ID C3Y5B7_BRAFL Unreviewed; 521 AA.
AC C3Y5B7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Lactase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_90432 {ECO:0000313|EMBL:EEN64164.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN64164.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN64164.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN64164.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|RuleBase:RU003690}.
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DR EMBL; GG666487; EEN64164.1; -; Genomic_DNA.
DR RefSeq; XP_002608154.1; XM_002608108.1.
DR AlphaFoldDB; C3Y5B7; -.
DR eggNOG; KOG0626; Eukaryota.
DR InParanoid; C3Y5B7; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU004468};
KW Hydrolase {ECO:0000256|RuleBase:RU004468};
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..521
FT /note="Lactase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002935215"
FT TRANSMEM 495..519
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 377
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 521 AA; 58811 MW; 4559D258F136D783 CRC64;
MLPLLTFSVL LSTACCAVYD YGAYDATRDS FLPGPFPDGF SFSTATAAYQ IEGGWNASGK
GESIWDRFSH TPGKVDRGDT GDVACDSYNK YREDVQLMKN MGLRDYRLSL SWPRIFPDGT
RAGGVNTDGV NYYNNVIDEL LANGITPMVT LYHWDLPQAL QDRYGGWVNE TLVEHFNDFA
AFAFQTFGDR VKYWITCGHT IIKAHARAYH TYDRDFRSTQ GGIVGITLNL DWAEPRDPEL
PADVQATDRY MQIYSDWFAH PIYVDGDYPP FIKEGLRQVG LANPGETVPE FSTEDAAYIA
GTADFFGLNH YKTRIVTSRD ITVGTAGSTF RDTIEATVAP EWPQSASSWL YVVPWGLRRL
LKHIKQTYGD PDVYITENGR SDPDVQPPIL EDTDRVCYYM TYIDEVLKAI KDDDVKVKSY
TAWSFMDNFE WDKGYTERFG LIYVNFTDPN RPRTPKRSAG FYTDIIASNG FPEGAEITKM
TRDMWEECRG GPAGWAAATH ANVGLLALCF LVTAMYNFLN M
//
