KLOT_MOUSE
ID KLOT_MOUSE Reviewed; 1014 AA.
AC O35082; B2RR78; O70175; O70621;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Klotho;
DE EC=3.2.1.31;
DE Contains:
DE RecName: Full=Klotho peptide;
DE Flags: Precursor;
GN Name=Kl;
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 [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC TISSUE=Kidney;
RX PubMed=9363890; DOI=10.1038/36285;
RA Kuro-o M., Matsumura Y., Aizawa H., Kawaguchi H., Suga T., Utsugi T.,
RA Ohyama Y., Kurabayashi M., Kaname T., Kume E., Iwasaki H., Iida A.,
RA Shiraki-Iida T., Nishikawa S., Nagai R., Nabeshima Y.;
RT "Mutation of the mouse klotho gene leads to a syndrome resembling ageing.";
RL Nature 390:45-51(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2),
RP AND TISSUE SPECIFICITY.
RX PubMed=9537505; DOI=10.1016/s0014-5793(98)00127-6;
RA Shiraki-Iida T., Aizawa H., Matsumura Y., Sekine S., Iida A., Anazawa H.,
RA Nagai R., Kuro-o M., Nabeshima Y.;
RT "Structure of the mouse klotho gene and its two transcripts encoding
RT membrane and secreted protein.";
RL FEBS Lett. 424:6-10(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=10631108; DOI=10.1006/bbrc.1999.2009;
RA Kato Y., Arakawa E., Kinoshita S., Shirai A., Furuya A., Yamano K.,
RA Nakamura K., Iida A., Anazawa H., Koh N., Iwano A., Imura A., Fujimori T.,
RA Kuro-o M., Hanai N., Takeshige K., Nabeshima Y.;
RT "Establishment of the anti-Klotho monoclonal antibodies and detection of
RT Klotho protein in kidneys.";
RL Biochem. Biophys. Res. Commun. 267:597-602(2000).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11095966; DOI=10.1006/bbrc.2000.3864;
RA Mori K., Yahata K., Mukoyama M., Suganami T., Makino H., Nagae T.,
RA Masuzaki H., Ogawa Y., Sugawara A., Nabeshima Y., Nakao K.;
RT "Disruption of klotho gene causes an abnormal energy homeostasis in mice.";
RL Biochem. Biophys. Res. Commun. 278:665-670(2000).
RN [6]
RP FUNCTION.
RX PubMed=11016890; DOI=10.1053/meta.2000.8606;
RA Utsugi T., Ohno T., Ohyama Y., Uchiyama T., Saito Y., Matsumura Y.,
RA Aizawa H., Itoh H., Kurabayashi M., Kawazu S., Tomono S., Oka Y., Suga T.,
RA Kuro-o M., Nabeshima Y., Nagai R.;
RT "Decreased insulin production and increased insulin sensitivity in the
RT klotho mutant mouse, a novel animal model for human aging.";
RL Metabolism 49:1118-1123(2000).
RN [7]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=11411791; DOI=10.1016/s0024-3205(01)01092-x;
RA Mizuno I., Takahashi Y., Okimura Y., Kaji H., Chihara K.;
RT "Upregulation of the klotho gene expression by thyroid hormone and during
RT adipose differentiation in 3T3-L1 adipocytes.";
RL Life Sci. 68:2917-2923(2001).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12204354; DOI=10.1016/s0378-5955(02)00483-5;
RA Kamemori M., Ohyama Y., Kurabayashi M., Takahashi K., Nagai R., Furuya N.;
RT "Expression of Klotho protein in the inner ear.";
RL Hear. Res. 171:103-110(2002).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=14528024; DOI=10.1210/me.2003-0048;
RA Tsujikawa H., Kurotaki Y., Fujimori T., Fukuda K., Nabeshima Y.;
RT "Klotho, a gene related to a syndrome resembling human premature aging,
RT functions in a negative regulatory circuit of vitamin D endocrine system.";
RL Mol. Endocrinol. 17:2393-2403(2003).
RN [10]
RP INDUCTION.
