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CAD1_DICDI
ID   CAD1_DICDI              Reviewed;         213 AA.
AC   P54657; Q23855; Q54MQ4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Calcium-dependent cell adhesion molecule 1;
DE            Short=CAD-1;
DE            Short=DdCAD-1;
DE   AltName: Full=GP24;
GN   Name=cadA; Synonyms=cad1; ORFNames=DDB_G0285793;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-62 AND 118-133,
RP   FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=8663243; DOI=10.1074/jbc.271.27.16399;
RA   Wong E.F.S., Brar S.K., Sesaki H., Yang C., Siu C.-H.;
RT   "Molecular cloning and characterization of DdCAD-1, a Ca2+-dependent cell-
RT   cell adhesion molecule, in Dictyostelium discoideum.";
RL   J. Biol. Chem. 271:16399-16408(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Yang C., Siu C.-H.;
RT   "Cloning, regulation, and promoter analysis of the cadA gene in
RT   Dictyostelium discoideum.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
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   NUCLEOTIDE SEQUENCE [MRNA] OF 4-193.
RC   STRAIN=AX2;
RA   Winckler T.;
RT   "Cloning of a putative 25 kDa protein from Dictyostelium discoideum.";
RL   Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
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).
RN   [6]
RP   INDUCTION.
RX   PubMed=17481898; DOI=10.1016/j.cub.2007.04.029;
RA   Bakthavatsalam D., Brazill D., Gomer R.H., Eichinger L., Rivero F.,
RA   Noegel A.A.;
RT   "A G protein-coupled receptor with a lipid kinase domain is involved in
RT   cell-density sensing.";
RL   Curr. Biol. 17:892-897(2007).
RN   [7]
RP   STRUCTURE BY NMR.
RX   PubMed=17057715; DOI=10.1038/nsmb1162;
RA   Lin Z., Sriskanthadevan S., Huang H., Siu C.-H., Yang D.;
RT   "Solution structures of the adhesion molecule DdCAD-1 reveal new insights
RT   into Ca(2+)-dependent cell-cell adhesion.";
RL   Nat. Struct. Mol. Biol. 13:1016-1022(2006).
CC   -!- FUNCTION: Mediates calcium-dependent cell-cell adhesion during the
CC       early stage of development. {ECO:0000269|PubMed:8663243}.
CC   -!- INTERACTION:
CC       P54657; P54657: cadA; NbExp=2; IntAct=EBI-8446773, EBI-8446773;
CC       P54657; P02599: calA; NbExp=4; IntAct=EBI-8446773, EBI-1808395;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8663243}.
CC       Note=Associated with the ecto-surface of the plasma membrane. May be
CC       transported to the plasma membrane via contractile vacuoles and its
CC       cell surface association may be mediated by an integral membrane
CC       protein.
CC   -!- DEVELOPMENTAL STAGE: Expressed soon after the initiation of
CC       development. {ECO:0000269|PubMed:8663243}.
CC   -!- INDUCTION: Expression is controlled by rpkA.
CC       {ECO:0000269|PubMed:17481898}.
CC   -!- DOMAIN: Cell binding activity is dependent on the N-terminal segment
CC       whereas the C-terminal domain tethers the protein to the cell membrane.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the Dictyostelium CAD family. {ECO:0000305}.
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DR   EMBL; U49650; AAC47135.1; -; mRNA.
DR   EMBL; AF340153; AAK17205.1; -; Genomic_DNA.
DR   EMBL; AAFI02000079; EAL64543.1; -; Genomic_DNA.
DR   EMBL; U20997; AAA62645.1; -; mRNA.
DR   RefSeq; XP_638048.1; XM_632956.1.
DR   PDB; 1YHP; NMR; -; A=2-213.
DR   PDB; 2B1O; NMR; -; A=2-213.
DR   PDBsum; 1YHP; -.
DR   PDBsum; 2B1O; -.
DR   AlphaFoldDB; P54657; -.
DR   BMRB; P54657; -.
DR   SMR; P54657; -.
DR   BioGRID; 1250289; 1.
