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Database: UniProt
Entry: A0A2Y9IX13_ENHLU
LinkDB: A0A2Y9IX13_ENHLU
Original site: A0A2Y9IX13_ENHLU 
ID   A0A2Y9IX13_ENHLU        Unreviewed;      1928 AA.
AC   A0A2Y9IX13;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Lactase-phlorizin hydrolase {ECO:0000313|RefSeq:XP_022353088.1};
GN   Name=LOC111143551 {ECO:0000313|RefSeq:XP_022353088.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022353088.1};
RN   [1] {ECO:0000313|RefSeq:XP_022353088.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022353088.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_022353088.1; XM_022497380.1.
DR   STRING; 391180.A0A2Y9IX13; -.
DR   KEGG; elk:111143551; -.
DR   OrthoDB; 3373839at2759; -.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0016020; C: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   Gene3D; 3.20.20.80; Glycosidases; 4.
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; 4.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 4.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 2.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 3.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|RuleBase:RU004468};
KW   Hydrolase {ECO:0000256|RuleBase:RU004468,
KW   ECO:0000313|RefSeq:XP_022353088.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1928
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016052366"
FT   TRANSMEM        1884..1904
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          323..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1221..1241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1274
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
FT   ACT_SITE        1750
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   1928 AA;  218446 MW;  9D628CD17878598A CRC64;
     MELAWNSVFI VLLSFSCRGL DWESDRNFIS AAGPLTNALL YQSSPLGTQG SKFAAEDEST
     DVCQQPLPAF LPEYFRRVHA SGITHYKVFL PWAQLLPAGS SENPDNKTVR CYQQFLETLK
     TAQLQPLVVL HHQTLPPSTV QRSEVFADLF ADYASFAFHS FGDLVQIWFT FSDLEEVMKE
     LPQQESRSSR LQTLTDAHRR AYEIYHEKYA SKGGKLSVVL HADAVLELLL EPSTSSLAKG
     AVDFLSLDLS YECQSEASLP QKLSKLQTIE SKVKIFIFNL RFQDCPSTRK NSTRLLFSLL
     EAISEHQVLT IGSDVNTLLS CSPSSKRSGP YSRMGSRSLQ ASAPRDVGRA AGSSPQGSAY
     RRVWATFANQ SRAERDAFLW DVFPEDFLWG VSTGAFNVEG GWAEGGRGPS VWDPMGHLNA
     ARGAVTPEVA SDSYHKVDID VALLRGLRAQ VYKFSISWSR IFPSGRGHRP SPQGVAYYSR
     LVDSLLAAGI EPMATLFHWD LPRALQEHGG WQNDSVVDAF LDYAAFCFAT FGDRVKLWVT
     FHEPWVMSYA GYGTGRHAPG LSDPRVASFK VAHLVLKAHA RVWHHYNSHY RLQQQGRVGI
     VLNSDWAEPL SPEKPEDLTA SERFLHFMLG WFAHPIFVDG DYPAALKAQI QQMNQRCPSP
     VAQLPEFTEA EKQLLKGSAD FLGLSHYTSR LISKTQEDSC IPSYDTIGGF SQHVDPAWPQ
     TSSSWIYVVP WGIRRLLQFV YLEYTRGKVP IYLAGNGMPI GETEDLFEDS LRVDYFNKYI
     NEVLKAIKDD LVDVRSYIAR ALMDGFEGPS GYSQRFGLHH INFNDSSKPR TPRKSAYFFS
     SIIEKNGFLP KVVKRLPSPS TSNFPPKMRA FTFPSDVPSK AKVVWEKFSN QPKFERDLFY
     HGTFRDDFLW GVSSSAYQIE GAWDADGKGP SIWDNFTHTP GSNVKGGATG DIACDSYNQL
     DADLNMLRAL KVKAYRFSLS WSRIFPTGRN NSINRHGVDY YNRLINGLVA SNISPMVTLY
     HWDLPQALQD IGGWENSSLI ELFNSYADFC FQTFGDRVKF WMTFNEPTYQ AWLGYGSGEF
     PPQVKDPGWA PYRIGHAIIK AHARVYHTYN EKYRQEQKGV ISLSLSTHWA EPKSPEIPRE
     VEAADRMLQF SLGWFAHPIF RNGDYPDAMK WKVGNRSELQ HLATSRLPSF TEEEKRYIRG
     TADVFCLNTY YSRIVQHRTP KLNPPSYEDD RETTETEDSS WPATAMDRAA PWGTRRLLNW
     IKEEYGDVPI YITENGVALT SPKVEDTDRL FYHKTYINEA LKAYRLDGVD LRGYSAWSLM
     DNFEWLNGYT VKFGLYHVDF NNTNRPRTAR ASARYYTEVI TNNGMPLPRE DEFLYGHFPE
     GFIWSAASAA YQIEGAWRAD GKGLSIWDTF SHTPLRVAND DTGDVACDSY HKIAEDVVAL
     QNLGVSHYRF SVAWSRVLPD GTTKYINEAG LNYYERLIDA LLAANIKPQV TIYHWDLPQA
     LQDVGGWENE TIVQRFKEYA DVLFQRLGDK VKFWITLNEP FVIANQGYGY GTSAPGISFR
     PGTAPYIVGH NLIKAHAEAW HLYNNTYRAS QGGMISITIS SDWAEPRDPS NQEDVEAARR
     YVQFMGGWFA HPIFKNGDYN EGMKTRIRDR SLAAGLSKSR LPEFTESEKK RINGTYDFFG
     FNHYTTILAY NLDYASWISS FDADRGVASI TDRSWPDSGS FWLKMTPFGF RRILNWLKEE
     YNNPPIYVTE NGVSQRGETD LNDTLRIYYL RSYINEALKA VQDKVDLRGY TVWSVMDNFE
     WATGFAERFG LHFVNYTDPS LPRIPKASAK FFASIARCNG FPDPAAGPHP CLQSEDAGPT
     ISPMREEEVQ FLGLTLRATE AQTALYVLFS LAILGVSCVT FLSYKYCKHS KQGKTQPGQQ
     ELSTISAF
//
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