ID   ZFY21_BOVIN             Reviewed;         254 AA.
AC   Q05B78;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Zinc finger FYVE domain-containing protein 21;
GN   Name=ZFYVE21;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Brain cortex;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) 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}.
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DR   EMBL; BC122654; AAI22655.1; -; mRNA.
DR   RefSeq; NP_001073055.1; NM_001079587.1.
DR   AlphaFoldDB; Q05B78; -.
DR   SMR; Q05B78; -.
DR   STRING; 9913.ENSBTAP00000041951; -.
DR   PaxDb; Q05B78; -.
DR   Ensembl; ENSBTAT00000044457; ENSBTAP00000041951; ENSBTAG00000003556.
DR   GeneID; 511413; -.
DR   KEGG; bta:511413; -.
DR   CTD; 79038; -.
DR   VEuPathDB; HostDB:ENSBTAG00000003556; -.
DR   VGNC; VGNC:55897; ZFYVE21.
DR   eggNOG; ENOG502QRR6; Eukaryota.
DR   GeneTree; ENSGT00940000159639; -.
DR   HOGENOM; CLU_103398_0_0_1; -.
DR   InParanoid; Q05B78; -.
DR   OMA; KRPAAAW; -.
DR   OrthoDB; 1256682at2759; -.
DR   Proteomes; UP000009136; Chromosome 21.
DR   Bgee; ENSBTAG00000003556; Expressed in bone marrow and 103 other tissues.
DR   ExpressionAtlas; Q05B78; baseline.
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; 2.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cytoplasmic vesicle; Endosome; Metal-binding;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..254
FT                   /note="Zinc finger FYVE domain-containing protein 21"
FT                   /id="PRO_0000281916"
FT   ZN_FING         44..104
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          107..254
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   254 AA;  27997 MW;  341861C48F25A483 CRC64;
     MSSEVAARRD AKKLVRSPSG LRMVPEHRAY GSPFGLEEPP WVPDKECPRC MQCDTKFDFL
     TRKHHCRRCG KCFCDKCCGQ KVALRRMCFV DPVRQCAGCA PVSRREADFY DRQLKLLLSG
     ATFLVTFENS EKPDTMVCRL SSNQRFLLLD GDGDGDGHRE VEVARIAAVQ MLTEGLPPGD
     TLSHTSLPAS RPAAEGGNAR AIGMTLQYTT PGAEGLTQLT LTAGEDADGS RRQATAWLAA
     MHKAAKLLYE SRDQ