TRIA_DICDI
ID TRIA_DICDI Reviewed; 697 AA.
AC Q54D84;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Trishanku;
GN Name=triA; ORFNames=DDB_G0292436;
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, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=17177856; DOI=10.1111/j.1432-0436.2006.00086.x;
RA Jaiswal J.K., Mujumdar N., Macwilliams H.K., Nanjundiah V.;
RT "Trishanku, a novel regulator of cell-type stability and morphogenesis in
RT Dictyostelium discoideum.";
RL Differentiation 74:596-607(2006).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=19878291; DOI=10.1111/j.1525-142x.2009.00377.x;
RA Mujumdar N., Inouye K., Nanjundiah V.;
RT "The trishanku gene and terminal morphogenesis in Dictyostelium
RT discoideum.";
RL Evol. Dev. 11:697-709(2009).
CC -!- FUNCTION: Required for normal morphogenesis and cell-type stability.
CC {ECO:0000269|PubMed:17177856, ECO:0000269|PubMed:19878291}.
CC -!- TISSUE SPECIFICITY: Expressed strongly in presumptive spore (prespore
CC or psp) cells during the late G2 phase of cell cycle. Present at a low
CC level in vegetative cells. {ECO:0000269|PubMed:17177856,
CC ECO:0000269|PubMed:19878291}.
CC -!- DEVELOPMENTAL STAGE: High expression during late G2-S phases. During
CC development, expression level peaks at 12-15 hr post-starvation, and
CC falls thereafter. {ECO:0000269|PubMed:17177856}.
CC -!- INDUCTION: Up-regulated by starvation.
CC -!- DISRUPTION PHENOTYPE: Mutant shows pleiotropic effects that include an
CC inability of the spore mass to go all the way to the top. The upper
CC cup, a tissue that derives from prestalk cells and anterior-like cells
CC (ALCs), does not develop properly; it is unable to lift the spore mass
CC to the top of the fruiting body, likely due to defective intercellular
CC adhesion. The differentiated state becomes unstable; prespore cells
CC transdifferentiate into prestalk and vice versa. Cells that find
CC themselves in the wrong environment sort out to the zone that is
CC appropriate to their new identity. The functional barrier that prevents
CC intermixing between the prestalk and prespore zones becomes weakened.
CC This permits prespore cells to move to the slug anterior and prestalk
CC cells to the posterior. Cells that have moved to the wrong zone switch
CC their state of differentiation in accord with their new location.
CC {ECO:0000269|PubMed:17177856, ECO:0000269|PubMed:19878291}.
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DR EMBL; AAFI02000190; EAL61197.1; -; Genomic_DNA.
DR RefSeq; XP_629612.1; XM_629610.1.
DR AlphaFoldDB; Q54D84; -.
DR SMR; Q54D84; -.
DR STRING; 44689.DDB0234260; -.
DR PaxDb; Q54D84; -.
DR EnsemblProtists; EAL61197; EAL61197; DDB_G0292436.
DR GeneID; 8628675; -.
DR KEGG; ddi:DDB_G0292436; -.
DR dictyBase; DDB_G0292436; triA.
DR eggNOG; KOG4350; Eukaryota.
DR HOGENOM; CLU_395598_0_0_1; -.
DR InParanoid; Q54D84; -.
DR OMA; FFASKIM; -.
DR Reactome; R-DDI-114608; Platelet degranulation.
DR Reactome; R-DDI-8951664; Neddylation.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q54D84; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; IMP:dictyBase.
DR GO; GO:0045165; P:cell fate commitment; IMP:dictyBase.
DR GO; GO:0001709; P:cell fate determination; IMP:dictyBase.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR CDD; cd00121; MATH; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 2: Evidence at transcript level;
KW Reference proteome.
FT CHAIN 1..697
FT /note="Trishanku"
FT /id="PRO_0000393271"
FT DOMAIN 122..189
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..449
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 697 AA; 79148 MW; FC49F887CE23AC6C CRC64;
MEIEPVVRIS FNGNNNQNNN NNNNNNTNNN SNNNNNNNNS SNINSTNKPS VKKPINQKMI
SNINNQKSPN PLNSSVDDNN NTNNNNNSNS NGTDEDIIKL ARDLTNTFGI LLGDSDQPSQ
FSDVIFKVGD RKFFASKIML VARSEYFKAM FTGSMKESSI KEITLEGVDP DVFFTVLKYI
CIGILDLDYD HRMVSSIYQY CDLLGLQRGK ELSLATMGKI AQMYLEKPDV ESALFLWDSL
NQSAIPVESV HPHLRAFVLQ YASISLHCDA FYSISLTTLV QMLRNDGLRM EELDILDCVI
DWCRENSQAS IQQQQQQQQQ QLQSANGASG KSHGKRSSSS HLKKHDGDGG SDGSCSSRCS
SRRNSLSLKD HHRQHIGNGG GGGGHYNNND CHSDTEETYS DIDDEEHRNG GGGVGDDFEN
DSEDGDDDDE DDDEDDDFTD DDDKDDSAND DYEYSTNKDD LDIIEDWDTT IDKNLLDEVL
PLIRWENMNI GEAFERLDNL KIIPDKEISN LLRHILKSNR GESFSFLGYH YRRPRNNRKR
PYPIEFLLGI TQPFDSNVTN EIIPLNSFSS EFGQSTNQFL YRIKKDIKLP ANLERFSFKD
REFFVQLKER EKGQLAVYLA FGSKLTKPLA ISVLASVIGF RFQDSIEFSF KKMFDEGFDS
AWGWPKFISL DTLYKQDKYS HYSDSFCLLI ELTSQWG
