位置:首页 > 蛋白库 > AARA_DICDI
AARA_DICDI
ID   AARA_DICDI              Reviewed;         757 AA.
AC   Q54I71; Q9GSG6;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Protein aardvark;
DE   AltName: Full=Suppressor of amiB protein 16;
GN   Name=aarA; Synonyms=aar, sab6; ORFNames=DDB_G0288877;
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], FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR
RP   LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11130075; DOI=10.1038/35047099;
RA   Grimson M.J., Coates J.C., Reynolds J.P., Shipman M., Blanton R.L.,
RA   Harwood A.J.;
RT   "Adherens junctions and b-catenin mediated cell signalling in a non-
RT   metazoan organism.";
RL   Nature 408:727-731(2000).
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   SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11792801; DOI=10.1242/jcs.114.24.4349;
RA   Coates J.C., Harwood A.J.;
RT   "Cell-cell adhesion and signal transduction during Dictyostelium
RT   development.";
RL   J. Cell Sci. 114:4349-4358(2001).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=12128211; DOI=10.1016/s0925-4773(02)00152-1;
RA   Coates J.C., Grimson M.J., Williams R.S.B., Bergman W., Blanton R.L.,
RA   Harwood A.J.;
RT   "Loss of the beta-catenin homologue aardvark causes ectopic stalk formation
RT   in Dictyostelium.";
RL   Mech. Dev. 116:117-127(2002).
RN   [5]
RP   IDENTIFICATION.
RX   PubMed=18164290; DOI=10.1016/j.yexcr.2007.12.002;
RA   Nagasaki A., Uyeda T.Q.P.;
RT   "Screening of genes involved in cell migration in Dictyostelium.";
RL   Exp. Cell Res. 314:1136-1146(2008).
CC   -!- FUNCTION: Required to regulate pattern formation during multi-cellular
CC       stages of development and for the formation of adherens junctions.
CC       Plays a structural role during the regulation of stalk formation.
CC       Involved in cell signaling. Required for spore-cell differentiation.
CC       Overexpression increases number and size of cell junctions and reduces
CC       spore-cell formation. {ECO:0000269|PubMed:11130075}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction.
CC   -!- DEVELOPMENTAL STAGE: Localized at the cell junctions in the developing
CC       fruiting body. {ECO:0000269|PubMed:11130075}.
CC   -!- DISRUPTION PHENOTYPE: Complete loss of cell junctions. Lacks actin-
CC       containing adherens junctions at the top of the stalk tube. Has weak
CC       stalks causing the fruiting body to frequently collapse. Displays
CC       multiple stalks appearance during late development. Shows no defects in
CC       growth or division. {ECO:0000269|PubMed:11130075,
CC       ECO:0000269|PubMed:11792801, ECO:0000269|PubMed:12128211}.
CC   -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF305417; AAG17931.1; -; mRNA.
DR   EMBL; AAFI02000126; EAL62962.1; -; Genomic_DNA.
DR   RefSeq; XP_636508.1; XM_631416.1.
DR   AlphaFoldDB; Q54I71; -.
DR   SMR; Q54I71; -.
DR   STRING; 44689.DDB0191132; -.
DR   PaxDb; Q54I71; -.
DR   EnsemblProtists; EAL62962; EAL62962; DDB_G0288877.
DR   GeneID; 8626891; -.
DR   KEGG; ddi:DDB_G0288877; -.
DR   dictyBase; DDB_G0288877; aarA.
DR   eggNOG; KOG4199; Eukaryota.
DR   HOGENOM; CLU_368213_0_0_1; -.
DR   InParanoid; Q54I71; -.
DR   PRO; PR:Q54I71; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005912; C:adherens junction; IDA:dictyBase.
DR   GO; GO:0045180; C:basal cortex; IDA:dictyBase.
DR   GO; GO:0005911; C:cell-cell junction; TAS:dictyBase.
DR   GO; GO:0005813; C:centrosome; TAS:dictyBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR   GO; GO:0045294; F:alpha-catenin binding; IPI:dictyBase.
