ID   ZFY21_RAT               Reviewed;         234 AA.
AC   D3ZVP7;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Zinc finger FYVE domain-containing protein 21;
GN   Name=Zfyve21;
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 GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in cell adhesion, and thereby in cell motility
CC       which requires repeated formation and disassembly of focal adhesions.
CC       Regulates microtubule-induced PTK2/FAK1 dephosphorylation, an event
CC       important for focal adhesion disassembly, as well as integrin beta-
CC       1/ITGB1 cell surface expression (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with PTK2/FAK1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cytoplasmic
CC       vesicle {ECO:0000250}. Endosome {ECO:0000250}.
CC   -!- DOMAIN: The FYVE-type zinc finger mediates interaction with PTK2/FAK1,
CC       and also interaction with PI(3)P and association with endosomes.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal region exhibits a structure similar to canonical
CC       PH domains, but lacks a positively charged interface to bind
CC       phosphatidylinositol phosphate. {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH474034; EDL97443.1; -; Genomic_DNA.
DR   RefSeq; XP_006240704.3; XM_006240642.3.
DR   AlphaFoldDB; D3ZVP7; -.
DR   SMR; D3ZVP7; -.
DR   STRING; 10116.ENSRNOP00000059837; -.
DR   PaxDb; D3ZVP7; -.
DR   GeneID; 362789; -.
DR   UCSC; RGD:1311036; rat.
DR   CTD; 79038; -.
DR   RGD; 1311036; Zfyve21.
DR   eggNOG; ENOG502QRR6; Eukaryota.
DR   InParanoid; D3ZVP7; -.
DR   OrthoDB; 1256682at2759; -.
DR   PhylomeDB; D3ZVP7; -.
DR   TreeFam; TF329481; -.
DR   PRO; PR:D3ZVP7; -.
DR   Proteomes; UP000002494; Unplaced.
DR   Proteomes; UP000234681; Chromosome 6.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.29.160; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR032031; ZFYVE21_C.
DR   InterPro; IPR038632; ZFYVE21_C_sf.
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; PF16696; ZFYVE21_C; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   3: Inferred from homology;
KW   Cell junction; Cytoplasmic vesicle; Endosome; Metal-binding;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..234
FT                   /note="Zinc finger FYVE domain-containing protein 21"
FT                   /id="PRO_0000401195"
FT   ZN_FING         44..104
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          107..234
FT                   /note="PH-like"
FT                   /evidence="ECO:0000250"
FT   BINDING         50
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ   SEQUENCE   234 AA;  26009 MW;  1DDA0240BBAD464C CRC64;
     MSSGVAARCD AKKLVRSPSG LRMVPEHRAF GSPFGLEEPQ WVPDKECPRC MQCDAKFDFI
     TRKHHCRRCG KCFCDRCCSQ KVPLRRMCFV DPVRQCADCA LVSHREAEFY DKQLKVLVSG
     ATFLVTFGDS EKPETMVCRL SNNQRCLILD GDSHHEIEIA HVCTVQILTE GFTPGAGSTR
     ATGMFLQYTV PGAEAAAQLR LMAGEDASGS KRQAAAWLAA MHKATKLLYE SRDQ