ID PKHF1_RAT Reviewed; 279 AA.
AC Q68FU1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=Pleckstrin homology domain-containing family F member 1;
DE Short=PH domain-containing family F member 1;
GN Name=Plekhf1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May induce apoptosis through the lysosomal-mitochondrial
CC pathway. Translocates to the lysosome initiating the permeabilization
CC of lysosomal membrane (LMP) and resulting in the release of CTSD and
CC CTSL to the cytoplasm. Triggers the caspase-independent apoptosis by
CC altering mitochondrial membrane permeabilization (MMP) resulting in the
CC release of PDCD8 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Lysosome {ECO:0000250}. Note=Translocates to
CC lysosome during apoptosis. {ECO:0000250}.
CC -!- DOMAIN: PH and FYVE-type zinc finger domains are required for lysosomal
CC location. {ECO:0000250}.
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DR EMBL; BC079354; AAH79354.1; -; mRNA.
DR RefSeq; NP_001013166.1; NM_001013148.1.
DR RefSeq; XP_006228967.1; XM_006228905.3.
DR AlphaFoldDB; Q68FU1; -.
DR SMR; Q68FU1; -.
DR STRING; 10116.ENSRNOP00000020352; -.
DR PhosphoSitePlus; Q68FU1; -.
DR PaxDb; 10116-ENSRNOP00000020352; -.
DR Ensembl; ENSRNOT00000020383.6; ENSRNOP00000020352.3; ENSRNOG00000027724.5.
DR Ensembl; ENSRNOT00000108120.1; ENSRNOP00000081760.1; ENSRNOG00000027724.5.
DR Ensembl; ENSRNOT00000113101.1; ENSRNOP00000091851.1; ENSRNOG00000027724.5.
DR Ensembl; ENSRNOT00065055614; ENSRNOP00065045780; ENSRNOG00065032307.
DR Ensembl; ENSRNOT00065055619; ENSRNOP00065045785; ENSRNOG00065032307.
DR Ensembl; ENSRNOT00065055627; ENSRNOP00065045793; ENSRNOG00065032307.
DR GeneID; 308543; -.
DR KEGG; rno:308543; -.
DR UCSC; RGD:1310544; rat.
DR AGR; RGD:1310544; -.
DR CTD; 79156; -.
DR RGD; 1310544; Plekhf1.
DR eggNOG; KOG1729; Eukaryota.
DR GeneTree; ENSGT00940000160728; -.
DR HOGENOM; CLU_064864_2_0_1; -.
DR InParanoid; Q68FU1; -.
DR OMA; ICMRCTH; -.
DR OrthoDB; 5385125at2759; -.
DR PhylomeDB; Q68FU1; -.
DR TreeFam; TF315235; -.
DR PRO; PR:Q68FU1; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000027724; Expressed in heart and 20 other cell types or tissues.
DR Genevisible; Q68FU1; RN.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:RGD.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISO:RGD.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007032; P:endosome organization; ISO:RGD.
DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:RGD.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0016050; P:vesicle organization; ISO:RGD.
DR CDD; cd15754; FYVE_PKHF1; 1.
DR CDD; cd01218; PH_Phafin2-like; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037871; PH_Phafin.
DR InterPro; IPR042762; PKHF1_FYVE.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46280:SF2; PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY F MEMBER 1; 1.
DR PANTHER; PTHR46280; PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY F MEMBER 2-RELATED; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; Lysosome; Metal-binding; Nucleus; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..279
FT /note="Pleckstrin homology domain-containing family F
FT member 1"
FT /id="PRO_0000251599"
FT DOMAIN 35..131
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 152..212
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 219..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 279 AA; 31441 MW; AC12C075B5573A76 CRC64;
MVDHLANTEI NSQRIAAVEN CFGASGQPLA LPGRVLLGEG VLTKECRKKA KPRIFFLFND
ILVYGSIVLS KRKYRSQHII PLEEVTLEPL PETLQAKNRW MIKTAKKSFV VSAASTTERQ
EWISHIEECV RRQLLATGRQ PTTEHAAPWI PDKATDICMR CTQTRFSALT RRHHCRKCGF
VVCAECSRER FLLPRLSPKP LRVCSLCYRE LAAQKRREEA KERFRGSPGQ LTHLGSTMCG
ASSGDDDDSD EDREGSGDGD WPTQVEFYAS GVSWSAFHS
//