DR   GO; GO:0031032; P:actomyosin structure organization; IMP:dictyBase.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0048870; P:cell motility; IGI:dictyBase.
DR   GO; GO:0051642; P:centrosome localization; IMP:dictyBase.
DR   GO; GO:0031154; P:culmination involved in sorocarp development; IEP:dictyBase.
DR   GO; GO:0140509; P:epithelium-like organization; IMP:dictyBase.
DR   GO; GO:0061245; P:establishment or maintenance of bipolar cell polarity; IMP:dictyBase.
DR   GO; GO:0051645; P:Golgi localization; IMP:dictyBase.
DR   GO; GO:0051495; P:positive regulation of cytoskeleton organization; IMP:dictyBase.
DR   GO; GO:0008104; P:protein localization; IMP:dictyBase.
DR   GO; GO:0009306; P:protein secretion; IMP:dictyBase.
DR   GO; GO:0010468; P:regulation of gene expression; IEP:dictyBase.
DR   GO; GO:0044671; P:sorocarp spore cell differentiation; IMP:dictyBase.
DR   GO; GO:0031150; P:sorocarp stalk development; IMP:dictyBase.
DR   GO; GO:0036360; P:sorocarp stalk morphogenesis; IMP:dictyBase.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   Pfam; PF00514; Arm; 1.
DR   SMART; SM00185; ARM; 6.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF81383; SSF81383; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 5.
DR   PROSITE; PS50181; FBOX; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell junction; Coiled coil; Cytoplasm;
KW   Developmental protein; Reference proteome; Repeat.
FT   CHAIN           1..757
FT                   /note="Protein aardvark"
FT                   /id="PRO_0000390561"
FT   DOMAIN          310..356
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REPEAT          454..498
FT                   /note="ARM 1"
FT   REPEAT          506..548
FT                   /note="ARM 2"
FT   REPEAT          549..591
FT                   /note="ARM 3"
FT   REPEAT          592..634
FT                   /note="ARM 4"
FT   REPEAT          635..678
FT                   /note="ARM 5"
FT   REPEAT          679..723
FT                   /note="ARM 6"
FT   REGION          39..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          121..205
FT                   /evidence="ECO:0000255"
FT   CONFLICT        544
FT                   /note="R -> K (in Ref. 1; AAG17931)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   757 AA;  85924 MW;  51A94DAAA66CC156 CRC64;
     MNDCGSLFNK KLFKMNLLFK HLKLQQHLKL QQKPLLNNSS INNNINNNNN NNNNNNSNND
     SNNTNTNIFN NSFLNSDLIE RLIIKFTIGY LKNNITEDYI EQILLENQNN FIKSTTTSNY
     ILEENNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNSSS SSSSILSKFN KLEEDNELEL
     QKKQKQQLEQ QEEELFNQFN FLEGIEDQND FLSEQETIQK IKFLIKMTAK SMSNYSSPNT
     LIPSVSKTYI SPFGLSSNGS TNNHNNNNNN NHHHHSNNGN LIESSNNVNN QLNVSNYNNN
     NSNHYDENNQ FDIFLIPTEM LVHLLSFLSA NDLWRISLTC KRIWYIVDVF KFWELLFEQT
     CPRIYYAMQF NSRWSNPTSF QSKMILCYID RLPTDNYKNF DKSDESGQIK KIIGVMNENL
     HNPMILRETC YILKRLSYRQ RKEDEHESLI ARYGGISLIL QAMKNHPYDA GVQEDACGAL
     GNLTCDSPNN MGLYSNDNYL SVVEQGGIQL ILQAMKNHMM NPGVQYNTSF VLRNLARNDV
     SESRVAIEGG IQSIATAMKN HPNHIGIQTQ GCGALRNLGC NDSNKVLSAK EGGIGLILRA
     MRSFSSHPDL QLNGCGALRN LARNEDNKNM ISRQNGIQLV LGAMSNHPDD PDVQDEGCAA
     LINLAYQDEA NEETIAREGG INLILKAMRN HPFHSGVQMQ GRGALKNLSC NPKNKLTIAR
     SGGIELMNIA MQNHPNFANR FLELSRILQV ALEDGNI
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024