DR   DIP; DIP-29248N; -.
DR   IntAct; P54657; 1.
DR   MINT; P54657; -.
DR   STRING; 44689.DDB0191175; -.
DR   PaxDb; P54657; -.
DR   EnsemblProtists; EAL64543; EAL64543; DDB_G0285793.
DR   GeneID; 8625286; -.
DR   KEGG; ddi:DDB_G0285793; -.
DR   dictyBase; DDB_G0285793; cadA.
DR   eggNOG; ENOG502SGUC; Eukaryota.
DR   HOGENOM; CLU_1362582_0_0_1; -.
DR   InParanoid; P54657; -.
DR   OMA; ESEIVCQ; -.
DR   PhylomeDB; P54657; -.
DR   EvolutionaryTrace; P54657; -.
DR   PRO; PR:P54657; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005938; C:cell cortex; TAS:dictyBase.
DR   GO; GO:0005911; C:cell-cell junction; IDA:dictyBase.
DR   GO; GO:0000331; C:contractile vacuole; IDA:dictyBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR   GO; GO:0030139; C:endocytic vesicle; IDA:dictyBase.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:dictyBase.
DR   GO; GO:0031012; C:extracellular matrix; IDA:dictyBase.
DR   GO; GO:0005576; C:extracellular region; IDA:dictyBase.
DR   GO; GO:0030175; C:filopodium; IDA:dictyBase.
DR   GO; GO:0030027; C:lamellipodium; IDA:dictyBase.
DR   GO; GO:0005811; C:lipid droplet; HDA:dictyBase.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR   GO; GO:0001726; C:ruffle; IDA:dictyBase.
DR   GO; GO:0005509; F:calcium ion binding; IDA:dictyBase.
DR   GO; GO:0005516; F:calmodulin binding; IPI:dictyBase.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0031152; P:aggregation involved in sorocarp development; TAS:dictyBase.
DR   GO; GO:0051702; P:biological process involved in interaction with symbiont; IDA:dictyBase.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:dictyBase.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:dictyBase.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:dictyBase.
DR   GO; GO:0010468; P:regulation of gene expression; IDA:dictyBase.
DR   GO; GO:1904643; P:response to curcumin; IDA:dictyBase.
DR   GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR   GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR   Gene3D; 2.60.40.1720; -; 1.
DR   InterPro; IPR015059; Ca_cell_adhesion_N_dom.
DR   InterPro; IPR038423; CAD_C_sf.
DR   InterPro; IPR011024; G_crystallin-like.
DR   InterPro; IPR029283; Membrane-bd.
DR   Pfam; PF08964; Crystall_3; 1.
DR   Pfam; PF14564; Membrane_bind; 1.
DR   SUPFAM; SSF49695; SSF49695; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cell adhesion; Cell membrane;
KW   Direct protein sequencing; Membrane; Reference proteome; Repeat.
FT   CHAIN           1..213
FT                   /note="Calcium-dependent cell adhesion molecule 1"
FT                   /id="PRO_0000089273"
FT   REPEAT          1..48
FT                   /note="1"
FT   REPEAT          49..97
FT                   /note="2"
FT   REPEAT          98..146
FT                   /note="3"
FT   REPEAT          147..194
FT                   /note="4"
FT   REGION          1..194
FT                   /note="4 X approximate tandem repeats"
FT   STRAND          8..13
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   TURN            14..16
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   STRAND          20..23
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   STRAND          25..30
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   HELIX           36..39
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   STRAND          43..46
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   STRAND          51..56
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   STRAND          73..78
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   HELIX           81..83
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   STRAND          87..92
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   STRAND          97..108
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   STRAND          115..121
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   STRAND          127..134
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   STRAND          136..140
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   STRAND          150..160
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   STRAND          165..176
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   TURN            177..180
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   STRAND          181..185
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   TURN            188..190
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   STRAND          193..201
FT                   /evidence="ECO:0007829|PDB:1YHP"
FT   STRAND          204..209
FT                   /evidence="ECO:0007829|PDB:1YHP"
SQ   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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