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Sca1 complex scaffold protein scaA

 SCAA_DICDI              Reviewed;        1582 AA.
Q54XY4;
15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
25-APR-2018, entry version 61.
RecName: Full=Sca1 complex scaffold protein scaA {ECO:0000303|PubMed:20493808};
Name=scaA {ECO:0000303|PubMed:20493808}; Synonyms=D1105, sca1;
ORFNames=DDB0220018, DDB_G0277843;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1]
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).
[2]
IDENTIFICATION IN THE SCA1 COMPLEX, FUNCTION, DISRUPTION PHENOTYPE,
DOMAIN, AND PHOSPHORYLATION AT SER-359.
PubMed=20493808; DOI=10.1016/j.devcel.2010.03.017;
Charest P.G., Shen Z., Lakoduk A., Sasaki A.T., Briggs S.P.,
Firtel R.A.;
"A Ras signaling complex controls the RasC-TORC2 pathway and directed
cell migration.";
Dev. Cell 18:737-749(2010).
-!- FUNCTION: Component of the Sca1 complex, a regulator of cell
motility, chemotaxis and signal relay (PubMed:20493808). The Sca1
complex is recruited to the plasma membrane in a
chemoattractant- and F-actin-dependent manner and is enriched at
the leading edge of chemotaxing cells where it regulates F-actin
dynamics and signal relay by controlling the activation of rasC
and the downstream target of rapamycin complex 2 (TORC2)-
Akt/protein kinase B (PKB) pathway (PubMed:20493808). ScaA acts as
a molecular scaffold, bringing together gefA, gefH and phr with
PP2A (PubMed:20493808). {ECO:0000269|PubMed:20493808}.
-!- SUBUNIT: Component of the Sca1 complex composed of at least gefA,
gefH, scaA, phr, and the protein phosphatase 2A subunits pppA and
pho2B (PubMed:20493808). {ECO:0000269|PubMed:20493808}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20493808}.
Note=The Sca1 complex is recruited to the plasma membrane in a
chemoattractant- and F-actin-dependent manner and is enriched at
the leading edge of chemotaxing cells (PubMed:20493808). Membrane
localization of the Sca1 complex is regulated by scaA
phosphorylation by PKB and PKB-related PKBR1 (PubMed:20493808).
{ECO:0000269|PubMed:20493808}.
-!- PTM: Phosphorylated at Ser-359 by PKB and PKBR1 is induced by
chemoattractant (PubMed:20493808). {ECO:0000269|PubMed:20493808}.
-!- DISRUPTION PHENOTYPE: Display directionality defects during
chemotaxis as well as defects in random motility
(PubMed:20493808). {ECO:0000269|PubMed:20493808}.
-----------------------------------------------------------------------
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EMBL; AAFI02000023; EAL68094.1; -; Genomic_DNA.
RefSeq; XP_642418.1; XM_637326.1.
STRING; 44689.DDB0220018; -.
iPTMnet; Q54XY4; -.
PaxDb; Q54XY4; -.
GeneID; 8621623; -.
KEGG; ddi:DDB_G0277843; -.
dictyBase; DDB_G0277843; scaA.
InParanoid; Q54XY4; -.
OMA; WDSQLIL; -.
PRO; PR:Q54XY4; -.
Proteomes; UP000002195; Chromosome 3.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0031252; C:cell leading edge; IMP:dictyBase.
GO; GO:0005829; C:cytosol; IDA:dictyBase.
GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
GO; GO:1905742; C:Ras guanyl-nucleotide exchange factor complex; IDA:dictyBase.
GO; GO:0032947; F:protein-containing complex scaffold activity; TAS:dictyBase.
GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:dictyBase.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IMP:dictyBase.
GO; GO:1904515; P:positive regulation of TORC2 signaling; IMP:dictyBase.
GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
InterPro; IPR037474; ScaA.
PANTHER; PTHR37516; PTHR37516; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Membrane; Phosphoprotein;
Reference proteome; Repeat; TPR repeat.
CHAIN 1 1582 Sca1 complex scaffold protein scaA.
/FTId=PRO_0000438890.
REPEAT 4 37 TPR 1. {ECO:0000255}.
REPEAT 166 199 TPR 2. {ECO:0000255}.
REPEAT 742 777 TPR 3. {ECO:0000255}.
REPEAT 1080 1113 TPR 4. {ECO:0000255}.
REGION 400 600 GefA and gefH binding.
{ECO:0000269|PubMed:20493808}.
REGION 1000 1400 PppA and pho2B binding.
{ECO:0000269|PubMed:20493808}.
COMPBIAS 110 124 Poly-Ser. {ECO:0000255}.
COMPBIAS 133 136 Poly-Pro. {ECO:0000255}.
