ID   DIS1B_DICDI             Reviewed;         253 AA.
AC   P02887; Q556R2;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   02-SEP-2026, entry version 160.
DE   RecName: Full=Discoidin-1 subunit B/C;
DE   AltName: Full=Discoidin I chain C/D;
DE   AltName: Full=Discoidin-1 subunit beta/gamma;
GN   Name=dscC-1; Synonyms=dscB-1; ORFNames=DDB_G0273065;
GN   and
GN   Name=dscC-2; Synonyms=dscB-2; ORFNames=DDB_G0273885;
OS   Dictyostelium discoideum (Social amoeba).
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   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   [3]
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   [4]
RP   PROTEIN SEQUENCE OF 2-18; 70-79; 105-128; 131-146 AND 188-197, CLEAVAGE OF
RP   INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RA   Bienvenut W.V., Patel H., Brunton V.G., Frame M.C.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [5]
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   [6]
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; J01284; AAA33199.1; -; Genomic_DNA.
DR   EMBL; J01283; AAA33198.1; -; Genomic_DNA.
DR   EMBL; AAFI02000011; EAL70633.1; -; Genomic_DNA.
DR   EMBL; AAFI02000009; EAL70750.1; -; Genomic_DNA.
DR   PIR; A03382; DLDOIC.
DR   PIR; B03382; B03382.
DR   RefSeq; XP_644559.1; XM_639467.1.
DR   RefSeq; XP_644692.1; XM_639600.1.
DR   AlphaFoldDB; P02887; -.
DR   SMR; P02887; -.
DR   ELM; P02887; -.
DR   FunCoup; P02887; 6.
DR   PaxDb; 44689-P02887; -.
DR   GeneID; 8618789; -.
DR   GeneID; 8619187; -.
DR   KEGG; ddi:DDB_G0273065; -.
DR   KEGG; ddi:DDB_G0273885; -.
DR   dictyBase; DDB_G0273065; dscC-1.
DR   dictyBase; DDB_G0273885; dscC-2.
DR   VEuPathDB; AmoebaDB:DDB_G0273885; -.
DR   eggNOG; KOG3516; Eukaryota.
DR   HOGENOM; CLU_1100181_0_0_1; -.
DR   InParanoid; P02887; -.
DR   OMA; IDCANDK; -.
DR   PhylomeDB; P02887; -.
DR   PRO; PR:P02887; -.
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   GO; GO:0051591; P:response to cAMP; IDA:dictyBase.
DR   GO; GO:0051593; P:response to folic acid; IDA:dictyBase.
DR   GO; GO:0009416; P:response to light stimulus; IDA:dictyBase.
DR   CDD; cd00057; FA58C; 1.
DR   FunFam; 2.60.120.260:FF:000016; Contactin-associated protein-like 4 isoform 1; 1.
DR   FunFam; 2.60.40.2080:FF:000001; Discoidin-1 subunit A; 1.
DR   Gene3D; 2.60.40.2080; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR052487; Galactose-binding_lectin.
DR   InterPro; IPR037221; H-type_lectin_dom_sf.
DR   InterPro; IPR019019; H-type_lectin_domain.
DR   PANTHER; PTHR46938:SF1; DISCOIDIN-1 SUBUNIT A-RELATED; 1.
DR   PANTHER; PTHR46938; DISCOIDIN-1 SUBUNIT A-RELATED-RELATED; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF09458; H_lectin; 1.
DR   SMART; SM00231; FA58C; 1.
DR   SUPFAM; SSF141086; Agglutinin HPA-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS01285; FA58C_1; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell adhesion; Cytoplasm; Direct protein sequencing; Lectin;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CHAIN           2..253
FT                   /note="Discoidin-1 subunit B/C"
FT                   /id="PRO_0000079917"
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:0000269|Ref.4"
SQ   SEQUENCE   253 AA;  28392 MW;  875EA94811F85444 CRC64;
     MSTQGLVQLI SNAQCHLRTS TNYNDVHTQF NAVLNYKNKG TNTIDGSEAW CSSIVDTNQY
     IVAGCEVPRT FMCVALQGRG DHDQWVTSYK IRYSLDNVTW SEYRNGAAIT GVTDRNTVVN
     HFFDTPIRAR SIAIHPLTWN NHISLRCEFY TQPVQSSVTQ VGADIYTGDN CALNTGSGKR
     EVVVPVKFQF EFATLPKVAL NFDQIDCTDA TNQTRIGVQP RNITTKGFDC VFYTWNANKV
     YSLRADYIAT ALE
//