ID A0A1B6Q7A0_SORBI Unreviewed; 590 AA.
AC A0A1B6Q7A0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 08-OCT-2025, entry version 42.
DE RecName: Full=CRAL-TRIO domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SORBI_3003G373100 {ECO:0000313|EMBL:KXG33790.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG33790.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:KXG33790.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the patellin family.
CC {ECO:0000256|ARBA:ARBA00007155}.
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DR EMBL; CM000762; KXG33790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B6Q7A0; -.
DR FunCoup; A0A1B6Q7A0; 93.
DR STRING; 4558.A0A1B6Q7A0; -.
DR Gramene; KXG33790; KXG33790; SORBI_3003G373100.
DR eggNOG; KOG1471; Eukaryota.
DR InParanoid; A0A1B6Q7A0; -.
DR OMA; LRGHKMN; -.
DR OrthoDB; 75724at2759; -.
DR Proteomes; UP000000768; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; 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 Gene3D; 1.10.8.20; N-terminal domain of phosphatidylinositol transfer protein sec14p; 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; IPR036598; GOLD_dom_sf.
DR InterPro; IPR044834; PATL.
DR InterPro; IPR056794; PATL1-6_C_GOLD.
DR PANTHER; PTHR45932:SF17; CELLULAR RETINALDEHYDE-BINDING_TRIPLE FUNCTION DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45932; PATELLIN-1; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR Pfam; PF25099; GOLD_PATL1_C; 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 SUPFAM; SSF101576; Supernatant protein factor (SPF), C-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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 303..478
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 479..585
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..20
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 64334 MW; E3DC66F2926C4BE5 CRC64;
MAEETQPEAA AAAAAAAPPA AEVVVTEAVA AEVEVPAAAE AEAEPETEKK ADEAAVTADD
AGEGTGSFKE ESNLVEDLPD PEKKALDEFK QLIAAALAAG EFNLPPPPPP PKAKEEPKAE
ETKTEEAKTE ETKTEEAKTE EPVKEEPKAE AEAAAEEPKA EVAADAPAEE VKTEVPPPEE
AKAETVAEEA KPAEPEPQEK TVVVAEEETA TKTVETIEET VVSAPAATSE EAVAPEAAAE
SDAAAPEPVL IWGVPLVGDD ECTDTVLLKF LRAREFKVKE AMAMLKSAVL WRKRFGITSL
LDADLGLPEL ENVVFYRGAD REGHPVCYNV YGEFQDKDLY EKAFGDDEKR ERFLKWRIQL
LERGILSKLD FSPSGICSMV QVTDLKNSPP MLGKHRAVTR QAVTLLQDNY PEFIAKKVFI
NVPWWYLAAN KMMSPFLTQR TKSKFVFASP AKSAETLFRY IAPEQVPVQF GGLFKVDDPE
FTTSDIVTEL TIKPSSKETI EIPVTENSTI VWELRVLGWE VSYGAEFTPD AEGGYTVIVQ
KSRKVPANEE PIMKGSFKVG EPGKLVLTVN NPASKKKKLL YRSKVKSTSE
//
