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Calcium-dependent cell adhesion molecule 1 (CAD-1) (DdCAD-1) (GP24)

 CAD1_DICDI              Reviewed;         213 AA.
P54657; Q23855; Q54MQ4;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
20-JUN-2018, entry version 104.
RecName: Full=Calcium-dependent cell adhesion molecule 1;
Short=CAD-1;
Short=DdCAD-1;
AltName: Full=GP24;
Name=cadA; Synonyms=cad1; ORFNames=DDB_G0285793;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-62 AND 118-133,
FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=8663243; DOI=10.1074/jbc.271.27.16399;
Wong E.F.S., Brar S.K., Sesaki H., Yang C., Siu C.-H.;
"Molecular cloning and characterization of DdCAD-1, a Ca2+-dependent
cell-cell adhesion molecule, in Dictyostelium discoideum.";
J. Biol. Chem. 271:16399-16408(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Yang C., Siu C.-H.;
"Cloning, regulation, and promoter analysis of the cadA gene in
Dictyostelium discoideum.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-193.
STRAIN=AX2;
Winckler T.;
"Cloning of a putative 25 kDa protein from Dictyostelium discoideum.";
Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
INDUCTION.
PubMed=17481898; DOI=10.1016/j.cub.2007.04.029;
Bakthavatsalam D., Brazill D., Gomer R.H., Eichinger L., Rivero F.,
Noegel A.A.;
"A G protein-coupled receptor with a lipid kinase domain is involved
in cell-density sensing.";
Curr. Biol. 17:892-897(2007).
[7]
STRUCTURE BY NMR.
PubMed=17057715; DOI=10.1038/nsmb1162;
Lin Z., Sriskanthadevan S., Huang H., Siu C.-H., Yang D.;
"Solution structures of the adhesion molecule DdCAD-1 reveal new
insights into Ca(2+)-dependent cell-cell adhesion.";
Nat. Struct. Mol. Biol. 13:1016-1022(2006).
-!- FUNCTION: Mediates calcium-dependent cell-cell adhesion during the
early stage of development. {ECO:0000269|PubMed:8663243}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-8446773, EBI-8446773;
P02599:calA; NbExp=4; IntAct=EBI-8446773, EBI-1808395;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8663243}.
Note=Associated with the ecto-surface of the plasma membrane. May
be transported to the plasma membrane via contractile vacuoles and
its cell surface association may be mediated by an integral
membrane protein.
-!- DEVELOPMENTAL STAGE: Expressed soon after the initiation of
development. {ECO:0000269|PubMed:8663243}.
-!- INDUCTION: Expression is controlled by rpkA.
{ECO:0000269|PubMed:17481898}.
-!- DOMAIN: Cell binding activity is dependent on the N-terminal
segment whereas the C-terminal domain tethers the protein to the
cell membrane.
-!- PTM: The N-terminus is blocked.
-!- SIMILARITY: Belongs to the Dictyostelium CAD family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U49650; AAC47135.1; -; mRNA.
EMBL; AF340153; AAK17205.1; -; Genomic_DNA.
EMBL; AAFI02000079; EAL64543.1; -; Genomic_DNA.
EMBL; U20997; AAA62645.1; -; mRNA.
RefSeq; XP_638048.1; XM_632956.1.
PDB; 1YHP; NMR; -; A=2-213.
PDB; 2B1O; NMR; -; A=2-213.
PDBsum; 1YHP; -.
PDBsum; 2B1O; -.
ProteinModelPortal; P54657; -.
SMR; P54657; -.
DIP; DIP-29248N; -.
IntAct; P54657; 1.
MINT; P54657; -.
PaxDb; P54657; -.
PRIDE; P54657; -.
EnsemblProtists; EAL64543; EAL64543; DDB_G0285793.
GeneID; 8625286; -.
KEGG; ddi:DDB_G0285793; -.
dictyBase; DDB_G0285793; cadA.
eggNOG; ENOG410J7U8; Eukaryota.
eggNOG; ENOG4112D7K; LUCA.
InParanoid; P54657; -.
OMA; ESEIVCQ; -.
PhylomeDB; P54657; -.
EvolutionaryTrace; P54657; -.
PRO; PR:P54657; -.
Proteomes; UP000002195; Chromosome 4.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0005938; C:cell cortex; TAS:dictyBase.
