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Klotho (EC 3.2.1.31) [Cleaved into: Klotho peptide]

 KLOT_RAT                Reviewed;        1014 AA.
Q9Z2Y9;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
20-JUN-2018, entry version 132.
RecName: Full=Klotho;
EC=3.2.1.31;
Contains:
RecName: Full=Klotho peptide;
Flags: Precursor;
Name=Kl;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, AND
DEVELOPMENTAL STAGE.
TISSUE=Lung;
PubMed=9791011; DOI=10.1006/bbrc.1998.9576;
Ohyama Y., Kurabayashi M., Masuda H., Nakamura T., Aihara Y.,
Kaname T., Suga T., Arai M., Aizawa H., Matsumura Y., Kuro-o M.,
Nabeshima Y., Nagai R.;
"Molecular cloning of rat klotho cDNA: markedly decreased expression
of klotho by acute inflammatory stress.";
Biochem. Biophys. Res. Commun. 251:920-925(1998).
[2]
INDUCTION.
PubMed=9731228; DOI=10.1006/bbrc.1998.9246;
Aizawa H., Saito Y., Nakamura T., Inoue M., Imanari T., Ohyama Y.,
Matsumura Y., Masuda H., Oba S., Mise N., Kimura K., Hasegawa A.,
Kurabayashi M., Kuro-o M., Nabeshima Y., Nagai R.;
"Downregulation of the Klotho gene in the kidney under sustained
circulatory stress in rats.";
Biochem. Biophys. Res. Commun. 249:865-871(1998).
[3]
TISSUE SPECIFICITY.
PubMed=10631108; DOI=10.1006/bbrc.1999.2009;
Kato Y., Arakawa E., Kinoshita S., Shirai A., Furuya A., Yamano K.,
Nakamura K., Iida A., Anazawa H., Koh N., Iwano A., Imura A.,
Fujimori T., Kuro-o M., Hanai N., Takeshige K., Nabeshima Y.;
"Establishment of the anti-Klotho monoclonal antibodies and detection
of Klotho protein in kidneys.";
Biochem. Biophys. Res. Commun. 267:597-602(2000).
[4]
INDUCTION.
PubMed=10892340; DOI=10.1007/s000180050038;
Nagai R., Saito Y., Ohyama Y., Aizawa H., Suga T., Nakamura T.,
Kurabayashi M., Kuroo M.;
"Endothelial dysfunction in the klotho mouse and downregulation of
klotho gene expression in various animal models of vascular and
metabolic diseases.";
Cell. Mol. Life Sci. 57:738-746(2000).
[5]
INDUCTION.
PubMed=11967236; DOI=10.1161/01.HYP.0000013734.33441.EA;
Mitani H., Ishizaka N., Aizawa T., Ohno M., Usui S., Suzuki T.,
Amaki T., Mori I., Nakamura Y., Sato M., Nangaku M., Hirata Y.,
Nagai R.;
"In vivo klotho gene transfer ameliorates angiotensin II-induced renal
damage.";
Hypertension 39:838-843(2002).
[6]
INDUCTION.
PubMed=12965205; DOI=10.1016/S0014-5793(03)00894-9;
Saito K., Ishizaka N., Mitani H., Ohno M., Nagai R.;
"Iron chelation and a free radical scavenger suppress angiotensin II-
induced downregulation of klotho, an anti-aging gene, in rat.";
FEBS Lett. 551:58-62(2003).
[7]
TISSUE SPECIFICITY.
PubMed=17992255; DOI=10.1172/JCI32409;
Ben-Dov I.Z., Galitzer H., Lavi-Moshayoff V., Goetz R., Kuro-o M.,
Mohammadi M., Sirkis R., Naveh-Many T., Silver J.;
"The parathyroid is a target organ for FGF23 in rats.";
J. Clin. Invest. 117:4003-4008(2007).
-!- FUNCTION: May have weak glycosidase activity towards
glucuronylated steroids. However, it lacks essential active site
Glu residues at positions 241 and 874, suggesting it may be
inactive as a glycosidase in vivo. May be involved in the
regulation of calcium and phosphorus homeostasis by inhibiting the
synthesis of active vitamin D (By similarity). Essential factor
for the specific interaction between FGF23 and FGFR1 (By
similarity). {ECO:0000250}.
