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Database: UniProt
Entry: A0A087Y481_POEFO
LinkDB: A0A087Y481_POEFO
Original site: A0A087Y481_POEFO 
ID   A0A087Y481_POEFO        Unreviewed;      1824 AA.
AC   A0A087Y481;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Sucrase-isomaltase, intestinal-like {ECO:0000313|Ensembl:ENSPFOP00000012834.2};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000012834.2, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000012834.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000256|ARBA:ARBA00004655}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004655}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004401}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00779}.
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DR   EMBL; AYCK01016296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AYCK01016297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AYCK01016298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 48698.ENSPFOP00000012834; -.
DR   Ensembl; ENSPFOT00000012851.2; ENSPFOP00000012834.2; ENSPFOG00000012686.2.
DR   eggNOG; KOG1065; Eukaryota.
DR   GeneTree; ENSGT00940000164162; -.
DR   OMA; ARWYDFH; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090599; F:alpha-glucosidase activity; IEA:UniProt.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd06602; GH31_MGAM_SI_GAA; 2.
DR   CDD; cd14752; GH31_N; 2.
DR   CDD; cd00111; Trefoil; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 2.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 4.
DR   Gene3D; 4.10.110.10; Spasmolytic Protein, domain 1; 2.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR030458; Glyco_hydro_31_AS.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR030459; Glyco_hydro_31_CS.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR017957; P_trefoil_CS.
DR   InterPro; IPR000519; P_trefoil_dom.
DR   InterPro; IPR044913; P_trefoil_dom_sf.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF168; P-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 2.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 2.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 2.
DR   Pfam; PF00088; Trefoil; 2.
DR   SMART; SM00018; PD; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 2.
DR   PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR   PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
DR   PROSITE; PS00025; P_TREFOIL_1; 1.
DR   PROSITE; PS51448; P_TREFOIL_2; 2.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Sulfation {ECO:0000256|ARBA:ARBA00022641};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          55..101
FT                   /note="P-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51448"
FT   DOMAIN          927..971
FT                   /note="P-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51448"
SQ   SEQUENCE   1824 AA;  207607 MW;  E77180C49B8FDDFE CRC64;
     MQRRGKMGKK RWTTTEIILL ILFILMTILA VTMIALFITK EPGTISDETA DGFIPQCPNI
     PMSERVDCYP DPGASKTGCE QRGCCWSPLD ERNVPWCFFP TNHGYMVHSL QTPKPTELHV
     EMKRMASPSL FGGDIQELTL HAEMQTNNRL HFKIYDTKST RFEVPHEHIP TVTSSPSSDI
     SETLEIRNNP FGLVVRRKEN KKVLFDTTMA PLVFADQYIQ LSAKLPSHNI YGLGEHVHQT
     YRHDTNWRTW PIFTRDAFPN GGTHNLYGHY PFFLCLEDES GKSFGVFLLN SNAMEVTLQP
     APAVTYRTIG GVLDFYILFG DTPEDVVHEF LQLIGMPVIP AYWSLGFQLS RWNYGSLDEV
     KATVERNRAI GLPYDIQYTD IDYMEDKKDF TYDKEKFKDL PGFADYLHEK GQKYILILDP
     AIATSKRVGG APYESYDRGT QQNAWVFESD GKTPLVGEVW PGETVFPDYT SQKCIDWWID
     EYVRFSKEVK HDALWIDMNE VANFKQGSNK GCAKNKLNYP PYTPKILDDV MYSKTLCMDA
     KQAWGNHYDV HSLYGYSMVL ATEKALQQVF GSNRTLMLTR SSFPGVGKYS GHWLGDNGAN
     WNDIKWAIPG MLEFGLFGVP YIGADICGFF DNSTEELCRR WMQVGAFYPF SRNHNAEGYM
     PQDPAYYGAD SMLVKSSKHY LNIRYTLLPY LYTLFYKAHT TGETVVRPLL HEFYSDSATW
     DVDRQFLWGK HLLITPVLEP GMDRVSAYIP DALWYDYDTM ERIEDRKTRV DMYLPADKLG
     LHIRGGAILP TQEPDVTTTH SRRNPMGLIV TLDDNNQAAG ELFWDDGDSR DTVKDGNYIH
     YQFSFANGRL NLQVTHAGYK DPNNLKFEKI TIMGVPNLPP SVSVTHMPSG SVTQLPSSSF
     YHDATKQVLF LSNLGLSLGE SYTVQFDMIS DELQRFDCHP EDNADETKCK ARGCLWQTST
     IEKVPWCYYP SDYGYTVTTT SETSTGMTLD ITRNMKYRSS GRPGSPDVNN LRVQIWYHAS
     DMLQFKIWDP TADRFEVPVP LSVPSTPEAD ESKRLYKVSV TQNPFGIQVV RKSTGTKIWD
     SAIPGFTFSD LFIQVSTRLS SNFVYGFGET EHTTYRHDLN YHTWGMFSKD QPPGYKMNCY
     GVHPFYMGLE DTADAHGVLL LNSNAMDVTF QPTPALTYRT IGGILDFYMV LGPTPEMVVQ
     EYTTLIGRPV LPAYWSLGFQ LCRYGYADDS EIEELYRGMK AARIPYDVQY ADIDYMERQL
     DFVLDSQFQN LPRLVDDMRA EGMRFIFILD PAISGNETVY PAFTRGKAAD VFIKWPSHLS
     NDIVWGKVWP DFPNVVVDES LDWDTQVEIY RAYTAFPDFF RTQTAAWWKQ EIQDFYNKMK
     FDGLWIDMNE PASFVHGTVG GKCLGNPLLE NPPYMPPLES SHMGLNHKTL CMNSEQILSN
     GKKVAHYDVH NLYGWSHTKP TFDALLEVTG KRGIVVTRST YPTSGKWAGH WLGDNNSSWD
     QLFKSIIGMM EFSLFGISYT GADICGFFNP AEYEMCLRWM QLGAFYPYSR NHNGKGNPRQ
     DPVAWDNRFA EASRDVLNIR YTLLPYLYLL MFEAHTKGST VVRPVLHEFV KDKATWDIYK
     QFLWGPALLI TPALDPGVTE VEGYLPDARW YDYHTAKNVG KRATKVSMNT PLEHINLHVR
     GGYILPWQKP ENNTFYSRKN PMGLIVALSD SGTAQGSVFW DDGEGIDTVG KNQYLLTSVK
     AEEKTLSSQI VHNALDPADH LILGVVRVWG AGTVKITGAT LTDKDGATHS LSVTHDTNTE
     ELTIDVTSKA VPLHHPFSIT WKTG
//
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