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Discoidin-1 subunit A (Discoidin-1 subunit alpha) (Discoidin I chain A)

 DIS1A_DICDI             Reviewed;         253 AA.
P02886; Q556P5; Q86AL3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 3.
18-JUL-2018, entry version 123.
RecName: Full=Discoidin-1 subunit A;
AltName: Full=Discoidin-1 subunit alpha;
Short=Discoidin I chain A;
Name=dscA-1; ORFNames=DDB_G0273063;
and
Name=dscA-2; ORFNames=DDB_G0273919;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6279874; DOI=10.1016/0022-2836(81)90278-3;
Poole S., Firtel R.A., Lamar E., Rowekamp W.;
"Sequence and expression of the discoidin I gene family in
Dictyostelium discoideum.";
J. Mol. Biol. 153:273-289(1981).
[2]
SEQUENCE REVISION.
PubMed=6754951; DOI=10.1016/0022-2836(82)90104-8;
Jellinghaus U., Schaetzle U., Schmid W., Rowekamp W.;
"Transcription of a dictyostelium discoidin-I gene in yeast
alternative promoter sites used in two different eukaryotic cells.";
J. Mol. Biol. 159:623-636(1982).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=12097910; DOI=10.1038/nature00847;
Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A.,
Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G.,
Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A.,
Platzer M., Rosenthal A., Noegel A.A.;
"Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
Nature 418:79-85(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
PubMed=6284373; DOI=10.1016/0092-8674(82)90058-7;
Devine J.M., Tsang A.S., Williams J.G.;
"Differential expression of the members of the discoidin I multigene
family during growth and development of Dictyostelium discoideum.";
Cell 28:793-800(1982).
[6]
CELL ATTACHMENT SITE.
PubMed=6509552; DOI=10.1016/0092-8674(84)90462-8;
Springer W.R., Cooper D.N.W., Barondes S.H.;
"Discoidin I is implicated in cell-substratum attachment and ordered
cell migration of Dictyostelium discoideum and resembles
fibronectin.";
Cell 39:557-564(1984).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=AX2;
PubMed=16926386; DOI=10.1074/mcp.M600113-MCP200;
Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
Soldati T.;
"Proteomics fingerprinting of phagosome maturation and evidence for
the role of a Galpha during uptake.";
Mol. Cell. Proteomics 5:2228-2243(2006).
-!- FUNCTION: Galactose- and N-acetylgalactosamine-binding lectin. May
play a role in cell-substratum adhesion rather than in cell-cell
adhesion. May be necessary for the maintenance of normal elongate
morphology during aggregation.
-!- SUBUNIT: Tetramer of four different chains (A to D).
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Stalk cells.
-!- CAUTION: The gene for this protein is duplicated in strains AX3
and AX4. These strains contain a duplication of a segment of 750
kb of chromosome 2 compared to the corresponding sequence in
strain AX2. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J01282; AAA33197.1; -; Genomic_DNA.
EMBL; AAFI02000011; EAL70650.1; -; Genomic_DNA.
EMBL; AAFI02000009; EAL70749.1; -; Genomic_DNA.
RefSeq; XP_644576.1; XM_639484.1.
RefSeq; XP_644675.1; XM_639583.1.
PDB; 2W94; X-ray; 1.80 A; A/B/C=1-253.
PDB; 2W95; X-ray; 1.75 A; A/B/C=1-253.
PDB; 2WN2; X-ray; 1.82 A; A/B/C=1-253.
PDB; 2WN3; X-ray; 1.59 A; A/B/C=1-253.
PDBsum; 2W94; -.
PDBsum; 2W95; -.
PDBsum; 2WN2; -.
PDBsum; 2WN3; -.
ProteinModelPortal; P02886; -.
SMR; P02886; -.
STRING; 44689.DDB0266623; -.
UniLectin; P02886; -.
PaxDb; P02886; -.
PRIDE; P02886; -.
EnsemblProtists; EAL70650; EAL70650; DDB_G0273919.
EnsemblProtists; EAL70749; EAL70749; DDB_G0273063.
GeneID; 8618769; -.
GeneID; 8619207; -.