COMPBIAS 137 141 Poly-Asn. {ECO:0000255}.
COMPBIAS 277 280 Poly-Gly. {ECO:0000255}.
COMPBIAS 692 726 Gly-rich. {ECO:0000255|PROSITE-
ProRule:PRU00008}.
COMPBIAS 860 934 Gly-rich. {ECO:0000255|PROSITE-
ProRule:PRU00008}.
COMPBIAS 863 982 Ser-rich. {ECO:0000255|PROSITE-
ProRule:PRU00016}.
COMPBIAS 931 934 Poly-Gly. {ECO:0000255}.
MOD_RES 359 359 Phosphoserine; by PKB.
{ECO:0000269|PubMed:20493808}.
SEQUENCE 1582 AA; 174927 MW; 648F6B8847F055AB CRC64;
MSSLDPSLST TPSTNRRGTF SKAKSFRRAA LNLEPQGTPG QPHAFRFLSG EEYSGPDIIE
NIKKPININI ESEEYKTPLF LGANGTLYNK YYIPIKIIGI DEPLPQTGLS PSLSSSSSSS
SSPSPPTTTS TTPPPPNNNN NSKQIKKNNS ISDLTPYLNF NSTDQIYTSF PESMAFDDYM
DYEESLVEWK RQVEQNLGII QLPHSIGRTY PRPKVIHEQL FRKNSEASND DSISYDIERK
LTDSDIKETN SSVNDDGESF SHSPTLRGNN GSSLSVGGGG DNHDNTSNKD NASSQGTNHG
VTLNHPNSGI NLRERSNSDT STGSFEGTQL DGSSPMDGSP STGSLAGFVA NGTRSRTNSI
TYFDQRNQRS NSLSPKHSML QSRLADSQSL DSSMYGKMGR SGSGFGMDHE SWFLQKDPWD
SQLILTEPHP DLFSTYEEYE YAMKNWAHEV ITKTSILPPH PGQFIQLPKN SELSTDDGSG
GGSGGSGVDG VGGNHQLGGS ARHMLEMDFE MAKNQSNWTL RPIIRPIITE ETMIFNRILS
QSNLKHTEYD HLFSIDQELP PSQVWKTLDS DEKLKITETI DRWYRKKLTI QRQTSTWFRG
GLWANHFLMP NIQSGWRESV SKKSSILPPL SLKALRRLDI NSEADGKRVE HSFPIPELPI
NFNKLLAPDM NLQYFLGMLE MPTAHSLSSA TGGQQQGGSG GGSGGSGSGS GSGSGLNMSG
TSGSSGKSEK DKDKETANYI AMHSINNTTN VGTKEDRRQY TKILQTYEQR LQFSFRLDAL
NSWSEGGYTP MELQEKKLDI EQLVAAPGFD LQNGVWSLVN NSAHFLDKFQ ETFDQVDLRL
YAPAIPMLPA IVPSVFINAG GGSGGGSGGA SGGGISTSSG TSPNIVRPGS SSIGGGQPPS
SPHIPSGSSL LSSPPNRQGS TGSFSFIGSP GGGGKISPTN SSSLESPRTQ SQLAAVVERG
SSPRSHSGGS ISTHPNTPSV SSNTFLSLIN TDSFPELLKF LDLTNEKLAL GKISSLVLLV
LTSELKGTMV IENILFSKDL QSLYRLARAI SFFDAVPLDL FTYPTHLNEM LTPSIFKGST
QEVVRLVFVY YYLGIIQERL NFFSNNVGIL GFVNSSRKDA AERIGIQFQN DREFLYKIFK
ALGRKSILVS NCFLFVLIQL IKMSESPTVQ SLLKGELLTH IRDLSASKFS HSRFAAKRLY
QILQEDPWKE FLMASYAESI KKNESQHLTD LTTMKEGPKL AIPSISLISE LTFNFCVGVL
ENINSTPIPK PIYKFILNDS IFFQLCNAIV KCKNFTQSTQ IVSKVFASLC KVLAKFNLFK
NSDSIKSGGK VDPKKQNDVE TGVAISPTLL FEIIGFLQNS SLDNNRYCSI IKTNMLIALR
QLLKQSEIFD SIKKEGNLYN KFLIPACRDG KNVEFNRNVW RLFFQMIRFH HGHIEYLEKS
KYLNALMDII SLNAGNVVLT NALHYLSKLF SLVSYETRKN ALRAPGTLSI DTKYSEKDVK
SLLNFFVERS CFIKFHMIYK KLTENTEGIQ IDQRLLINIT TFYRIISFLP SCQKLLKDTL
KNPEYKTGII QVSKMYKPSE TF


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