LCTL_MOUSE
ID LCTL_MOUSE Reviewed; 566 AA.
AC Q8K1F9; Q8BPR1; Q8K2M9;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Lactase-like protein;
DE AltName: Full=Klotho/lactase-phlorizin hydrolase-related protein;
DE Flags: Precursor;
GN Name=Lctl; Synonyms=Klph;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
RX PubMed=12084582; DOI=10.1016/s0167-4781(02)00281-6;
RA Ito S., Fujimori T., Hayashizaki Y., Nabeshima Y.;
RT "Identification of a novel mouse membrane-bound family 1 glycosidase-like
RT protein, which carries an atypical active site structure.";
RL Biochim. Biophys. Acta 1576:341-345(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [3]
RP FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=29425878; DOI=10.1016/j.exer.2018.02.001;
RA Fan J., Lerner J., Wyatt M.K., Cai P., Peterson K., Dong L., Wistow G.;
RT "The klotho-related protein KLPH (lctl) has preferred expression in lens
RT and is essential for expression of clic5 and normal lens suture
RT formation.";
RL Exp. Eye Res. 169:111-121(2018).
CC -!- FUNCTION: Plays a role in formation of the lens suture in the eye,
CC which is important for normal optical properties of the lens.
CC {ECO:0000269|PubMed:29425878}.
CC -!- SUBUNIT: May form dimers. {ECO:0000269|PubMed:29425878}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:12084582}; Single-pass membrane protein
CC {ECO:0000305|PubMed:12084582}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K1F9-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q8K1F9-3; Sequence=VSP_015833, VSP_015834;
CC -!- TISSUE SPECIFICITY: Strongly expressed in the lens of the eye, where it
CC localizes to the equatorial epithelium and outer layers of newly
CC extending fiber cells (at protein level) (PubMed:29425878). May also be
CC expressed in kidney and skin (PubMed:12084582). However, another study
CC suggests that expression is specific to eye and is minimal in other
CC tissues (PubMed:29425878). {ECO:0000269|PubMed:12084582,
CC ECO:0000269|PubMed:29425878}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. The lens of the eye appears
CC normal in young animals. However, formation of the lens suture is
CC abnormal with an X-shaped or double-Y shaped morphology instead of a
CC tight Y-shaped pattern. Optics of the lens are distorted and cortical
CC cataracts develop; the phenotype progressively worsens with age.
CC Expression of CLIC5 in the lens epithelium is almost completely absent.
CC {ECO:0000269|PubMed:29425878}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. Klotho
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the glycosyl hydrolase 1 family, Asp-
CC 200 is present instead of the conserved Glu which is an active site
CC residue. It is therefore expected that this protein lacks glycosidase
CC activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30631.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF309072; AAM77699.1; -; mRNA.
DR EMBL; BC030631; AAH30631.1; ALT_INIT; mRNA.
DR CCDS; CCDS23274.1; -. [Q8K1F9-1]
DR RefSeq; NP_665834.1; NM_145835.2. [Q8K1F9-1]
DR AlphaFoldDB; Q8K1F9; -.
DR SMR; Q8K1F9; -.
DR BioGRID; 231660; 1.
DR STRING; 10090.ENSMUSP00000034969; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR GlyGen; Q8K1F9; 2 sites.
DR PhosphoSitePlus; Q8K1F9; -.
DR PaxDb; Q8K1F9; -.
DR PRIDE; Q8K1F9; -.
DR ProteomicsDB; 292246; -. [Q8K1F9-1]
DR ProteomicsDB; 292247; -. [Q8K1F9-3]
DR Antibodypedia; 26209; 45 antibodies from 17 providers.
DR DNASU; 235435; -.
DR Ensembl; ENSMUST00000034969; ENSMUSP00000034969; ENSMUSG00000032401. [Q8K1F9-1]
DR GeneID; 235435; -.
DR KEGG; mmu:235435; -.
DR UCSC; uc009qbl.1; mouse. [Q8K1F9-1]
DR CTD; 197021; -.
DR MGI; MGI:2183549; Lctl.
DR VEuPathDB; HostDB:ENSMUSG00000032401; -.
DR eggNOG; KOG0626; Eukaryota.
DR GeneTree; ENSGT00940000157369; -.
DR HOGENOM; CLU_001859_1_3_1; -.
DR InParanoid; Q8K1F9; -.
DR OMA; VEACDRK; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q8K1F9; -.
DR TreeFam; TF314803; -.
DR BioGRID-ORCS; 235435; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Lctl; mouse.
DR PRO; PR:Q8K1F9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8K1F9; protein.
DR Bgee; ENSMUSG00000032401; Expressed in lens of camera-type eye and 31 other tissues.
DR ExpressionAtlas; Q8K1F9; baseline and differential.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Reference proteome; Sensory transduction; Signal; Transmembrane;
KW Transmembrane helix; Vision.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..566
FT /note="Lactase-like protein"
FT /id="PRO_0000042252"
FT TOPO_DOM 21..540
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 562..566
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..159
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015833"
FT VAR_SEQ 529..566
FT /note="EPLLRHMHVASEIVVPTVCALSILTAALMLTLLLRRRG -> GDVAETGSPL
FT HLHLSKHLFRITLLFCCRSSRDVYFSGS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015834"
SQ SEQUENCE 566 AA; 64826 MW; EC50A5730275DD84 CRC64;
MKPVWVIILG WILLVPRVGT AWRGPPEEAS FYYGTFPPGF SWGVGSSAYQ TEGAWDEDGK
GPSIWDAFTH GRKEQVLGGD TADTACDSYY KVQEDIALLK ELQVSHYRFS LSWPRLLPTG
VRAEQVNKRG IKFYSDFIDA LLKSNITPVV TLHHWDLPQM LQVAYGGWQN VSMTRYFSDY
ADLCFEVFGD RVKHWLTFSD PRTMVEKGYE TGLHAPGLRL QGTGLYVAAH HIIKAHAQAW
HSYNNTWRSK QHGLVGISLN CDWGEPVDID NPDDIEAAER YLQFCLGWFA NPIYAGDYPQ
VMKDHIGTKS AEQGLEMSRL PTFSLQEKSY LKGTSDFLGL GHFTTRYITQ RKYPSHQGPS
YQNDRDLVEL VDPNWPEMGS PWLYSVPWGF RRLLNFAQTQ YGDPPIYVTE SGAPQKLHCT
QFCDEWRIQY LKGYINEMLK AIKDGVDIKG YTSWSLLDKF EWEKGYADKY GFYYVEFNVR
NKPRYPKASV QYYKEIITAS GFPNPQEVES WRLKALETCS INNQMLATEP LLRHMHVASE
IVVPTVCALS ILTAALMLTL LLRRRG
