ID I1L0J1_SOYBN Unreviewed; 467 AA.
AC I1L0J1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=CRAL-TRIO domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=100809450 {ECO:0000313|EnsemblPlants:KRH36854};
GN ORFNames=GLYMA_09G028400 {ECO:0000313|EMBL:KRH36854.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH36854};
RN [1] {ECO:0000313|EMBL:KRH36854.1, ECO:0000313|EnsemblPlants:KRH36854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH36854};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH36854.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH36854}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH36854};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH36854.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH36854.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the patellin family.
CC {ECO:0000256|ARBA:ARBA00007155}.
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DR EMBL; CM000842; KRH36854.1; -; Genomic_DNA.
DR RefSeq; XP_003535132.1; XM_003535084.3.
DR AlphaFoldDB; I1L0J1; -.
DR SMR; I1L0J1; -.
DR STRING; 3847.I1L0J1; -.
DR PaxDb; 3847-GLYMA09G03300-1; -.
DR EnsemblPlants; KRH36854; KRH36854; GLYMA_09G028400.
DR GeneID; 100809450; -.
DR Gramene; KRH36854; KRH36854; GLYMA_09G028400.
DR KEGG; gmx:100809450; -.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_023762_1_1_1; -.
DR InParanoid; I1L0J1; -.
DR OMA; NEFSEHE; -.
DR OrthoDB; 53323at2759; -.
DR Proteomes; UP000008827; Chromosome 9.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 2.60.120.680; GOLD domain; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR044834; PATL.
DR PANTHER; PTHR45932; PATELLIN-1; 1.
DR PANTHER; PTHR45932:SF2; PATELLIN-4; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827}.
FT DOMAIN 181..354
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 355..462
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
FT REGION 19..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 52979 MW; E36672C4B056B3E2 CRC64;
MTAEVMAQEE TQAAEVVVVA VAEPQKEKDA EENVEPREPS SVDETKPKTV EKSSSYKEES
NYLSDLKEFE RKALSELKSK LEEAILGNTL FDPKKEALPE NEEKKNEGEE KEEEEEKKVE
VEENDVSIWG VTLLPSKGAE GVDVVLLKFL RAREFKVNDA FEMLKKTLKW RKESKIDSVV
DEDFGSDLAS AAYMNGVDHE GHPVCYNIFG AFESEESYQK TFGTEEKRSE FLRWRCQLME
KGIQRLNLKP GGVSSLLQIN DLKNSPGPSK LRVATKQTLA MFQDNYPEMV AKNIFINVPF
WYYALNALLS PFLTQRTKSK FVVARPNKVT ETLTKYIPIE EIPVHYGGFK RENDSEFSSQ
DVAVSELILK AGSTATIEIP ALEVGYSLCW DLTVLGWELS YKEEFVPTDE GSYTVIVQKG
KKMGSQEGPV RNTFRNNEPG KVVLTIENTS NKKKKVLYRY KSIKSSF
//
