DIS1A_DICDI
ID DIS1A_DICDI Reviewed; 253 AA.
AC P02886; Q556P5; Q86AL3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Discoidin-1 subunit A;
DE AltName: Full=Discoidin-1 subunit alpha;
DE Short=Discoidin I chain A;
GN Name=dscA-1; ORFNames=DDB_G0273063;
GN and
GN Name=dscA-2; ORFNames=DDB_G0273919;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6279874; DOI=10.1016/0022-2836(81)90278-3;
RA Poole S., Firtel R.A., Lamar E., Rowekamp W.;
RT "Sequence and expression of the discoidin I gene family in Dictyostelium
RT discoideum.";
RL J. Mol. Biol. 153:273-289(1981).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=6754951; DOI=10.1016/0022-2836(82)90104-8;
RA Jellinghaus U., Schaetzle U., Schmid W., Rowekamp W.;
RT "Transcription of a dictyostelium discoidin-I gene in yeast alternative
RT promoter sites used in two different eukaryotic cells.";
RL J. Mol. Biol. 159:623-636(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
RX PubMed=6284373; DOI=10.1016/0092-8674(82)90058-7;
RA Devine J.M., Tsang A.S., Williams J.G.;
RT "Differential expression of the members of the discoidin I multigene family
RT during growth and development of Dictyostelium discoideum.";
RL Cell 28:793-800(1982).
RN [6]
RP CELL ATTACHMENT SITE.
RX PubMed=6509552; DOI=10.1016/0092-8674(84)90462-8;
RA Springer W.R., Cooper D.N.W., Barondes S.H.;
RT "Discoidin I is implicated in cell-substratum attachment and ordered cell
RT migration of Dictyostelium discoideum and resembles fibronectin.";
RL Cell 39:557-564(1984).
RN [7]
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).
CC -!- FUNCTION: Galactose- and N-acetylgalactosamine-binding lectin. May play
CC a role in cell-substratum adhesion rather than in cell-cell adhesion.
CC May be necessary for the maintenance of normal elongate morphology
CC during aggregation.
CC -!- SUBUNIT: Tetramer of four different chains (A to D).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Stalk cells.
CC -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC AX4. These strains contain a duplication of a segment of 750 kb of
CC chromosome 2 compared to the corresponding sequence in strain AX2.
CC {ECO:0000305}.
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DR EMBL; J01282; AAA33197.1; -; Genomic_DNA.
DR EMBL; AAFI02000011; EAL70650.1; -; Genomic_DNA.
DR EMBL; AAFI02000009; EAL70749.1; -; Genomic_DNA.
DR RefSeq; XP_644576.1; XM_639484.1.
DR RefSeq; XP_644675.1; XM_639583.1.
DR PDB; 2W94; X-ray; 1.80 A; A/B/C=1-253.
DR PDB; 2W95; X-ray; 1.75 A; A/B/C=1-253.
DR PDB; 2WN2; X-ray; 1.82 A; A/B/C=1-253.
DR PDB; 2WN3; X-ray; 1.59 A; A/B/C=1-253.
DR PDBsum; 2W94; -.
DR PDBsum; 2W95; -.
DR PDBsum; 2WN2; -.
DR PDBsum; 2WN3; -.
DR AlphaFoldDB; P02886; -.
DR SMR; P02886; -.
DR UniLectin; P02886; -.
DR PaxDb; P02886; -.
DR ABCD; P02886; 1 sequenced antibody.
DR EnsemblProtists; EAL70650; EAL70650; DDB_G0273919.
DR EnsemblProtists; EAL70749; EAL70749; DDB_G0273063.
DR GeneID; 8618769; -.
DR GeneID; 8619207; -.
DR KEGG; ddi:DDB_G0273063; -.
DR KEGG; ddi:DDB_G0273919; -.
DR dictyBase; DDB_G0273063; dscA-1.
DR dictyBase; DDB_G0273919; dscA-2.
DR eggNOG; KOG3516; Eukaryota.
DR HOGENOM; CLU_1100181_0_0_1; -.
DR InParanoid; P02886; -.
DR OMA; GHISLRC; -.
DR PhylomeDB; P02886; -.
DR EvolutionaryTrace; P02886; -.
DR PRO; PR:P02886; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0009986; C:cell surface; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0031012; C:extracellular matrix; IDA:dictyBase.
DR GO; GO:0097708; C:intracellular vesicle; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0098636; C:protein complex involved in cell adhesion; IDA:dictyBase.
DR GO; GO:0106139; C:symbiont cell surface; IDA:dictyBase.
DR GO; GO:0030246; F:carbohydrate binding; IDA:dictyBase.
DR GO; GO:1990458; F:lipooligosaccharide binding; IDA:dictyBase.
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:0031589; P:cell-substrate adhesion; IDA:dictyBase.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0106136; P:lectin-induced modified bacterial internalization; IDA:dictyBase.
DR GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR GO; GO:1902168; P:response to catechin; IDA:dictyBase.
DR GO; GO:1904643; P:response to curcumin; IDA: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 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; Acetylation; Cell adhesion; Cytoplasm; Lectin;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..253
FT /note="Discoidin-1 subunit A"
FT /id="PRO_0000079915"
FT DOMAIN 2..152
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT MOTIF 79..81
FT /note="Cell attachment site"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250"
FT CONFLICT 98
FT /note="V -> L (in Ref. 1; AAA33197)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="A -> P (in Ref. 1; AAA33197)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="R -> P (in Ref. 1; AAA33197)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:2WN3"
FT TURN 9..13
FT /evidence="ECO:0007829|PDB:2WN3"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:2WN3"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:2WN3"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:2WN3"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:2WN3"
FT STRAND 61..77
FT /evidence="ECO:0007829|PDB:2WN3"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2WN3"
FT STRAND 85..99
FT /evidence="ECO:0007829|PDB:2WN3"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:2WN3"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:2WN3"
FT STRAND 119..142
FT /evidence="ECO:0007829|PDB:2WN3"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:2WN3"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:2WN3"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2WN3"
FT STRAND 177..187
FT /evidence="ECO:0007829|PDB:2WN3"
FT STRAND 197..208
FT /evidence="ECO:0007829|PDB:2WN3"
FT STRAND 213..222
FT /evidence="ECO:0007829|PDB:2WN3"
FT STRAND 225..234
FT /evidence="ECO:0007829|PDB:2WN3"
FT STRAND 239..252
FT /evidence="ECO:0007829|PDB:2WN3"
SQ SEQUENCE 253 AA; 28259 MW; 9120E828FC9BD8A4 CRC64;
MSTQGLVQLL ANAQCHLRTS TNYNGVHTQF NSALNYKNNG TNTIDGSEAW CSSIVDTNQY
IVAGCEVPRT FMCVALQGRG DADQWVTSYK IRYSLDNVSW FEYRNGAAVT GVTDRNTVVN
HFFDTPIRAR SIAIHPLTWN GHISLRCEFY TQPVQSSVTQ VGADIYTGDN CALNTGSGKR
EVVVPVKFQF EFATLPKVAL NFDQIDCTDA TNQTRIGVQP RNITTKGFDC VFYTWNENKV
YSLRADYIAT ALE