-!- FUNCTION: The Klotho peptide generated by cleavage of the
membrane-bound isoform may be an anti-aging circulating hormone
which would extend life span by inhibiting insulin/IGF1 signaling.
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: A beta-D-glucuronoside + H(2)O = D-glucuronate
+ an alcohol.
-!- SUBUNIT: Homodimer. Interacts with FGF23 and FGFR1. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:O35082}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:O35082}. Apical cell membrane
{ECO:0000250|UniProtKB:O35082}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:O35082}. Note=Its shedding leads to
a soluble peptide. {ECO:0000250|UniProtKB:O35082}.
-!- SUBCELLULAR LOCATION: Klotho peptide: Secreted
{ECO:0000250|UniProtKB:O35082}.
-!- TISSUE SPECIFICITY: Present in cortical renal tubules and the
parathyroid (at protein level). Strongly expressed in kidney.
Expressed at low levels in brain, lung, intestine and ovaries.
{ECO:0000269|PubMed:10631108, ECO:0000269|PubMed:17992255,
ECO:0000269|PubMed:9791011}.
-!- DEVELOPMENTAL STAGE: Expressed faintly from E18 in the kidney.
Expression increases in the kidney after 4 days of age.
{ECO:0000269|PubMed:9791011}.
-!- INDUCTION: Down-regulated by angiotensin II and iron overload (at
protein level). Down-regulated by acute inflammatory stress, and
in models for long-term hypertension, diabetes mellitus and
chronic renal failure. {ECO:0000269|PubMed:10892340,
ECO:0000269|PubMed:11967236, ECO:0000269|PubMed:12965205,
ECO:0000269|PubMed:9731228, ECO:0000269|PubMed:9791011}.
-!- DOMAIN: Contains 2 glycosyl hydrolase 1 regions. However, the
first region lacks the essential Glu active site residue at
position 241, and the second one lacks the essential Glu active
site residue at position 874.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. Klotho
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The thread of life
- Issue 65 of December 2005;
URL="https://web.expasy.org/spotlight/back_issues/065";
-----------------------------------------------------------------------
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EMBL; AB017820; BAA34740.1; -; mRNA.
PIR; JE0333; JE0333.
RefSeq; NP_112626.1; NM_031336.1.
UniGene; Rn.30061; -.
ProteinModelPortal; Q9Z2Y9; -.
SMR; Q9Z2Y9; -.
STRING; 10116.ENSRNOP00000001449; -.
CAZy; GH1; Glycoside Hydrolase Family 1.
PaxDb; Q9Z2Y9; -.
PRIDE; Q9Z2Y9; -.
GeneID; 83504; -.
KEGG; rno:83504; -.
UCSC; RGD:620396; rat.
CTD; 9365; -.
RGD; 620396; Kl.
eggNOG; KOG0626; Eukaryota.
eggNOG; COG2723; LUCA.
HOGENOM; HOG000060126; -.
HOVERGEN; HBG081856; -.
InParanoid; Q9Z2Y9; -.
KO; K14756; -.
OrthoDB; EOG091G0035; -.
PhylomeDB; Q9Z2Y9; -.
TreeFam; TF314803; -.
PRO; PR:Q9Z2Y9; -.
Proteomes; UP000002494; Unplaced.
Genevisible; Q9Z2Y9; RN.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; TAS:RGD.
GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
GO; GO:0004566; F:beta-glucuronidase activity; IEA:UniProtKB-EC.
GO; GO:0017134; F:fibroblast growth factor binding; IBA:GO_Central.
GO; GO:0005104; F:fibroblast growth factor receptor binding; IBA:GO_Central.
GO; GO:0002526; P:acute inflammatory response; IDA:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:1901657; P:glycosyl compound metabolic process; IBA:GO_Central.
GO; GO:0008286; P:insulin receptor signaling pathway; IEA:InterPro.
GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IMP:RGD.
