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Database: UniProt
Entry: ALFIN_MEDSA
LinkDB: ALFIN_MEDSA
Original site: 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   27-MAR-2024, entry version 98.
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 DNA-templated transcription; 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; Zinc/RING finger domain, C3HC4 (zinc finger); 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; CPG BINDING PROTEIN; 1.
DR   PANTHER; PTHR12321:SF60; PHD FINGER PROTEIN ALFIN-LIKE 7; 1.
DR   Pfam; PF12165; Alfin; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 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
//
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