SCAA_DICDI
ID SCAA_DICDI Reviewed; 1582 AA.
AC Q54XY4;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Sca1 complex scaffold protein scaA {ECO:0000303|PubMed:20493808};
GN Name=scaA {ECO:0000303|PubMed:20493808}; Synonyms=D1105, sca1;
GN ORFNames=DDB0220018, DDB_G0277843;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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 [2]
RP IDENTIFICATION IN THE SCA1 COMPLEX, FUNCTION, DISRUPTION PHENOTYPE, DOMAIN,
RP AND PHOSPHORYLATION AT SER-359.
RX PubMed=20493808; DOI=10.1016/j.devcel.2010.03.017;
RA Charest P.G., Shen Z., Lakoduk A., Sasaki A.T., Briggs S.P., Firtel R.A.;
RT "A Ras signaling complex controls the RasC-TORC2 pathway and directed cell
RT migration.";
RL Dev. Cell 18:737-749(2010).
CC -!- FUNCTION: Component of the Sca1 complex, a regulator of cell motility,
CC chemotaxis and signal relay (PubMed:20493808). The Sca1 complex is
CC recruited to the plasma membrane in a chemoattractant- and F-actin-
CC dependent manner and is enriched at the leading edge of chemotaxing
CC cells where it regulates F-actin dynamics and signal relay by
CC controlling the activation of rasC and the downstream target of
CC rapamycin complex 2 (TORC2)-Akt/protein kinase B (PKB) pathway
CC (PubMed:20493808). ScaA acts as a molecular scaffold, bringing together
CC gefA, gefH and phr with PP2A (PubMed:20493808).
CC {ECO:0000269|PubMed:20493808}.
CC -!- SUBUNIT: Component of the Sca1 complex composed of at least gefA, gefH,
CC scaA, phr, and the protein phosphatase 2A subunits pppA and pho2B
CC (PubMed:20493808). {ECO:0000269|PubMed:20493808}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20493808}.
CC Note=The Sca1 complex is recruited to the plasma membrane in a
CC chemoattractant- and F-actin-dependent manner and is enriched at the
CC leading edge of chemotaxing cells (PubMed:20493808). Membrane
CC localization of the Sca1 complex is regulated by scaA phosphorylation
CC by PKB and PKB-related PKBR1 (PubMed:20493808).
CC {ECO:0000269|PubMed:20493808}.
CC -!- PTM: Phosphorylated at Ser-359 by PKB and PKBR1 is induced by
CC chemoattractant (PubMed:20493808). {ECO:0000269|PubMed:20493808}.
CC -!- DISRUPTION PHENOTYPE: Display directionality defects during chemotaxis
CC as well as defects in random motility (PubMed:20493808).
CC {ECO:0000269|PubMed:20493808}.
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DR EMBL; AAFI02000023; EAL68094.1; -; Genomic_DNA.
DR RefSeq; XP_642418.1; XM_637326.1.
DR AlphaFoldDB; Q54XY4; -.
DR STRING; 44689.DDB0220018; -.
DR iPTMnet; Q54XY4; -.
DR PaxDb; Q54XY4; -.
DR GeneID; 8621623; -.
DR KEGG; ddi:DDB_G0277843; -.
DR dictyBase; DDB_G0277843; scaA.
DR eggNOG; ENOG502R6N6; Eukaryota.
DR HOGENOM; CLU_245066_0_0_1; -.
DR InParanoid; Q54XY4; -.
DR OMA; KDPWDSQ; -.
DR PRO; PR:Q54XY4; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0031252; C:cell leading edge; IMP:dictyBase.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:1905742; C:Ras guanyl-nucleotide exchange factor complex; IDA:dictyBase.
DR GO; GO:0060090; F:molecular adaptor activity; TAS:dictyBase.
DR GO; GO:0030295; F:protein kinase activator activity; IDA:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IMP:dictyBase.
DR GO; GO:1904515; P:positive regulation of TORC2 signaling; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
DR InterPro; IPR037474; ScaA.
DR PANTHER; PTHR37516; PTHR37516; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat.
FT CHAIN 1..1582
FT /note="Sca1 complex scaffold protein scaA"
FT /id="PRO_0000438890"
FT REPEAT 4..37
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 166..199
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 742..777
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 1080..1113
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..600
FT /note="GefA and gefH binding"
FT /evidence="ECO:0000269|PubMed:20493808"
FT REGION 468..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1400
FT /note="PppA and pho2B binding"
FT /evidence="ECO:0000269|PubMed:20493808"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 359
FT /note="Phosphoserine; by PKB"
FT /evidence="ECO:0000269|PubMed:20493808"
SQ 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
