PKHF2_CHICK
ID PKHF2_CHICK Reviewed; 249 AA.
AC Q5ZLY5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Pleckstrin homology domain-containing family F member 2;
DE Short=PH domain-containing family F member 2;
GN Name=PLEKHF2; ORFNames=RCJMB04_4g10;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: May play a role in early endosome fusion upstream of RAB5,
CC hence regulating receptor trafficking and fluid-phase transport.
CC Enhances cellular sensitivity to TNF-induced apoptosis. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
CC Note=Colocalizes with EEA1 and RAB5 at endosomal membrane fusion hot
CC spots. May translocate to the endoplasmic reticulum in the early phase
CC of apoptosis. {ECO:0000250}.
CC -!- DOMAIN: The FYVE domain is important for binding to the endosomal
CC membrane. {ECO:0000250}.
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DR EMBL; AJ719599; CAG31258.1; -; mRNA.
DR RefSeq; NP_001026118.1; NM_001030947.1.
DR AlphaFoldDB; Q5ZLY5; -.
DR SMR; Q5ZLY5; -.
DR STRING; 9031.ENSGALP00000025718; -.
DR PaxDb; Q5ZLY5; -.
DR GeneID; 420234; -.
DR KEGG; gga:420234; -.
DR CTD; 79666; -.
DR VEuPathDB; HostDB:geneid_420234; -.
DR eggNOG; KOG1729; Eukaryota.
DR InParanoid; Q5ZLY5; -.
DR OrthoDB; 1237900at2759; -.
DR PhylomeDB; Q5ZLY5; -.
DR PRO; PR:Q5ZLY5; -.
DR Proteomes; UP000000539; Unplaced.
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: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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Endosome; Membrane; Metal-binding;
KW Protein transport; Reference proteome; Transport; Zinc; Zinc-finger.
FT CHAIN 1..249
FT /note="Pleckstrin homology domain-containing family F
FT member 2"
FT /id="PRO_0000251602"
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..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..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"
SQ SEQUENCE 249 AA; 27715 MW; D8930D75AED5374A CRC64;
MVDRLANSEA NTRRISIVEN CFGAAGQPLT IPGRVLIGEG VLTKLCRKKP KARQFFLFND
ILVYGNIVIQ KKKYNKQHII PLENVTIDSI QDEGDLRNGW LIKTPTKSFA VYAATATEKS
EWMNHINKCV SDLLSKSGKT PSNEHAAVWV PDSEATVCMR CQKAKFTPVN RRHHCRKCGF
VVCGPCSEKR FLLPSQSSKP VRICDSCYDL LSTGEMTACQ STRSDSYSQS PKSSLNDASD
DDDDEDSSD