RX PubMed=15485693; DOI=10.1016/j.cardiores.2004.07.011;
RA Narumiya H., Sasaki S., Kuwahara N., Irie H., Kusaba T., Kameyama H.,
RA Tamagaki K., Hatta T., Takeda K., Matsubara H.;
RT "HMG-CoA reductase inhibitors up-regulate anti-aging klotho mRNA via RhoA
RT inactivation in IMCD3 cells.";
RL Cardiovasc. Res. 64:331-336(2004).
RN [11]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15665504; DOI=10.1247/csf.29.91;
RA Li S.-A., Watanabe M., Yamada H., Nagai A., Kinuta M., Takei K.;
RT "Immunohistochemical localization of Klotho protein in brain, kidney, and
RT reproductive organs of mice.";
RL Cell Struct. Funct. 29:91-99(2004).
RN [12]
RP CLEAVAGE, TISSUE SPECIFICITY, SUBUNIT, GLYCOSYLATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15135068; DOI=10.1016/j.febslet.2004.03.090;
RA Imura A., Iwano A., Tohyama O., Tsuji Y., Nozaki K., Hashimoto N.,
RA Fujimori T., Nabeshima Y.;
RT "Secreted Klotho protein in sera and CSF: implication for post-
RT translational cleavage in release of Klotho protein from cell membrane.";
RL FEBS Lett. 565:143-147(2004).
RN [13]
RP ENZYME ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14701853; DOI=10.1074/jbc.m312392200;
RA Tohyama O., Imura A., Iwano A., Freund J.-N., Henrissat B., Fujimori T.,
RA Nabeshima Y.;
RT "Klotho is a novel beta-glucuronidase capable of hydrolyzing steroid beta-
RT glucuronides.";
RL J. Biol. Chem. 279:9777-9784(2004).
RN [14]
RP FUNCTION, LACK OF ENZYMATIC ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16123266; DOI=10.1126/science.1112766;
RA Kurosu H., Yamamoto M., Clark J.D., Pastor J.V., Nandi A., Gurnani P.,
RA McGuinness O.P., Chikuda H., Yamaguchi M., Kawaguchi H., Shimomura I.,
RA Takayama Y., Herz J., Kahn C.R., Rosenblatt K.P., Kuro-o M.;
RT "Suppression of aging in mice by the hormone Klotho.";
RL Science 309:1829-1833(2005).
RN [15]
RP FUNCTION, AND INTERACTION WITH FGF23 AND FGFR1.
RX PubMed=17086194; DOI=10.1038/nature05315;
RA Urakawa I., Yamazaki Y., Shimada T., Iijima K., Hasegawa H., Okawa K.,
RA Fujita T., Fukumoto S., Yamashita T.;
RT "Klotho converts canonical FGF receptor into a specific receptor for
RT FGF23.";
RL Nature 444:770-774(2006).
RN [16]
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: May have weak glycosidase activity towards glucuronylated
CC steroids. However, it lacks essential active site Glu residues at
CC positions 241 and 874, suggesting it may be inactive as a glycosidase
CC in vivo. May be involved in the regulation of calcium and phosphorus
CC homeostasis by inhibiting the synthesis of active vitamin D. Essential
CC factor for the specific interaction between FGF23 and FGFR1.
CC -!- FUNCTION: The Klotho peptide generated by cleavage of the membrane-
CC bound isoform may be an anti-aging circulating hormone which would
CC extend life span by inhibiting insulin/IGF1 signaling.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate;
CC Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; EC=3.2.1.31;
CC Evidence={ECO:0000269|PubMed:14701853};
CC -!- ACTIVITY REGULATION: Inhibited by D-saccharic acid 1,4-lactone and
CC taurocholic acid. {ECO:0000269|PubMed:14701853}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.249 mM for 4-methylumbelliferylglucuronide
CC {ECO:0000269|PubMed:14701853};
CC KM=0.251 mM for estrone 3-beta-D-glucuronide
CC {ECO:0000269|PubMed:14701853};
CC KM=0.174 mM for beta-estradiol 3-beta-D-glucuronide
CC {ECO:0000269|PubMed:14701853};
CC KM=0.251 mM for estriol 3-beta-D-glucuronide
CC {ECO:0000269|PubMed:14701853};
CC Vmax=0.62 uM/h/ug enzyme {ECO:0000269|PubMed:14701853};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:14701853};
CC -!- SUBUNIT: Homodimer. Interacts with FGF23 and FGFR1.
