ID A0A182NNG6_9DIPT Unreviewed; 1242 AA.
AC A0A182NNG6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE RecName: Full=Galectin {ECO:0008006|Google:ProtNLM};
OS Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR009201-PA, ECO:0000313|Proteomes:UP000075884};
RN [1] {ECO:0000313|Proteomes:UP000075884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles dirus WRAIR2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ADIR009201-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR009201-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the formin homology family.
CC {ECO:0000256|ARBA:ARBA00023449}.
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DR AlphaFoldDB; A0A182NNG6; -.
DR STRING; 7168.A0A182NNG6; -.
DR EnsemblMetazoa; ADIR009201-RA; ADIR009201-PA; ADIR009201.
DR VEuPathDB; VectorBase:ADIR009201; -.
DR OrthoDB; 471257at2759; -.
DR Proteomes; UP000075884; Unassembled WGS sequence.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IEA:InterPro.
DR CDD; cd00070; GLECT; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR014767; DAD_dom.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR043592; FMNL_animal.
DR InterPro; IPR001079; Galectin_CRD.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR45857; FORMIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR45857:SF4; FORMIN-LIKE PROTEIN; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 2.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF00337; Gal-bind_lectin; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SMART; SM00908; Gal-bind_lectin; 1.
DR SMART; SM00276; GLECT; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51231; DAD; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51304; GALECTIN; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}.
FT DOMAIN 86..538
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 655..1055
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1062..1095
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT DOMAIN 1112..1242
FT /note="Galectin"
FT /evidence="ECO:0000259|PROSITE:PS51304"
FT REGION 223..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 449..543
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 998..1056
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 231..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..634
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1242 AA; 140086 MW; B2CBAB8A7A229D0A CRC64;
MGLASSKAVS SIAVSSHGVS AEKGSGGNGR LSKDNVIVET NYPSLSADIQ QPCSILPSPS
GSSGIDTWKT SSCHVRQASI RSRNLQPMPD AGELDRRFAK VLASMDLPPD KAKLLKNYDN
EKKWDIICDQ EMVHAKDPPA HYLTKLRTYL DPKASRSHRK RKMVGESTST QVLRDLEISL
RTNHIEWVKE FLDDENQGLD ALIDYLSFRL AMMRHEQRIL EAKSESDEGL TTKETAANSS
YGSNETNHKI APNGFMRPGL GDMLDSPSIK RRSRHIAKLN MGLTTDDIHV CIMCMRAIMN
NKYGFNMVIQ HREAINCIAL SLIHKSLRTK ALVLELLAAI CLVKGGHEII LFAFDNFKKV
CSEQRRFQTL MEYFMNYELF NIDFMVACMQ FVNIVVHSVE DMNYRVHLQY EFTALGLDEY
LEKLRLTESE ELHVQISAYL DNVFDVAALM EDSETKTAAL ERVNELEDEL GRALDQASEI
EREALFKIGE LEAELSRTRS ERDDLYNKQL VVEDEIVKLK RALKQHEQES QSRQSMLLEL
ENLTKTLPKG TSIADVSNLL AKGGLSELSP TGASSGGQQQ APPIPPPPAP PIPPSNAPMP
PPPPCPPAPP LGLTNGGGEP PKAPPKPPTF IPVPPPMGGP HGGNALHCTD GAMTIKRKVQ
PKYKLPTLNW VALKPNQVRG TIFNELDDEK LHRQIDFVDF EERFKIGMGG PVSNGNCDMD
GLTAFPSKRF KKPEHISLLE HTRLRNIAIS RRKLEMPAET VIKAINNLDL KLLSLENVEL
LQKMTPTDQE QKLYKEYVIE KKDLNQLTEE DKFMLQLTKV ERISSKLSIM NYIGNFFESW
HLISPQVYSI ISASSSIKSS KKFRAVLEVI LAFGNYLNSS KRGPAYGFKL QSLDTLLDTK
SNDKRMSLMH YIVATIRQKF PEMMNFDTEL FCIDKAAQVS LEMLISDVNE LEKGMETVRK
EADLRGKGTQ SHVLRDFLAN SEEKLKKIRT DCKTAQTCDQ ENEQRRRLEA AALQASAKKD
EEEQVVLRNN KINNQKKQQE AVINELKLKA HAVREKKLLQ QDEVYNGALE DILLGLKNEP
YRRADAVRRS QRRRIDSNRL SRTMEEVEPS PFLGLLPVGL GLYRKITIRG RMTHDMFNVN
LQVGPNVDPR DDAALHISIR PREGLIVRNT YQFRSWGVEE RFGGCPVQKK SYFDISITVK
PDSYGIAVNG CHFCDFNHRL PYASVRFIHT GVGAQIDAII TE
//
