ALFIN_MEDSA
ID ALFIN_MEDSA Reviewed; 257 AA.
AC Q40359;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=PHD finger protein Alfin1;
GN Name=ALFIN-1;
OS Medicago sativa (Alfalfa).
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; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Regen S / HG2-N1; TISSUE=Callus;
RX PubMed=8108516; DOI=10.1104/pp.102.2.681;
RA Winicov I.;
RT "cDNA encoding putative zinc finger motifs from salt-tolerant alfalfa
RT (Medicago sativa L.) cells.";
RL Plant Physiol. 102:681-682(1993).
RN [2]
RP TISSUE SPECIFICITY, AND DNA-BINDING.
RX PubMed=9869418; DOI=10.1023/a:1006081926699;
RA Bastola D.R., Pethe V.V., Winicov I.;
RT "Alfin1, a novel zinc-finger protein in alfalfa roots that binds to
RT promoter elements in the salt-inducible MsPRP2 gene.";
RL Plant Mol. Biol. 38:1123-1135(1998).
RN [3]
RP FUNCTION, AND INDUCTION BY NACL.
RX PubMed=10364398; DOI=10.1104/pp.120.2.473;
RA Winicov I., Bastola D.R.;
RT "Transgenic overexpression of the transcription factor alfin1 enhances
RT expression of the endogenous MsPRP2 gene in alfalfa and improves salinity
RT tolerance of the plants.";
RL Plant Physiol. 120:473-480(1999).
RN [4]
RP FUNCTION.
RX PubMed=10750899; DOI=10.1007/pl00008150;
RA Winicov I.;
RT "Alfin1 transcription factor overexpression enhances plant root growth
RT under normal and saline conditions and improves salt tolerance in
RT alfalfa.";
RL Planta 210:416-422(2000).
CC -!- FUNCTION: Histone-binding component that specifically recognizes H3
CC tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription
CC start sites of virtually all active genes (By similarity).
CC Transcriptional regulator that binds specifically to DNA sequences 5'-
CC GNGGTG-3' or 5'-GTGGNG-3', including promoter elements of the salt-
CC inducible PRP2 gene. Plays a role in salinity tolerance. {ECO:0000250,
CC ECO:0000269|PubMed:10364398, ECO:0000269|PubMed:10750899}.
CC -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the roots.
CC {ECO:0000269|PubMed:9869418}.
CC -!- INDUCTION: By NaCl. {ECO:0000269|PubMed:10364398}.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Alfin family. {ECO:0000305}.
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DR EMBL; L07291; AAA20093.2; -; mRNA.
DR PIR; T09646; T09646.
DR AlphaFoldDB; Q40359; -.
DR SMR; Q40359; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071472; P:cellular response to salt stress; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR CDD; cd15613; PHD_AL_plant; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045104; Alfin.
DR InterPro; IPR021998; Alfin_N.
DR InterPro; IPR044104; PHD_AL_plant.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12321; PTHR12321; 1.
DR Pfam; PF12165; Alfin; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; DNA-binding; Metal-binding; Nucleus; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..257
FT /note="PHD finger protein Alfin1"
FT /id="PRO_0000412935"
FT ZN_FING 200..252
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 145..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..200
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 210
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250"
FT SITE 216
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250"
FT SITE 220
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250"
FT SITE 225
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250"
SQ SEQUENCE 257 AA; 28820 MW; 192C5EC5AA859E36 CRC64;
MEGMAQHPVP RTVEEVFSDY KGRRAGLIKA LTTDVEKFYQ LVDPEKENLC LYGFPNETWE
VNLPVEEVPP ELPEPALGIN FARDGMQEKD WLSLVAVHSD SWLLAVAFYF GARFGFGKND
RKRLFQMIND LPTVFELATG TAKQSKDQLT AHNNGSNSKY KSSGKSRQSE SQTKGVKMSA
PVKEEVDSGE EEEEDDDEQG ATCGACGDNY GTDEFWICCD MCEKWFHGKC VKITPAKAEH
IKQYKCPGCS IKKPRIG