GO; GO:0042421; P:norepinephrine biosynthetic process; IMP:RGD.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:1990776; P:response to angiotensin; IEP:RGD.
GO; GO:0071774; P:response to fibroblast growth factor; IEP:RGD.
GO; GO:0033280; P:response to vitamin D; IEP:RGD.
InterPro; IPR001360; Glyco_hydro_1.
InterPro; IPR033132; Glyco_hydro_1_N_CS.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR028546; Klotho.
PANTHER; PTHR10353; PTHR10353; 6.
PANTHER; PTHR10353:SF10; PTHR10353:SF10; 6.
Pfam; PF00232; Glyco_hydro_1; 3.
PRINTS; PR00131; GLHYDRLASE1.
SUPFAM; SSF51445; SSF51445; 2.
PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Glycoprotein; Glycosidase;
Hydrolase; Membrane; Reference proteome; Repeat; Secreted; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 34 {ECO:0000255}.
CHAIN 35 1014 Klotho.
/FTId=PRO_0000042249.
CHAIN 35 ? Klotho peptide. {ECO:0000250}.
/FTId=PRO_0000042250.
TOPO_DOM 35 983 Extracellular. {ECO:0000255}.
TRANSMEM 984 1004 Helical. {ECO:0000255}.
TOPO_DOM 1005 1014 Cytoplasmic. {ECO:0000255}.
REGION 59 508 Glycosyl hydrolase-1 1.
REGION 517 955 Glycosyl hydrolase-1 2.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 346 346 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 609 609 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 614 614 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 696 696 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 1014 AA; 116800 MW; 16F3B57581AC1DF0 CRC64;
MPARAPPRRL PRLLLLRLLS LHLLLLTLRA RCLSAEPGQG AQTWARFARP PVPEASGLLH
DTFPDGFLWA VGSAAYQTEG GWRQHGKGAS IWDTFTHHPR AIPEDSPIVM APSGAPLPPL
PSTGDVASDS YNNVYRDTEG LRELGVTHYR FSISWARVLP NGTAGTPNRE GLRYYRRLLE
RLRELGVQPV VTLYHWDLPQ RLQDTYGGWA NRALADHFRD YAELCFRHFG GQVKYWITID
NPYVVAWHGY ATGRLAPGVR GSSRLGYLVA HNLLLAHAKV WRLYNTSFRP TQGGRVSIAL
GSHWITPRRM TDYHIRECQK SLDFVLGWFA KPIFIDGDYP KSMKNNLSSL LPDFTESEKR
FIRGTADFFA LSFGPTLSFQ LLDPSMKFRQ LESPSLRQLL SWIDLEYNHP QIFIVENGWF
VSGTTRRDDA KYMYYLKKFI MESLKAIRLD GVDVIGYTAW SLMDGFEWHR GYSIRRGLFY
VDFLSQDKEL LPKSSALFYQ KLIENNGFPP LPENQPLEGT FPCDFAWGVV DNYIQVDPTL
SQFTDPNVYL WDVHHSKRLI KVDGVVAKKR KPYCVDFSAI RPQITLLREM RVTHFRFSLD
WALILPLGNQ TQVNRTVLHF YRCMVSELVH ANITPVVALW QPATPHQGLP HALAKHGAWE
NPHTALAFAD YANLCFEELG HWVKFWITIN EPNSRNMTYR AGHHLLKAHA LAWHLYDDKF
RAAQKGKISI ALQVDWIEPA CPFSQKDKEV AERVLEFDVG WLAEPIFGSG DYPHVMREWL
NQKNNFLLPY FTEDEKKLIR GSFDFLALSH YTTILVDWEK EDPIKYNDYL EVQEMTDITW
LNSPNQVAVV PWGLRKALNW LRFKYGDLPM FVTANGIDDD PHAEQDSLRM YYIKNYVNEA
LKAYVLDGIN LCGYFAYSLS DRSVPKSGFY RYAANQFEPK PSIKHYRKII DNNGFLGSGT
LGRFCPEEYT VCTGCGFFQT RKSLLAFISF LVFAFVTSLA LIYYYSKKGR RRYK


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