GO; GO:0005911; C:cell-cell junction; IDA:dictyBase.
GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
GO; GO:0030139; C:endocytic vesicle; IDA:dictyBase.
GO; GO:0009897; C:external side of plasma membrane; IDA:dictyBase.
GO; GO:0030175; C:filopodium; IDA:dictyBase.
GO; GO:0030027; C:lamellipodium; IDA:dictyBase.
GO; GO:0005811; C:lipid droplet; HDA:dictyBase.
GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
GO; GO:0001726; C:ruffle; IDA:dictyBase.
GO; GO:0031982; C:vesicle; IDA:dictyBase.
GO; GO:0005509; F:calcium ion binding; IDA:dictyBase.
GO; GO:0005516; F:calmodulin binding; IPI:dictyBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; IDA:dictyBase.
GO; GO:0031152; P:aggregation involved in sorocarp development; TAS:dictyBase.
GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:dictyBase.
GO; GO:0010468; P:regulation of gene expression; IDA:dictyBase.
GO; GO:1904643; P:response to curcumin; IDA:dictyBase.
GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
Gene3D; 2.60.40.1720; -; 1.
InterPro; IPR015059; Ca_cell_adhesion_N_dom.
InterPro; IPR038423; CAD_C_sf.
InterPro; IPR011024; G_crystallin-like.
InterPro; IPR029283; Membrane-bd.
Pfam; PF08964; Crystall_3; 1.
Pfam; PF14564; Membrane_bind; 1.
SUPFAM; SSF49695; SSF49695; 1.
1: Evidence at protein level;
3D-structure; Calcium; Cell adhesion; Cell membrane;
Complete proteome; Direct protein sequencing; Membrane;
Reference proteome; Repeat.
CHAIN 1 213 Calcium-dependent cell adhesion molecule
1.
/FTId=PRO_0000089273.
REPEAT 1 48 1.
REPEAT 49 97 2.
REPEAT 98 146 3.
REPEAT 147 194 4.
REGION 1 194 4 X approximate tandem repeats.
STRAND 8 13 {ECO:0000244|PDB:1YHP}.
TURN 14 16 {ECO:0000244|PDB:1YHP}.
STRAND 20 23 {ECO:0000244|PDB:1YHP}.
STRAND 25 30 {ECO:0000244|PDB:1YHP}.
HELIX 36 39 {ECO:0000244|PDB:1YHP}.
STRAND 43 46 {ECO:0000244|PDB:1YHP}.
STRAND 51 56 {ECO:0000244|PDB:1YHP}.
STRAND 68 71 {ECO:0000244|PDB:1YHP}.
STRAND 73 78 {ECO:0000244|PDB:1YHP}.
HELIX 81 83 {ECO:0000244|PDB:1YHP}.
STRAND 87 92 {ECO:0000244|PDB:1YHP}.
STRAND 97 108 {ECO:0000244|PDB:1YHP}.
STRAND 115 121 {ECO:0000244|PDB:1YHP}.
STRAND 127 134 {ECO:0000244|PDB:1YHP}.
STRAND 136 140 {ECO:0000244|PDB:1YHP}.
STRAND 150 160 {ECO:0000244|PDB:1YHP}.
STRAND 165 176 {ECO:0000244|PDB:1YHP}.
TURN 177 180 {ECO:0000244|PDB:1YHP}.
STRAND 181 185 {ECO:0000244|PDB:1YHP}.
TURN 188 190 {ECO:0000244|PDB:1YHP}.
STRAND 193 201 {ECO:0000244|PDB:1YHP}.
STRAND 204 209 {ECO:0000244|PDB:1YHP}.
SEQUENCE 213 AA; 23926 MW; FEE35BA62236293C CRC64;
MSVDANKVKF FFGKNCTGES FEYNKGETVR FNNGDKWNDK FMSCLVGSNV RCNIWEHNEI
DTPTPGKFQE LAQGSTNNDL TSINGLSKFQ VLPGAFQWAV DVKIVNKVNS TAGSYEMTIT
PYQVDKVACK DGDDFVQLPI PKLTPPDSEI VSHLTVRQTH TPYDYVVNGS VYFKYSPTTG
QVTVIKKDET FPKNMTVTQD DNTSFIFNLN SEK


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