KEGG; ddi:DDB_G0273063; -.
KEGG; ddi:DDB_G0273919; -.
dictyBase; DDB_G0273063; dscA-1.
dictyBase; DDB_G0273919; dscA-2.
InParanoid; P02886; -.
OMA; GHISLRC; -.
PhylomeDB; P02886; -.
EvolutionaryTrace; P02886; -.
PRO; PR:P02886; -.
Proteomes; UP000002195; Chromosome 2.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0009986; C:cell surface; IDA:dictyBase.
GO; GO:0031012; C:extracellular matrix; IDA:dictyBase.
GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
GO; GO:0098636; C:protein complex involved in cell adhesion; IDA:dictyBase.
GO; GO:0046871; F:N-acetylgalactosamine binding; IDA:dictyBase.
GO; GO:0070492; F:oligosaccharide binding; IDA:dictyBase.
GO; GO:0030247; F:polysaccharide binding; IDA:dictyBase.
GO; GO:0007155; P:cell adhesion; IDA:dictyBase.
GO; GO:0098609; P:cell-cell adhesion; IDA:dictyBase.
GO; GO:0007010; P:cytoskeleton organization; TAS:dictyBase.
GO; GO:0051262; P:protein tetramerization; IDA:dictyBase.
GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
GO; GO:1902168; P:response to catechin; IDA:dictyBase.
GO; GO:1904643; P:response to curcumin; IDA:dictyBase.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.40.2080; -; 1.
InterPro; IPR000421; FA58C.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR037221; H-type_lectin_dom_sf.
InterPro; IPR019019; H-type_lectin_domain.
Pfam; PF00754; F5_F8_type_C; 1.
Pfam; PF09458; H_lectin; 1.
SUPFAM; SSF141086; SSF141086; 1.
SUPFAM; SSF49785; SSF49785; 1.
PROSITE; PS01285; FA58C_1; 1.
PROSITE; PS50022; FA58C_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell adhesion; Complete proteome;
Cytoplasm; Lectin; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250}.
CHAIN 2 253 Discoidin-1 subunit A.
/FTId=PRO_0000079915.
DOMAIN 2 152 F5/8 type C. {ECO:0000255|PROSITE-
ProRule:PRU00081}.
MOTIF 79 81 Cell attachment site.
MOD_RES 2 2 N-acetylserine. {ECO:0000250}.
CONFLICT 98 98 V -> L (in Ref. 1; AAA33197).
{ECO:0000305}.
CONFLICT 107 107 A -> P (in Ref. 1; AAA33197).
{ECO:0000305}.
CONFLICT 130 130 R -> P (in Ref. 1; AAA33197).
{ECO:0000305}.
STRAND 6 8 {ECO:0000244|PDB:2WN3}.
TURN 9 13 {ECO:0000244|PDB:2WN3}.
STRAND 15 20 {ECO:0000244|PDB:2WN3}.
HELIX 29 31 {ECO:0000244|PDB:2WN3}.
HELIX 43 45 {ECO:0000244|PDB:2WN3}.
STRAND 48 51 {ECO:0000244|PDB:2WN3}.
STRAND 61 77 {ECO:0000244|PDB:2WN3}.
STRAND 80 83 {ECO:0000244|PDB:2WN3}.
STRAND 85 99 {ECO:0000244|PDB:2WN3}.
HELIX 103 106 {ECO:0000244|PDB:2WN3}.
STRAND 113 116 {ECO:0000244|PDB:2WN3}.
STRAND 119 142 {ECO:0000244|PDB:2WN3}.
STRAND 144 151 {ECO:0000244|PDB:2WN3}.
STRAND 157 166 {ECO:0000244|PDB:2WN3}.
HELIX 172 174 {ECO:0000244|PDB:2WN3}.
STRAND 177 187 {ECO:0000244|PDB:2WN3}.
STRAND 197 208 {ECO:0000244|PDB:2WN3}.
STRAND 213 222 {ECO:0000244|PDB:2WN3}.
STRAND 225 234 {ECO:0000244|PDB:2WN3}.
STRAND 239 252 {ECO:0000244|PDB:2WN3}.
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


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