DIS2_DICDI
ID DIS2_DICDI Reviewed; 257 AA.
AC P42530; Q54CX1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Discoidin-2;
DE AltName: Full=Discoidin II;
GN Name=dscE; ORFNames=DDB_G0292552;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=AX2;
RX PubMed=8759914; DOI=10.1093/oxfordjournals.pcp.a028973;
RA Fukuzawa M., Ochiai H.;
RT "Molecular cloning and characterization of the cDNA for discoidin II of
RT Dictyostelium discoideum.";
RL Plant Cell Physiol. 37:505-514(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) ALONE AND IN COMPLEX WITH
RP MONOSACCHARIDES, SUBUNIT, CALCIUM-BINDING SITES, AND PHOSPHORYLATION AT
RP HIS-84.
RX PubMed=18384150; DOI=10.1002/prot.22038;
RA Aragao K.S., Satre M., Imberty A., Varrot A.;
RT "Structure determination of Discoidin II from Dictyostelium discoideum and
RT carbohydrate binding properties of the lectin domain.";
RL Proteins 73:43-52(2008).
CC -!- FUNCTION: Galactose-binding lectin. May be necessary for the primary
CC process of spore formation and may be involved in spore coat formation.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:18384150}.
CC -!- TISSUE SPECIFICITY: Maturing spore cells.
CC -!- DEVELOPMENTAL STAGE: Levels increase around 8 hours of development to
CC reach maximal levels at 16 hours and a high expression is maintained
CC during later development.
CC -!- PTM: The N-terminus is blocked.
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DR EMBL; D29628; BAA06107.1; -; mRNA.
DR EMBL; AAFI02000194; EAL61079.1; -; Genomic_DNA.
DR RefSeq; XP_629549.1; XM_629547.1.
DR PDB; 2VM9; X-ray; 1.75 A; A=1-257.
DR PDB; 2VMC; X-ray; 1.90 A; A=1-257.
DR PDB; 2VMD; X-ray; 1.90 A; A=1-257.
DR PDB; 2VME; X-ray; 2.45 A; A/B/C/D/E/F=1-257.
DR PDBsum; 2VM9; -.
DR PDBsum; 2VMC; -.
DR PDBsum; 2VMD; -.
DR PDBsum; 2VME; -.
DR AlphaFoldDB; P42530; -.
DR SMR; P42530; -.
DR STRING; 44689.DDB0215382; -.
DR UniLectin; P42530; -.
DR iPTMnet; P42530; -.
DR PaxDb; P42530; -.
DR EnsemblProtists; EAL61079; EAL61079; DDB_G0292552.
DR GeneID; 8628807; -.
DR KEGG; ddi:DDB_G0292552; -.
DR dictyBase; DDB_G0292552; dscE.
DR eggNOG; KOG2649; Eukaryota.
DR HOGENOM; CLU_1100181_0_0_1; -.
DR InParanoid; P42530; -.
DR OMA; DNGQMRW; -.
DR PhylomeDB; P42530; -.
DR EvolutionaryTrace; P42530; -.
DR PRO; PR:P42530; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0098636; C:protein complex involved in cell adhesion; IBA:GO_Central.
DR GO; GO:0031160; C:spore wall; IDA:dictyBase.
DR GO; GO:0031982; C:vesicle; IDA:dictyBase.
DR GO; GO:0030246; F:carbohydrate binding; IDA:dictyBase.
DR GO; GO:0016936; F:galactoside binding; IDA:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046871; F:N-acetylgalactosamine binding; IDA:dictyBase.
DR GO; GO:0070492; F:oligosaccharide binding; IDA:dictyBase.
DR GO; GO:0030247; F:polysaccharide binding; IDA:dictyBase.
DR GO; GO:0007155; P:cell adhesion; IDA:dictyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:dictyBase.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR CDD; cd00057; FA58C; 1.
DR Gene3D; 2.60.40.2080; -; 1.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR037221; H-type_lectin_dom_sf.
DR InterPro; IPR019019; H-type_lectin_domain.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF09458; H_lectin; 1.
DR SMART; SM00231; FA58C; 1.
DR SUPFAM; SSF141086; SSF141086; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Direct protein sequencing; Lectin;
KW Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..257
FT /note="Discoidin-2"
FT /id="PRO_0000079914"
FT DOMAIN 10..154
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REGION 1..155
FT /note="Beta-sandwich"
FT REGION 156..162
FT /note="Linker"
FT REGION 163..257
FT /note="Lectin-like"
FT MOTIF 81..83
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 209
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 218
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 238
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT MOD_RES 84
FT /note="Phosphohistidine"
FT /evidence="ECO:0000305|PubMed:18384150"
FT TURN 10..14
FT /evidence="ECO:0007829|PDB:2VM9"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:2VM9"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:2VM9"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:2VM9"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:2VM9"
FT STRAND 63..79
FT /evidence="ECO:0007829|PDB:2VM9"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:2VM9"
FT STRAND 87..100
FT /evidence="ECO:0007829|PDB:2VM9"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:2VM9"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:2VM9"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:2VM9"
FT STRAND 121..144
FT /evidence="ECO:0007829|PDB:2VM9"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:2VM9"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:2VM9"
FT STRAND 180..190
FT /evidence="ECO:0007829|PDB:2VM9"
FT STRAND 200..210
FT /evidence="ECO:0007829|PDB:2VM9"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:2VM9"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:2VM9"
FT STRAND 243..254
FT /evidence="ECO:0007829|PDB:2VM9"
SQ SEQUENCE 257 AA; 28575 MW; DA59AFFC98FE3E19 CRC64;
MSVPAGSVSC LANALLNLRS STDYNADHGV KNSILNFSNS KDASRFDGSE SWSSSVLDKN
QFIVAGSDSV KHFVAISTQG RGDHDQWVTS YKLRYTLDNV NWVEYNNGEI INANKDRNSI
VTINFNPPIK ARSIAIHPQT YNNHISLRWE LYALPVKSYS NPSVQVGEVS IGDRSLNSGT
GSRTIVRHVK FPVEFLSVPI VSIGCKKVDA HTDNGQMRWE GKSENITTKG FDLTFITWGN
NAVYDLTFDY VAVEFNN
