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PKHF1_RAT
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   03-AUG-2022, entry version 125.
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; Q68FU1; -.
DR   Ensembl; ENSRNOT00000020383; ENSRNOP00000020352; ENSRNOG00000027724.
DR   Ensembl; ENSRNOT00000108120; ENSRNOP00000081760; ENSRNOG00000027724.
DR   Ensembl; ENSRNOT00000113101; ENSRNOP00000091851; ENSRNOG00000027724.
DR   GeneID; 308543; -.
DR   KEGG; rno:308543; -.
DR   UCSC; RGD:1310544; rat.
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; VSWSAFH; -.
DR   OrthoDB; 1237900at2759; -.
DR   PhylomeDB; Q68FU1; -.
DR   TreeFam; TF315235; -.
DR   PRO; PR:Q68FU1; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000027724; Expressed in heart and 20 other 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; -; 1.
DR   Gene3D; 3.30.40.10; -; 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   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF57903; SSF57903; 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
 
 
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