracellular.
{ECO:0000305|PubMed:10347183}.
TRANSMEM 361 378 Helical. {ECO:0000305}.
TOPO_DOM 379 394 Cytoplasmic.
{ECO:0000305|PubMed:10347183}.
TRANSMEM 395 419 Helical. {ECO:0000305}.
TOPO_DOM 420 433 Extracellular.
{ECO:0000305|PubMed:10347183}.
TRANSMEM 434 454 Helical. {ECO:0000305}.
TOPO_DOM 455 591 Cytoplasmic.
{ECO:0000305|PubMed:10347183}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 225 225 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 474 474 Phosphoserine.
{ECO:0000250|UniProtKB:P41438}.
MOD_RES 485 485 Phosphoserine.
{ECO:0000250|UniProtKB:P41438}.
MOD_RES 499 499 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 503 503 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 63 MVPSSPAVEKQVPVEPGPDPELRSWRHLVCYLCFYGFMAQI
RPGESFITPYLLGPDKNFTREQ -> MRPQPAEPAPGGRGN
EACSIHSE (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042891.
VAR_SEQ 432 591 FQLYSVYFLILSIIYFLGAMLDGLRHCQRGHHPRQPPAQGL
RSAAEEKAAQALSVQDKGLGGLQPAQSPPLSPEDSLGAVGP
ASLEQRQSDPYLAQAPAPQAAEFLSPVTTPSPCTLCSAQAS
GPEAADETCPQLAVHPPGVSKLGLQCLPSDGVQNVNQ ->
NEELHVASLSLWKSHLRLAADTLSSEGSSGSGPRSWFLSPT
LRAALHGPVCPSEVCPS (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044497.
VARIANT 27 27 H -> R (in dbSNP:rs1051266).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7615551,
ECO:0000269|PubMed:7641195,
ECO:0000269|PubMed:7826387,
ECO:0000269|Ref.6}.
/FTId=VAR_020210.
VARIANT 558 558 A -> V (in dbSNP:rs35786590).
/FTId=VAR_052404.
CONFLICT 62 63 EQ -> DE (in Ref. 1 and 4).
{ECO:0000305}.
CONFLICT 268 268 R -> P (in Ref. 1; AAA98442).
{ECO:0000305}.
CONFLICT 457 457 H -> D (in Ref. 4; AAB35058).
{ECO:0000305}.
CONFLICT 483 483 A -> R (in Ref. 4; AAB35058).
{ECO:0000305}.
CONFLICT 549 549 C -> S (in Ref. 1, 4, 5 and 6).
{ECO:0000305}.
SEQUENCE 591 AA; 64868 MW; 0437B1615F5517EB CRC64;
MVPSSPAVEK QVPVEPGPDP ELRSWRHLVC YLCFYGFMAQ IRPGESFITP YLLGPDKNFT
REQVTNEITP VLSYSYLAVL VPVFLLTDYL RYTPVLLLQG LSFVSVWLLL LLGHSVAHMQ
LMELFYSVTM AARIAYSSYI FSLVRPARYQ RVAGYSRAAV LLGVFTSSVL GQLLVTVGRV
SFSTLNYISL AFLTFSVVLA LFLKRPKRSL FFNRDDRGRC ETSASELERM NPGPGGKLGH
ALRVACGDSV LARMLRELGD SLRRPQLRLW SLWWVFNSAG YYLVVYYVHI LWNEVDPTTN
SARVYNGAAD AASTLLGAIT SFAAGFVKIR WARWSKLLIA GVTATQAGLV FLLAHTRHPS
SIWLCYAAFV LFRGSYQFLV PIATFQIASS LSKELCALVF GVNTFFATIV KTIITFIVSD
VRGLGLPVRK QFQLYSVYFL ILSIIYFLGA MLDGLRHCQR GHHPRQPPAQ GLRSAAEEKA
AQALSVQDKG LGGLQPAQSP PLSPEDSLGA VGPASLEQRQ SDPYLAQAPA PQAAEFLSPV
TTPSPCTLCS AQASGPEAAD ETCPQLAVHP PGVSKLGLQC LPSDGVQNVN Q


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