LEG1_HAECO
ID LEG1_HAECO Reviewed; 283 AA.
AC O44126; Q86FX2; Q9NJV0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=32 kDa beta-galactoside-binding lectin;
DE AltName: Full=Galectin-1;
GN Name=GAL-1; Synonyms=Hco-gal-3b {ECO:0000303|PubMed:10717307};
OS Haemonchus contortus (Barber pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Trichostrongyloidea; Haemonchidae; Haemonchus.
OX NCBI_TaxID=6289;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=Moredun; TISSUE=Gut;
RX PubMed=10599080; DOI=10.1017/s003118209900503x;
RA Newlands G.F.J., Skuce P.J., Knox D.P., Smith S.K., Smith W.D.;
RT "Cloning and characterization of a beta-galactoside-binding protein
RT (galectin) from the gut of the gastrointestinal nematode parasite
RT Haemonchus contortus.";
RL Parasitology 119:483-490(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10717307; DOI=10.1016/s0166-6851(99)00230-3;
RA Greenhalgh C.J., Loukas A., Donald D., Nikolaou S., Newton S.E.;
RT "A family of galectins from Haemonchus contortus.";
RL Mol. Biochem. Parasitol. 107:117-121(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=17125929; DOI=10.1016/j.vetpar.2006.10.015;
RA Li C., Wei X., Xu L., Li X.;
RT "Recombinant galectins of male and female Haemonchus contortus do not
RT hemagglutinate erythrocytes of their natural host.";
RL Vet. Parasitol. 144:299-303(2007).
RN [4]
RP FUNCTION, AND INTERACTION WITH GOAT TMEM63A.
RX PubMed=25879191; DOI=10.1186/s13071-015-0816-3;
RA Yuan C., Zhang H., Wang W., Li Y., Yan R., Xu L., Song X., Li X.;
RT "Transmembrane protein 63A is a partner protein of Haemonchus contortus
RT galectin in the regulation of goat peripheral blood mononuclear cells.";
RL Parasit. Vectors 8:211-211(2015).
RN [5]
RP FUNCTION, AND INTERACTION WITH GOAT TMEM147.
RX PubMed=27337943; DOI=10.1186/s13071-016-1640-0;
RA Li Y., Yuan C., Wang L., Lu M., Wang Y., Wen Y., Yan R., Xu L., Song X.,
RA Li X.;
RT "Transmembrane protein 147 (TMEM147): another partner protein of Haemonchus
RT contortus galectin on the goat peripheral blood mononuclear cells (PBMC).";
RL Parasit. Vectors 9:355-355(2016).
RN [6]
RP FUNCTION, AND INTERACTION WITH GOAT TMEM63A AND GOAT TMEM147.
RX PubMed=28870237; DOI=10.1186/s13071-017-2353-8;
RA Lu M., Tian X., Yang X., Yuan C., Ehsan M., Liu X., Yan R., Xu L., Song X.,
RA Li X.;
RT "The N- and C-terminal carbohydrate recognition domains of Haemonchus
RT contortus galectin bind to distinct receptors of goat PBMC and contribute
RT differently to its immunomodulatory functions in host-parasite
RT interactions.";
RL Parasit. Vectors 10:409-409(2017).
CC -!- FUNCTION: Binds galactose. Exerts immunomodulatory effects on host
CC peripheral blood mononuclear cells to down-regulate host immune
CC response (PubMed:25879191, PubMed:27337943, PubMed:28870237).
CC Hemagglutinates human, dog, rabbit, chicken and mouse erythrocytes but
CC does not hemagglutinate the erythrocytes of goat, its natural host
CC (PubMed:17125929). {ECO:0000269|PubMed:17125929,
CC ECO:0000269|PubMed:25879191, ECO:0000269|PubMed:27337943,
CC ECO:0000269|PubMed:28870237}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via domain galectin 2) with
CC goat TMEM147 (PubMed:27337943, PubMed:28870237). Interacts (via domain
CC galectin 1) with goat TMEM63A (PubMed:25879191, PubMed:28870237).
CC {ECO:0000269|PubMed:25879191, ECO:0000269|PubMed:27337943,
CC ECO:0000269|PubMed:28870237}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10599080}.
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DR EMBL; AF036098; AAB88823.1; -; mRNA.
DR EMBL; AF105969; AAF63406.1; -; mRNA.
DR EMBL; AY253330; AAP05997.1; -; mRNA.
DR EMBL; AY253331; AAP05998.1; -; mRNA.
DR AlphaFoldDB; O44126; -.
DR SMR; O44126; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0032945; P:negative regulation of mononuclear cell proliferation; IDA:UniProtKB.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0001817; P:regulation of cytokine production; IDA:UniProtKB.
DR GO; GO:0032944; P:regulation of mononuclear cell proliferation; IMP:UniProtKB.
DR GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0050764; P:regulation of phagocytosis; IMP:UniProtKB.
DR CDD; cd00070; GLECT; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR044156; Galectin-like.
DR InterPro; IPR001079; Galectin_CRD.
DR PANTHER; PTHR11346; PTHR11346; 1.
DR Pfam; PF00337; Gal-bind_lectin; 2.
DR SMART; SM00908; Gal-bind_lectin; 2.
DR SMART; SM00276; GLECT; 2.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS51304; GALECTIN; 2.
PE 1: Evidence at protein level;
KW Lectin; Membrane; Repeat.
FT CHAIN 1..283
FT /note="32 kDa beta-galactoside-binding lectin"
FT /id="PRO_0000076959"
FT DOMAIN 17..148
FT /note="Galectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT DOMAIN 156..283
FT /note="Galectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT BINDING 217..223
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /evidence="ECO:0000250"
FT CONFLICT 73
FT /note="V -> I (in Ref. 2; AAF63406 and 3; AAP05997/
FT AAP05998)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="E -> G (in Ref. 3; AAP05998)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="V -> E (in Ref. 3; AAP05998)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 283 AA; 32530 MW; 84D319BF6F383750 CRC64;
MVSQFLHWYE YNKPVPYRSL LQEKIEPGQT LIVKGSTIDE SQRFTINLHS KSADFSGNDV
PLHISVRFDE GKVVMNTFAN GEWGKEERKS LPIKKGDSFD IRIRAHDDRF QIVIDQKEFK
DYEHRLPLTS ITHLSIDGDL YLNHVHWGGK YYPVPYESGI ASGFPIDKTL LIFGTVEKKA
KRFNINLLRR NGDIALHFNP RFDEKAVIRN ALAANEWGNE EREGKMPFEK GVGFDLAIKN
EAYAFQIFVN GERFTSFAHR QDPNDISGLQ IQGDIELTGI QIQ
