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KLOT_MACFA
ID   KLOT_MACFA              Reviewed;        1014 AA.
AC   Q8WP17; Q8WP18;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Klotho;
DE            EC=3.2.1.31;
DE   Contains:
DE     RecName: Full=Klotho peptide;
DE   Flags: Precursor;
GN   Name=KL;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA   Koh N., Fujimori T., Nabeshima Y.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       similarity). Essential factor for the specific interaction between
CC       FGF23 and FGFR1 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
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   -!- SUBUNIT: Homodimer. Interacts with FGF23 and FGFR1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC       {ECO:0000250|UniProtKB:O35082}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:O35082}. Apical cell membrane
CC       {ECO:0000250|UniProtKB:O35082}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:O35082}. Note=Isoform 1 shedding leads to a
CC       soluble peptide. {ECO:0000250|UniProtKB:O35082}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC       {ECO:0000250|UniProtKB:O35082}.
CC   -!- SUBCELLULAR LOCATION: [Klotho peptide]: Secreted
CC       {ECO:0000250|UniProtKB:O35082}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Membrane-bound;
CC         IsoId=Q8WP17-1; Sequence=Displayed;
CC       Name=2; Synonyms=Secreted;
CC         IsoId=Q8WP17-2; Sequence=VSP_015826, VSP_015827;
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   -!- 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; AF064053; AAC77917.1; -; mRNA.
DR   EMBL; AF064054; AAC77918.1; -; mRNA.
DR   AlphaFoldDB; Q8WP17; -.
DR   SMR; Q8WP17; -.
DR   STRING; 9541.XP_005586019.1; -.
DR   eggNOG; KOG0626; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004566; F:beta-glucuronidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007568; P:aging; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Glycoprotein; Glycosidase; Hydrolase;
KW   Membrane; Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..1014
FT                   /note="Klotho"
FT                   /id="PRO_0000042245"
FT   CHAIN           36..?
FT                   /note="Klotho peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000042246"
FT   TOPO_DOM        36..983
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        984..1004
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1005..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..551
FT                   /note="DTTLSQFTDLNVYLW -> SQLAKPISSLTKPYH (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_015826"
FT   VAR_SEQ         552..1014
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_015827"
SQ   SEQUENCE   1014 AA;  116469 MW;  00669CD244A4DD0F CRC64;
     MPASAPPRRP RPPPPSLSLS LLLVLLGLAG RRLRAEPGDG AQTWARFARP PAPEAAGLFQ
     GTFPDGFLWA VGSAAYQTEG GWQQHGKGAS IWDTFTHHPL APPGDSRIAN VPSGAPSPLQ
     PATGDVASDS YNNVFRDTEA LRELGVTHYR FSISWARVLP NGSAGVPNRE GLRYYRRLLE
     RLRELGVQPV VTLYHWDLPQ RLQDAYGGWA NRALADHFRD YAELCFRHFG GQVKYWITID
     NPYVVAWHGY ATGRLAPGIR GSPRLGYLVA HNLLLAHAKV WHLYNTSFRP TQGGQVSIAL
     SSHWINPRRM TDHSIKECQK SLDFVLGWFA KPIFIDGDYP ESMKNNLSSL LPDFTESEKK
     FIKGTADFFA LSFGPTLSFQ LLDPHMKFRQ LESPSLRQLL SWIDLEYNHP QIFIVENGWF
     VSGTTKRDDA KYMYYLKKFI METLKAIKLD GVDVIGYTAW SLMDGFEWHR GYSIRRGLFY
     VDFLSQEKTL LPKSSALFYQ KLIEKNGFPP LPENQPLEGT FPCDFAWGIV DNYIQVDTTL
     SQFTDLNVYL WDVHHSKRLI KVDGVVTKKR KSYCVDFAAI QPQITLLQEM HVTHFRFSLD
     WALILPLGNQ SQVNHTILQY YRCMVSELVR VNITPVVALW QPVAPNQGLP RLLARQGAWE
     NPYTALAFAE YARLCFQELG HHVKLWITMN EPYTRNMTYS AGHNLLKAHA LAWHVYNEKF
     RHAQNGKISI ALQADWIEPA CPFSQKDKEV AERVLEFDIG WLAEPIFGSG DYPWVMRDWL
     NQRNNFLLPY FTEDEKKLIQ GTFDFLALSH YTTILVDSEK EDPIKYNDYL EVQEMTDITW
     LNSPSQVAVV PWGLRKVLNW LKFKYGDLPM YIISNGIDDG LHAEDDQLRV YYMQNYINEA
     LKAHILDGIN LCGYFAYSFN DRTAPRFGLY RFAADQFEPK PSMKHYRKII DSNGFPGPET
     LEKFCPEEFT VCTECSFFHT RKPLVAFIAF LFFAFIVSLS LIFYYSKKGR RRYQ
 
 
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