CC {ECO:0000269|PubMed:15135068, ECO:0000269|PubMed:17086194}.
CC -!- INTERACTION:
CC O35082; P16092: Fgfr1; NbExp=2; IntAct=EBI-1570828, EBI-7953898;
CC O35082; Q61851-1: Fgfr3; NbExp=2; IntAct=EBI-1570828, EBI-15820536;
CC O35082; Q03142: Fgfr4; NbExp=2; IntAct=EBI-1570828, EBI-15633599;
CC O35082; P04426: Wnt1; NbExp=2; IntAct=EBI-1570828, EBI-1570911;
CC O35082; P17553: Wnt3; NbExp=4; IntAct=EBI-1570828, EBI-1570853;
CC O35082; P22724: Wnt4; NbExp=2; IntAct=EBI-1570828, EBI-1570945;
CC O35082; P22725: Wnt5a; NbExp=2; IntAct=EBI-1570828, EBI-1570983;
CC O35082; Q9GZV9: FGF23; Xeno; NbExp=5; IntAct=EBI-1570828, EBI-6594125;
CC O35082; P11362: FGFR1; Xeno; NbExp=2; IntAct=EBI-1570828, EBI-1028277;
CC O35082; P11362-7: FGFR1; Xeno; NbExp=3; IntAct=EBI-1570828, EBI-15609945;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:10631108, ECO:0000269|PubMed:12204354,
CC ECO:0000269|PubMed:15135068, ECO:0000269|PubMed:9363890}; Single-pass
CC type I membrane protein {ECO:0000305|PubMed:9363890}. Apical cell
CC membrane {ECO:0000269|PubMed:15665504}; Single-pass type I membrane
CC protein {ECO:0000305|PubMed:15665504}. Note=Isoform 1 shedding leads to
CC a soluble peptide. {ECO:0000269|PubMed:16123266}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC {ECO:0000269|PubMed:10631108, ECO:0000269|PubMed:15135068}.
CC -!- SUBCELLULAR LOCATION: [Klotho peptide]: Secreted
CC {ECO:0000269|PubMed:16123266}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Membrane-bound;
CC IsoId=O35082-1; Sequence=Displayed;
CC Name=2; Synonyms=Secreted;
CC IsoId=O35082-2; Sequence=VSP_015828, VSP_015829;
CC -!- TISSUE SPECIFICITY: Membrane-bound protein is present in distal renal
CC tubules, inner ear, ependymal cells of brain choroid plexus, elongating
CC spermatids and mature oocytes (at protein level). Soluble peptide is
CC present in serum (100 pM) and cerebrospinal fluid. Expressed strongly
CC in kidney, moderately in brain choroid plexus, and at low levels in
CC pituitary, placenta, skeletal muscle, urinary bladder, aorta, pancreas,
CC testis, ovary, colon, thyroid gland and adipocytes.
CC {ECO:0000269|PubMed:10631108, ECO:0000269|PubMed:11411791,
CC ECO:0000269|PubMed:12204354, ECO:0000269|PubMed:15135068,
CC ECO:0000269|PubMed:15665504, ECO:0000269|PubMed:16123266,
CC ECO:0000269|PubMed:9363890, ECO:0000269|PubMed:9537505}.
CC -!- DEVELOPMENTAL STAGE: Not expressed in the embryo. Expressed in the
CC kidney of newborns. {ECO:0000269|PubMed:9363890}.
CC -!- INDUCTION: Induced by 1,25-dihydroxyvitamin D(3) in kidney. Down-
CC regulated by angiotensin II and up-regulated by statins through
CC modulation of the RhoA pathway in epithelial cells (in vitro). Isoform
CC 1 (but not isoform 2) is up-regulated by thyroid hormone in adipocytes.
CC {ECO:0000269|PubMed:11411791, ECO:0000269|PubMed:14528024,
CC ECO:0000269|PubMed:15485693}.
CC -!- DOMAIN: Contains 2 glycosyl hydrolase 1 regions. However, the first
CC region lacks the essential Glu active site residue at position 241, and
CC the second one lacks the essential Glu active site residue at position
CC 874.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15135068}.
