ID A0A6J1J0S7_CUCMA Unreviewed; 435 AA.
AC A0A6J1J0S7;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE RecName: Full=Growth-regulating factor {ECO:0000256|RuleBase:RU367127};
GN Name=LOC111481644 {ECO:0000313|RefSeq:XP_022982951.1};
OS Cucurbita maxima (Pumpkin) (Winter squash).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX NCBI_TaxID=3661 {ECO:0000313|Proteomes:UP000504608, ECO:0000313|RefSeq:XP_022982951.1};
RN [1] {ECO:0000313|RefSeq:XP_022982951.1}
RP IDENTIFICATION.
RC TISSUE=Young leaves {ECO:0000313|RefSeq:XP_022982951.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- FUNCTION: Transcription activator. {ECO:0000256|RuleBase:RU367127}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU01002, ECO:0000256|RuleBase:RU367127}.
CC -!- DOMAIN: The QLQ domain and WRC domain may be involved in protein-
CC protein interaction and DNA-binding, respectively.
CC {ECO:0000256|RuleBase:RU367127}.
CC -!- SIMILARITY: Belongs to the GRF family. {ECO:0000256|ARBA:ARBA00008122,
CC ECO:0000256|RuleBase:RU367127}.
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DR RefSeq; XP_022982951.1; XM_023127183.1.
DR AlphaFoldDB; A0A6J1J0S7; -.
DR GeneID; 111481644; -.
DR KEGG; cmax:111481644; -.
DR OrthoDB; 1927209at2759; -.
DR Proteomes; UP000504608; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0099402; P:plant organ development; IEA:UniProtKB-ARBA.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR031137; GRF.
DR InterPro; IPR014977; WRC_dom.
DR PANTHER; PTHR31602:SF63; GROWTH-REGULATING FACTOR 3; 1.
DR PANTHER; PTHR31602; GROWTH-REGULATING FACTOR 5; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF08879; WRC; 1.
DR SMART; SM00951; QLQ; 1.
DR PROSITE; PS51666; QLQ; 1.
DR PROSITE; PS51667; WRC; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|RuleBase:RU367127};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU01002}; Reference proteome {ECO:0000313|Proteomes:UP000504608};
KW Transcription {ECO:0000256|RuleBase:RU367127};
KW Transcription regulation {ECO:0000256|RuleBase:RU367127}.
FT DOMAIN 92..127
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 164..208
FT /note="WRC"
FT /evidence="ECO:0000259|PROSITE:PS51667"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 169..179
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01002"
FT MOTIF 197..204
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01002"
FT COMPBIAS 1..14
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..357
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 47230 MW; 03816FA3B3D97CC6 CRC64;
MDFDLKKCRR QAESEKEEEV EEPQHSAKIC KFFVEQPHRL QQQQPQPSSC SSVLPLFVPG
SINDSKASNM LSAFPDSTSS SSSHRLPRTL GYFSVAQRHE LELQALIFRY MLAGVAVPPE
LLHPIKKSLL SSTAPLFLHH PLQHFPHYPT SLLQAGYWGR AAMDPEPGRC RRTDGKKWRC
SRDVVAGQKY CERHMHRGRN RSRKPVETTT TKPTYTTTTT TTAAAVSSGG GSLCSNANRV
VGGGGGRPFS TVESGKYSCV CGQTPSVDLL HLNQGASSDS LPENKNFYES QKEASAGDGK
SDGHILRHFF DDWPRSENGD CGSDNSNASQ RMNPTSLSIS VAGNPPSSSS DVSLKLSTGG
GSDQGSGDPH LHQNGNIDGE HMHLNWAAGW AATQMASMGG PLAEALRSAN KNSLPTTVLH
QLQRTTNSEA NFIST
//