PKHF2_MOUSE
ID PKHF2_MOUSE Reviewed; 249 AA.
AC Q91WB4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Pleckstrin homology domain-containing family F member 2;
DE Short=PH domain-containing family F member 2;
GN Name=Plekhf2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Eye;
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).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=18288467; DOI=10.1007/s00109-007-0298-7;
RA Li C., Liu Q., Li N., Chen W., Wang L., Wang Y., Yu Y., Cao X.;
RT "EAPF/Phafin-2, a novel endoplasmic reticulum-associated protein,
RT facilitates TNF-alpha-triggered cellular apoptosis through endoplasmic
RT reticulum-mitochondrial apoptotic pathway.";
RL J. Mol. Med. 86:471-484(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-248, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-239 AND SER-248, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May play a role in early endosome fusion upstream of RAB5,
CC hence regulating receptor trafficking and fluid-phase transport (By
CC similarity). Enhances cellular sensitivity to TNF-induced apoptosis.
CC {ECO:0000250, ECO:0000269|PubMed:18288467}.
CC -!- SUBUNIT: May interact with EEA1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9H8W4}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9H8W4}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9H8W4}. Note=Colocalizes with EEA1 and RAB5 at
CC endosomal membrane fusion hot spots. May translocate to the endoplasmic
CC reticulum in the early phase of apoptosis.
CC {ECO:0000250|UniProtKB:Q9H8W4}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, stomach and thymus, as well as
CC in kidney, spleen, and skeletal muscle. Also expressed in peripheral
CC blood mononuclear cells and dendritic cells.
CC {ECO:0000269|PubMed:18288467}.
CC -!- INDUCTION: Up-regulated by TNF, bacterial lipopolysaccharides (LPS) and
CC phorbol myristate acetate (PMA) (at protein level).
CC {ECO:0000269|PubMed:18288467}.
CC -!- DOMAIN: The PH and FYVE domains may be important for TNF-induced
CC localization to the endoplasmic reticulum and for enhanced cellular
CC sensitivity to TNF-induced apoptosis. The FYVE domain is important for
CC binding to the endosomal membrane (By similarity). {ECO:0000250}.
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DR EMBL; AK033666; BAC28417.1; -; mRNA.
DR EMBL; AK154634; BAE32730.1; -; mRNA.
DR EMBL; BC016134; AAH16134.1; -; mRNA.
DR EMBL; BC039276; AAH39276.1; -; mRNA.
DR CCDS; CCDS17962.1; -.
DR RefSeq; NP_780384.1; NM_175175.4.
DR AlphaFoldDB; Q91WB4; -.
DR SMR; Q91WB4; -.
DR BioGRID; 214938; 3.
DR STRING; 10090.ENSMUSP00000054745; -.
DR iPTMnet; Q91WB4; -.
DR PhosphoSitePlus; Q91WB4; -.
DR EPD; Q91WB4; -.
DR jPOST; Q91WB4; -.
DR MaxQB; Q91WB4; -.
DR PaxDb; Q91WB4; -.
DR PeptideAtlas; Q91WB4; -.
DR PRIDE; Q91WB4; -.
DR ProteomicsDB; 288221; -.
DR Antibodypedia; 25937; 121 antibodies from 22 providers.
DR Ensembl; ENSMUST00000054776; ENSMUSP00000054745; ENSMUSG00000049969.
DR GeneID; 71801; -.
DR KEGG; mmu:71801; -.
DR UCSC; uc008ryw.2; mouse.
DR CTD; 79666; -.
DR MGI; MGI:1919051; Plekhf2.
DR VEuPathDB; HostDB:ENSMUSG00000049969; -.
DR eggNOG; KOG1729; Eukaryota.
DR GeneTree; ENSGT00940000156408; -.
DR HOGENOM; CLU_064864_1_0_1; -.
DR InParanoid; Q91WB4; -.
DR OMA; VCMRCKK; -.
DR OrthoDB; 1237900at2759; -.
DR PhylomeDB; Q91WB4; -.
DR TreeFam; TF315235; -.
DR BioGRID-ORCS; 71801; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Plekhf2; mouse.
DR PRO; PR:Q91WB4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q91WB4; protein.
DR Bgee; ENSMUSG00000049969; Expressed in granulocyte and 172 other tissues.
DR ExpressionAtlas; Q91WB4; baseline and differential.
DR Genevisible; Q91WB4; MM.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0030133; C:transport vesicle; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; 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 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Endosome; Membrane; Metal-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Transport; Zinc;
KW Zinc-finger.
FT CHAIN 1..249
FT /note="Pleckstrin homology domain-containing family F
FT member 2"
FT /id="PRO_0000251601"
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 221..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Polar residues"
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"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 44
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8W4"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 249 AA; 27755 MW; A2609E652CF21E98 CRC64;
MVDRLANSEA NTRRISIVES CFGAAGQPLT IPGRVLIGEG VLTKLCRKKP KARQFFLFND
ILVYGNIVIQ KKKYNKQHII PLENVTIDSI KDEGELRNGW LIKTPTKSFA VYAATATEKS
EWMNHINKCV TDLLSKSGKT PSNEHAAVWV PDSEATVCMR CQKAKFTPVN RRHHCRKCGF
VVCGPCSEKR FLLPSQSSKP VRICDFCYDL LSTGDMAACQ PTRSDSYSQS LKSPLNDASD
DDDDDDSSD
