FRMA_DICDI
ID FRMA_DICDI Reviewed; 1154 AA.
AC Q54EW0;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=FERM domain-containing protein A;
GN Name=frmA; ORFNames=DDB_G0291303;
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=AX2;
RX PubMed=18349074; DOI=10.1242/jcs.021725;
RA Patel H., Koenig I., Tsujioka M., Frame M.C., Anderson K.I., Brunton V.G.;
RT "The multi-FERM-domain-containing protein FrmA is required for turnover of
RT paxillin-adhesion sites during cell migration of Dictyostelium.";
RL J. Cell Sci. 121:1159-1164(2008).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=AX2;
RX PubMed=19002378; DOI=10.1007/s00018-008-8527-y;
RA Patel H., Brunton V.G.;
RT "Loss of FrmA leads to increased cell-cell adhesion and impaired multi-
RT cellular development of Dictyostelium cells.";
RL Cell. Mol. Life Sci. 66:145-155(2009).
CC -!- FUNCTION: Key regulator of adhesion dynamics, it acts as an anti-
CC adhesive. Plays a critical role in the regulation of cell-cell
CC adhesion, multi-cellular development and, in particular, the formation
CC of the organising center known as the tip. Required for turnover of
CC paxillin-adhesion sites during cell migration. Plays a major role in
CC normal cell shape, cell-substrate adhesion and actin cytoskeleton
CC organization. {ECO:0000269|PubMed:18349074,
CC ECO:0000269|PubMed:19002378}.
CC -!- DEVELOPMENTAL STAGE: It is present during all stages of starvation-
CC induced multicellular development. It is 5.7-, 6.5- and 10.9-fold
CC higher at 8, 16 and 24 h, respectively after starvation.
CC -!- INDUCTION: By starvation. {ECO:0000269|PubMed:19002378}.
CC -!- DISRUPTION PHENOTYPE: Loss of FrmA leads to increased cell-cell
CC adhesion and results in impaired multi-cellular development, slug
CC migration and fruiting bodies. Mutants show increased adhesion because
CC of an increased number, persistence and mislocalization of paxillin
CC rich cell-substrate adhesions, which is associated with decreased
CC motility. FrmA null cells are unable to efficiently sort to the apex of
CC mounds and form the organising center known as the tip. They also show
CC a delayed expression of LagC. {ECO:0000269|PubMed:18349074,
CC ECO:0000269|PubMed:19002378}.
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DR EMBL; AAFI02000177; EAL61635.1; -; Genomic_DNA.
DR RefSeq; XP_635130.1; XM_630038.1.
DR AlphaFoldDB; Q54EW0; -.
DR SMR; Q54EW0; -.
DR STRING; 44689.DDB0233517; -.
DR PaxDb; Q54EW0; -.
DR EnsemblProtists; EAL61635; EAL61635; DDB_G0291303.
DR GeneID; 8628076; -.
DR KEGG; ddi:DDB_G0291303; -.
DR dictyBase; DDB_G0291303; frmA.
DR eggNOG; KOG4261; Eukaryota.
DR HOGENOM; CLU_276155_0_0_1; -.
DR InParanoid; Q54EW0; -.
DR OMA; CQCLDAI; -.
DR PRO; PR:Q54EW0; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; IMP:dictyBase.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0046956; P:positive phototaxis; IMP:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR CDD; cd14473; FERM_B-lobe; 2.
DR Gene3D; 1.20.80.10; -; 2.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR032425; FERM_f0.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF16511; FERM_f0; 1.
DR Pfam; PF00373; FERM_M; 2.
DR SMART; SM00295; B41; 2.
DR SUPFAM; SSF47031; SSF47031; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS50057; FERM_3; 2.
PE 2: Evidence at transcript level;
KW Reference proteome; Repeat.
FT CHAIN 1..1154
FT /note="FERM domain-containing protein A"
FT /id="PRO_0000391331"
FT DOMAIN 218..547
FT /note="FERM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 666..1103
FT /note="FERM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 122..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1154 AA; 129489 MW; BAD3FC4458267127 CRC64;
MAVLSLVELC FISIMERMEY NNQALQKIPP QLIERLINFM VYKLPPNHLS LQTISKPIRI
KLVRQNRVIT MRFSIYNTID KIIHQIYERI INEEKMEQNE KQKNSSNNNL LSLLTLNNNN
QNNNSSIITT TTTTTNNNNN SNCGSSSSSS SSKQILWGSI ENYGLFQQSG SFRNARWLQL
DKTLAYYEID SNETLEFKTC KSVLKIRFFG PWERVVHPLH QSTMLDETIK TFVFDESKTV
SEISMELAKK LQLKYPEELS LKVQCEEEDD GRGIWLSADL TLPEQGIDPL YTIFLLKRQF
FFCKDIIIDF SMDAEMLHFV FCQCLDAIID TSHPCSPTES ILFAALQCQI CFGDYVHGSK
EIDQIRQRDF LPMEFINQKN ILKEILIQYQ RLIGMSEQKA KLNYIQLAKS LKTYGYTFFK
VTNRQTSIVN NNLSSSGGSG NGSGSGNGSS SSSSNSSSGN NNNHNHHNHQ QLFGISSEAV
LTLDPMTNNT ISLYSLSNIR KWHVLNNVFT IEYNDRKDTF ISMEAEAISH VLSSYIHHNL
RETPSIQKQW DQNYLSVSGR NSLTNGRKRL STCSNCSSDS MEFDSSKSNT KDKDWKYQYG
LVIKKCALYI EPKKLYINPL STQITGSMVN KELNKDTKVT KVLKVLTDLS SKMILSFSKS
SPAKEREIVV KFSDKKVKSF VVDEQKTVSE ITQEIGLKLG IKNPEEFSLQ LIVNNKNNNN
NNNSNNSSTS SSSSSSVNNS GIFDGLNNSN VNNVFYNSYI VNSSISNNSN SNSNSNILNN
SNDEQSTSTS TSSSLGGIWL KPYQPLSEQS ISPDSKLLFK KKFYTSDIGA ADDCNSDPVY
FNLLFFQSKD AIISNTYTCS KEEAIQLAAT LFQINFGDHN PNIHKPGFLK SQDLKFFLPP
NSLELWGLSF QKIEKSIYKE HQNLRGIKEV YAKYRYVQLC RSLKTFGAIF FSVRQLLPNK
TNGSSSSSSN NNGGNSNNGI NGNGIITGGN GGSGGGGSGI GGNGSGINTG GNGFGGSQQI
PINQPLVLGF SRKCILFMTA KTKKFLVEYP LTHLRRWAYH KDTQCLTLDF GDYEMGRIVL
QTTESEEISS YLSDYIDYIQ TKLVGSQSFS RSIFNSDNNS SSFFSNSFCN NTTTTTTTTT
TTTTTTTTTT TNNV
