GIL1_ENTHI
ID GIL1_ENTHI Reviewed; 1278 AA.
AC P32022;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Galactose-inhibitable lectin 170 kDa subunit;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE, AND
RP VARIANT ARG-442.
RX PubMed=2014248; DOI=10.1073/pnas.88.8.3248;
RA Mann B.J., Torian B.E., Vedvick T.S., Petri W.A. Jr.;
RT "Sequence of a cysteine-rich galactose-specific lectin of Entamoeba
RT histolytica.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3248-3251(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=15729342; DOI=10.1038/nature03291;
RA Loftus B.J., Anderson I., Davies R., Alsmark U.C., Samuelson J., Amedeo P.,
RA Roncaglia P., Berriman M., Hirt R.P., Mann B.J., Nozaki T., Suh B., Pop M.,
RA Duchene M., Ackers J., Tannich E., Leippe M., Hofer M., Bruchhaus I.,
RA Willhoeft U., Bhattacharya A., Chillingworth T., Churcher C.M., Hance Z.,
RA Harris B., Harris D., Jagels K., Moule S., Mungall K.L., Ormond D.,
RA Squares R., Whitehead S., Quail M.A., Rabbinowitsch E., Norbertczak H.,
RA Price C., Wang Z., Guillen N., Gilchrist C., Stroup S.E., Bhattacharya S.,
RA Lohia A., Foster P.G., Sicheritz-Ponten T., Weber C., Singh U.,
RA Mukherjee C., El-Sayed N.M.A., Petri W.A., Clark C.G., Embley T.M.,
RA Barrell B.G., Fraser C.M., Hall N.;
RT "The genome of the protist parasite Entamoeba histolytica.";
RL Nature 433:865-868(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RA Lorenzi H., Amedeo P., Inman J., Schobel S., Caler E.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lectin that binds galactose.
CC -!- SUBUNIT: Heterodimer of a heavy (170 kDa) and a light subunit (35 kDa)
CC linked by disulfide bonds.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: N-glycosylated.
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DR EMBL; M59850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS571212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P32022; -.
DR ABCD; P32022; 4 sequenced antibodies.
DR VEuPathDB; AmoebaDB:EHI5A_097310; -.
DR VEuPathDB; AmoebaDB:EHI5A_223980; -.
DR VEuPathDB; AmoebaDB:EHI5A_267920; -.
DR VEuPathDB; AmoebaDB:EHI7A_034930; -.
DR VEuPathDB; AmoebaDB:EHI8A_064380; -.
DR VEuPathDB; AmoebaDB:EHI_133900; -.
DR VEuPathDB; AmoebaDB:KM1_116600; -.
DR VEuPathDB; AmoebaDB:KM1_116910; -.
DR VEuPathDB; AmoebaDB:KM1_117020; -.
DR VEuPathDB; AmoebaDB:KM1_117130; -.
DR VEuPathDB; AmoebaDB:KM1_117340; -.
DR Proteomes; UP000001926; Partially assembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Lectin; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1278
FT /note="Galactose-inhibitable lectin 170 kDa subunit"
FT /id="PRO_0000087491"
FT TRANSMEM 1220..1240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 875
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 977
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 442
FT /note="K -> R"
FT /evidence="ECO:0000269|PubMed:2014248"
FT CONFLICT 1..4
FT /note="DKLN -> GRLD (in Ref. 1; M59850)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="I -> N (in Ref. 1; M59850)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="L -> G (in Ref. 1; M59850)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="E -> T (in Ref. 1; M59850)"
FT /evidence="ECO:0000305"
FT CONFLICT 55..61
FT /note="TTTDGNK -> DKNDNT (in Ref. 1; M59850)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="D -> N (in Ref. 1; M59850)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="K -> N (in Ref. 1; M59850)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="K -> R (in Ref. 1; M59850)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="N -> S (in Ref. 1; M59850)"
FT /evidence="ECO:0000305"
FT CONFLICT 818
FT /note="D -> N (in Ref. 1; M59850)"
FT /evidence="ECO:0000305"
FT CONFLICT 825
FT /note="N -> T (in Ref. 1; M59850)"
FT /evidence="ECO:0000305"
FT CONFLICT 981
FT /note="T -> A (in Ref. 1; M59850)"
FT /evidence="ECO:0000305"
FT CONFLICT 1141
FT /note="Missing (in Ref. 1; M59850)"
FT /evidence="ECO:0000305"
FT CONFLICT 1223..1225
FT /note="VVV -> AVI (in Ref. 1; M59850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1278 AA; 143583 MW; B48C33E7F5EB2CB1 CRC64;
DKLNEFSADI DYYDLGIMSR GKNAGSWYHS YEHQYDVFYY LAMQPWRHFV WTTCTTTDGN
KECYKYTINE DHNVKVEDIN KTDIKQDFCQ KEYAYPIEKY EVDWDNVPVD EQRIESVDIN
GKTCFKYAAK RPLAYVYLNT KMTYATKTEA YDVCRMDFIG GRSITFRSFN TENKAFIDQY
NTNTTSKCLL KVYDNNVNTH LAIIFGITDS TVIKSLQENL SLLSQLKTVK GVTLYYLKDD
TYFTVNITLD QLKYDTLVKY TAGTGQVDPL INIAKNDLAT KVADKSKDKN ANDKIKRGTM
IVLMDTALGS EFNAETEFDR KNISVHTVVL NRNKDPKITR SALRLVSLGP HYHEFTGNDE
VNATITALFK GIRANLTERC DRDKCSGFCD AMNRCTCPMC CENDCFYTSC DVETGSCIPW
PKAKPKAKKE CPATCVGSYE CKDLEGCVVT KYNDTCQPKV KCMVPYCDND KNLTEVCKQK
ANCEADQKPS SDGYCWSYTC DQTTGFCKKD KRGKEMCTGK TNNCQEYVCD SEQRCSVRDK
VCVKTSPYIE MSCYVAKCNL NTGMCENRLS CDTYSSCGGD STGSVCKCDS TTGNKCQCNK
VKNGNYCNSK NHEICDYTGT TPQCKVSNCT EDLVRDGCLI KRCNETSKTT YWENVDCSNT
KIEFAKDDKS ETMCKQYYST TCLNGKCVVQ AVGDVSNVGC GYCSMGTDNI ITYHDDCNSR
KSQCGNFNGK CIKGNDNSYS CVFEKDKTSS KSDNDICAEC SSLTCPADTT YRTYTYDSKT
GTCKATVQPT PACSVCESGK FVEKCKDQKL ERKVTLEDGK EYKYNIPKDC VNEQCIPRTY
IDCLGNDDNF KSIYNFYLPC QAYVTATYHY SSLFNLTSYK LHLPQSEEFM KEADKEAYCT
YEITTRECKT CSLIETREKV QEVDLCAEET KNGGVPFKCK NNNCIIDPNF DCQPIECKIQ
EIVITEKDGI KTTTCKNTTK TTCDTNNKRI EDARKAFIEG KEGIEQVECA STVCQNDNSC
PIITDVEKCN QNTEVDYGCK AMTGECDGTT YLCKFVQLTD DPSLDSEHFR TKSGVELNNA
CLKYKCVESK GSDGKITHKW EIDTERSNAN PKPRNPCETA TCNQTTGETI YTKKTCTVSE
EFPTITPNQG RCFYCQCSYL DGSSVLTMYG ETDKEYYDLD ACGNCRVWNQ TDRTQQLNNH
TECILAGEIN NVGAIAAATT VAVVVVAVVV ALIVVSIGLF KTYQLVSSAM KNAITITNEN
AEYVGADNEA TNAATFNG
