DIS1D_DICDI
ID DIS1D_DICDI Reviewed; 253 AA.
AC P02888; Q556R1; Q86AK9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Discoidin-1 subunit D;
DE AltName: Full=Discoidin-1 subunit delta;
DE Short=Discoidin I chain D;
GN Name=dscD-1; ORFNames=DDB_G0273067;
GN and
GN Name=dscD-2; ORFNames=DDB_G0273887;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-149.
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 [4]
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 [5]
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; AAFI02000011; EAL70634.1; -; Genomic_DNA.
DR EMBL; AAFI02000009; EAL70751.1; -; Genomic_DNA.
DR EMBL; J01285; AAA33200.1; -; Genomic_DNA.
DR PIR; A03383; DLDOID.
DR RefSeq; XP_644560.1; XM_639468.1.
DR RefSeq; XP_644691.1; XM_639599.1.
DR AlphaFoldDB; P02888; -.
DR SMR; P02888; -.
DR PaxDb; P02888; -.
DR EnsemblProtists; EAL70634; EAL70634; DDB_G0273887.
DR EnsemblProtists; EAL70751; EAL70751; DDB_G0273067.
DR GeneID; 8618788; -.
DR GeneID; 8619188; -.
DR KEGG; ddi:DDB_G0273067; -.
DR KEGG; ddi:DDB_G0273887; -.
DR dictyBase; DDB_G0273067; dscD-1.
DR dictyBase; DDB_G0273887; dscD-2.
DR eggNOG; KOG3516; Eukaryota.
DR HOGENOM; CLU_1100181_0_0_1; -.
DR InParanoid; P02888; -.
DR OMA; WCASVVD; -.
DR PhylomeDB; P02888; -.
DR PRO; PR:P02888; -.
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; HDA:dictyBase.
DR GO; GO:0098636; C:protein complex involved in cell adhesion; IDA:dictyBase.
DR GO; GO:0030246; F:carbohydrate binding; IDA:dictyBase.
DR GO; GO:0046871; F:N-acetylgalactosamine binding; IDA:dictyBase.
DR GO; GO:0070492; F:oligosaccharide binding; IBA:GO_Central.
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 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 Acetylation; Cell adhesion; Cytoplasm; Lectin; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..253
FT /note="Discoidin-1 subunit D"
FT /id="PRO_0000079918"
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"
SQ SEQUENCE 253 AA; 28307 MW; 3C91D5E8A9E5E81F CRC64;
MSTQGLVTLL GNAQCHLRTS TNYNGVHTQF NAALNYKNKG TNTIDGSEAW CSSIVDTNQY
IVAGCEVPRT FMCVALQGRG DHDQWVTSYK IRYSLDNVTW SEYRNGAAIT GVTDRNTVVN
HFFDTPIRAR SIAIHPLTWN NHISLRCEFY TQPVQSSVTQ VGADIYTGDN CALNTGSGKR
EVVVPVKFQF EFATLPKVAL NFDQIDCTDA TNQTRIGVQP RNITTKGFDC VFYTWNENKV
YSLRADYIAT ALE