CC -!- DISRUPTION PHENOTYPE: Mice display a syndrome resembling to human
CC aging, with short lifespan, infertility, atherosclerosis, skin atrophy,
CC osteoporosis and emphysema. They have various metabolic abnormalities,
CC including increased insulin sensitivity and decreased insulin
CC production. Mice overexpressing Kl have increased resistance to insulin
CC and IGF1, a lifespan extended of more than 20%, and generate fewer
CC offspring. {ECO:0000269|PubMed:11095966}.
CC -!- MISCELLANEOUS: [Isoform 1]: Predominates over the secreted form by more
CC than 10 times in all tissues examined.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. Klotho
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The thread of life - Issue
CC 65 of December 2005;
CC URL="https://web.expasy.org/spotlight/back_issues/065";
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DR EMBL; AB005141; BAA23381.1; -; mRNA.
DR EMBL; AB010088; BAA25307.1; -; mRNA.
DR EMBL; AB010091; BAA25308.1; -; Genomic_DNA.
DR EMBL; AB010091; BAA25309.1; -; Genomic_DNA.
DR EMBL; BC138258; AAI38259.1; -; mRNA.
DR EMBL; BC138259; AAI38260.1; -; mRNA.
DR CCDS; CCDS19889.1; -. [O35082-1]
DR RefSeq; NP_038851.2; NM_013823.2. [O35082-1]
DR AlphaFoldDB; O35082; -.
DR SMR; O35082; -.
DR BioGRID; 200958; 8.
DR CORUM; O35082; -.
DR DIP; DIP-39894N; -.
DR IntAct; O35082; 10.
DR MINT; O35082; -.
DR STRING; 10090.ENSMUSP00000077899; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR GlyGen; O35082; 6 sites.
DR iPTMnet; O35082; -.
DR PhosphoSitePlus; O35082; -.
DR jPOST; O35082; -.
DR PaxDb; O35082; -.
DR PeptideAtlas; O35082; -.
DR PRIDE; O35082; -.
DR ProteomicsDB; 264854; -. [O35082-1]
DR ProteomicsDB; 264855; -. [O35082-2]
DR ABCD; O35082; 1 sequenced antibody.
DR Antibodypedia; 7860; 392 antibodies from 40 providers.
DR DNASU; 16591; -.
DR Ensembl; ENSMUST00000078856; ENSMUSP00000077899; ENSMUSG00000058488. [O35082-1]
DR GeneID; 16591; -.
DR KEGG; mmu:16591; -.
DR UCSC; uc009auk.2; mouse. [O35082-2]
DR UCSC; uc009aul.2; mouse. [O35082-1]
DR CTD; 9365; -.
DR MGI; MGI:1101771; Kl.
DR VEuPathDB; HostDB:ENSMUSG00000058488; -.
DR eggNOG; KOG0626; Eukaryota.
DR GeneTree; ENSGT00940000157614; -.
DR HOGENOM; CLU_001859_5_2_1; -.
DR InParanoid; O35082; -.
DR OMA; LHYYRCV; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; O35082; -.
DR TreeFam; TF314803; -.
DR Reactome; R-MMU-109704; PI3K Cascade.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-190374; FGFR1c and Klotho ligand binding and activation.
DR Reactome; R-MMU-5654219; Phospholipase C-mediated cascade: FGFR1.
DR Reactome; R-MMU-5654687; Downstream signaling of activated FGFR1.
DR Reactome; R-MMU-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-MMU-5654689; PI-3K cascade:FGFR1.
DR Reactome; R-MMU-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-MMU-5654726; Negative regulation of FGFR1 signaling.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR BioGRID-ORCS; 16591; 9 hits in 73 CRISPR screens.
DR PRO; PR:O35082; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O35082; protein.
DR Bgee; ENSMUSG00000058488; Expressed in choroid plexus of fourth ventricle and 60 other tissues.
DR Genevisible; O35082; MM.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; ISS:MGI.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; ISS:MGI.
DR GO; GO:0004566; F:beta-glucuronidase activity; IEA:UniProtKB-EC.
DR GO; GO:0017134; F:fibroblast growth factor binding; IPI:UniProtKB.
DR GO; GO:0005104; F:fibroblast growth factor receptor binding; IPI:UniProtKB.
DR GO; GO:0002526; P:acute inflammatory response; ISO:MGI.
