SL17_ENTHI
ID SL17_ENTHI Reviewed; 1285 AA.
AC P23502;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=170 kDa surface lectin;
DE Flags: Precursor;
GN Name=CEL-170/4;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 16-33.
RX PubMed=2000392; DOI=10.1073/pnas.88.5.1849;
RA Tannich E., Ebert F., Horstmann R.D.;
RT "Primary structure of the 170-kDa surface lectin of pathogenic Entamoeba
RT histolytica.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:1849-1853(1991).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Tannich E., Nickel R., Ebert F., Horstmann R.D.;
RL Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 16-30.
RX PubMed=2536731; DOI=10.1016/s0021-9258(19)81714-3;
RA Petri W.A. Jr., Chapman M.D., Snodgrass T., Mann B.J., Broman J.,
RA Ravdin J.I.;
RT "Subunit structure of the galactose and N-acetyl-D-galactosamine-
RT inhibitable adherence lectin of Entamoeba histolytica.";
RL J. Biol. Chem. 264:3007-3012(1989).
CC -!- FUNCTION: Mediates adherence of E.histolytica to colonic mucins, an
CC essential step for pathogenic tissue invasion.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- PTM: Phosphorylated regions may have a role in signal transduction.
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DR EMBL; M60498; AAA29106.1; -; Genomic_DNA.
DR EMBL; X61003; CAA43321.1; -; Genomic_DNA.
DR PIR; A39117; A39117.
DR AlphaFoldDB; P23502; -.
DR STRING; 5759.rna_EHI_012270-1; -.
DR VEuPathDB; AmoebaDB:EHI5A_097310; -.
DR VEuPathDB; AmoebaDB:EHI5A_206100; -.
DR VEuPathDB; AmoebaDB:EHI5A_223980; -.
DR VEuPathDB; AmoebaDB:EHI7A_034930; -.
DR VEuPathDB; AmoebaDB:EHI8A_064380; -.
DR VEuPathDB; AmoebaDB:EHI_012270; -.
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 eggNOG; KOG1225; Eukaryota.
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; Glycoprotein; Lectin; Membrane; Phosphoprotein;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:2000392,
FT ECO:0000269|PubMed:2536731"
FT CHAIN 16..1285
FT /note="170 kDa surface lectin"
FT /id="PRO_0000022350"
FT TOPO_DOM 16..1218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1219..1247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1248..1285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 378..407
FT /note="1"
FT REPEAT 408..438
FT /note="2"
FT REPEAT 439..464
FT /note="3"
FT REPEAT 465..497
FT /note="4"
FT REPEAT 498..525
FT /note="5"
FT REPEAT 526..554
FT /note="6"
FT REPEAT 555..584
FT /note="7"
FT REPEAT 585..620
FT /note="8"
FT REPEAT 621..653
FT /note="9"
FT REGION 378..653
FT /note="9 X approximate tandem repeats"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 16
FT /note="D -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1285 AA; 144411 MW; 64BB2DFD2AD8ECBA CRC64;
MKLLLLNILL LCCLADKLNE FSADIDYYDL GIMSRGKNAG SWYHSYTHQY DVFYYLAMQP
WRHFVWTTCE TTKGNKECYK YIINEDHNLN AQQLNNIKNL DKQDFCQKEY AYPIEKYEVD
WDNVPVDEQQ IESVDINGKT CFKYAAKRPL AYVYLNTKMT YATKTEAYDV CRMDFIGGRS
ITFRSFNNEN KDFIDQYNTN TTSKCIIDVH KNNVNTHLAI ILGITDSTVI KSLQENLSLL
SQLKQSRVTL YYLKDDSYAT DNIKLKDLKY ETLVKYTAGQ GQVDPLVNQA KNDLFKMISD
KKIKRGTMVV LMDNALGSEF NAETEFDRKN ISVHTVVLNR NKDSKITYSA LKLVSLGPHY
HEFTSNSEVS TTIDELFKGI RANLTERCDR DKCSGFCDAM NRCTCPMCCE NDCFYTSCDV
ETGSCIPWPK AKPKAKKECP ATCVGLYECK DLEGCVVTKY NASCEPKVKC MVPYCDDDNN
LKEVCKQKAN CEADQKPSSD GYCWSYTCDE TTGFCKKYKH GNLCTGKTTN CQEYVCDSEQ
RCTVQEKVCV KTSPYIEMSC YVAKCNLNTG MCENRLSCDT YSSCGGDSTG SVCKCDASTG
NQCKCNKVEN GNYCDSSKHE ICDYTGDKPK CIVSECTEDL VRDGCLIKRC NKTSKTTYWE
NVDCSNTKIE FAQDGKSETM CKPYYSATCL NGQCVVQAVG DVSNVGCGYC SMGTDNVITY
HDDCDSRKSQ CGNFNGKCQP NGDNSYSCVF EKDKTSSKSD NDICAECSSL TCPADTTYRT
YTYDSKTGTC KATVKPTPSC SVCEKGKFVE KSKDQKLERK VTLEDGKEYQ YNIPKDCVNE
QCIPRTYVDC LANDDNFGEI YKFYLPCQAY VTATYHYSSL FNLTSYKLHL PQSEEFMKEA
DKEAYCTYEI TTRECKTCSL TETKEKVEEI DLCAEETKNG GVPFKCKNNN CIIDPNFDCQ
PIECKIQEIV ITEKDGIKTT TCKDGTKTTC DTNNKRIEDA RKAFIEGKEG IEQVECASTV
CQNDNSCPII ADVEKCNQNT EVDYGCKAMT GECDGTTYLC KFVQLTDDPS LDSEHFRTKS
GVELNNACLK YKCVESKGSD GKITHKWEID TERSNIDPKP RNPCETATCD QTTGETIYTK
KTCTVSEEFP TITPNQGRCF YCQCSYLDGS SVLTMYGETD KEYYDLDACG NCRVWNQTDR
TQQLNNHTEC ILAGEINNVG AIAAATTVAV VVVAVVVALI VVSIGLFKTY QLVSSAMKNA
ITTTNENAEY VGADNEATNA ATYNG