DR GO; GO:0007568; P:aging; IMP:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; IGI:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006112; P:energy reserve metabolic process; IMP:MGI.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:InterPro.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; ISO:MGI.
DR GO; GO:0042421; P:norepinephrine biosynthetic process; ISO:MGI.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISO:MGI.
DR GO; GO:0090080; P:positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway; IGI:MGI.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:1990776; P:response to angiotensin; IEA:Ensembl.
DR GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR028546; Klotho.
DR PANTHER; PTHR10353; PTHR10353; 5.
DR PANTHER; PTHR10353:SF10; PTHR10353:SF10; 5.
DR Pfam; PF00232; Glyco_hydro_1; 3.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 2.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Glycosidase; Hydrolase;
KW Membrane; Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..1014
FT /note="Klotho"
FT /id="PRO_0000042247"
FT CHAIN 35..?
FT /note="Klotho peptide"
FT /id="PRO_0000042248"
FT TOPO_DOM 35..982
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 983..1003
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1004..1014
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 59..508
FT /note="Glycosyl hydrolase-1 1"
FT REGION 517..955
FT /note="Glycosyl hydrolase-1 2"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 537..550
FT /note="DTTLSQFTDPNVYL -> SPLTKPSVGLLLPH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9363890"
FT /id="VSP_015828"
FT VAR_SEQ 551..1014
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9363890"
FT /id="VSP_015829"
FT CONFLICT 854
FT /note="L -> V (in Ref. 2; BAA25308)"
FT /evidence="ECO:0000305"
FT CONFLICT 948
FT /note="K -> R (in Ref. 1; BAA23381 and 2; BAA25308)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1014 AA; 116398 MW; 24BD772A1F81B8EC CRC64;
MLARAPPRRP PRLVLLRLLL LHLLLLALRA RCLSAEPGQG AQTWARFARA PAPEAAGLLH
DTFPDGFLWA VGSAAYQTEG GWRQHGKGAS IWDTFTHHSG AAPSDSPIVV APSGAPSPPL
SSTGDVASDS YNNVYRDTEG LRELGVTHYR FSISWARVLP NGTAGTPNRE GLRYYRRLLE
RLRELGVQPV VTLYHWDLPQ RLQDTYGGWA NRALADHFRD YAELCFRHFG GQVKYWITID
NPYVVAWHGY ATGRLAPGVR GSSRLGYLVA HNLLLAHAKV WHLYNTSFRP TQGGRVSIAL
SSHWINPRRM TDYNIRECQK SLDFVLGWFA KPIFIDGDYP ESMKNNLSSL LPDFTESEKR
LIRGTADFFA LSFGPTLSFQ LLDPNMKFRQ LESPNLRQLL SWIDLEYNHP PIFIVENGWF
VSGTTKRDDA KYMYYLKKFI METLKAIRLD GVDVIGYTAW SLMDGFEWHR GYSIRRGLFY
VDFLSQDKEL LPKSSALFYQ KLIEDNGFPP LPENQPLEGT FPCDFAWGVV DNYVQVDTTL
SQFTDPNVYL WDVHHSKRLI KVDGVVAKKR KPYCVDFSAI RPQITLLREM RVTHFRFSLD
WALILPLGNQ TQVNHTVLHF YRCMISELVH ANITPVVALW QPAAPHQGLP HALAKHGAWE
NPHTALAFAD YANLCFKELG HWVNLWITMN EPNTRNMTYR AGHHLLRAHA LAWHLYDDKF
RAAQKGKISI ALQADWIEPA CPFSQNDKEV AERVLEFDIG WLAEPIFGSG DYPRVMRDWL
NQKNNFLLPY FTEDEKKLVR GSFDFLAVSH YTTILVDWEK EDPMKYNDYL EVQEMTDITW
LNSPSQVAVV PWGLRKVLNW LRFKYGDLPM YVTANGIDDD PHAEQDSLRI YYIKNYVNEA
LKAYVLDDIN LCGYFAYSLS DRSAPKSGFY RYAANQFEPK PSMKHYRKII DSNGFLGSGT
LGRFCPEEYT VCTECGFFQT RKSLLVFISF LVFTFIISLA LIFHYSKKGQ RSYK
