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Database: UniProt
Entry: W5N586_LEPOC
LinkDB: W5N586_LEPOC
Original site: W5N586_LEPOC 
ID   W5N586_LEPOC            Unreviewed;       446 AA.
AC   W5N586;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Zinc finger FYVE-type containing 19 {ECO:0000313|Ensembl:ENSLOCP00000015795.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000015795.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000015795.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AHAT01019019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015206353.1; XM_015350867.1.
DR   AlphaFoldDB; W5N586; -.
DR   STRING; 7918.ENSLOCP00000015795; -.
DR   Ensembl; ENSLOCT00000015825.1; ENSLOCP00000015795.1; ENSLOCG00000012832.1.
DR   GeneID; 102690881; -.
DR   CTD; 84936; -.
DR   eggNOG; KOG1818; Eukaryota.
DR   GeneTree; ENSGT00390000016108; -.
DR   InParanoid; W5N586; -.
DR   OMA; CDGELFC; -.
DR   OrthoDB; 1459288at2759; -.
DR   Proteomes; UP000018468; Linkage group LG7.
DR   Bgee; ENSLOCG00000012832; Expressed in ovary and 13 other cell types or tissues.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0032154; C:cleavage furrow; IBA:GO_Central.
DR   GO; GO:0030496; C:midbody; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR   GO; GO:0009838; P:abscission; IBA:GO_Central.
DR   GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; IBA:GO_Central.
DR   CDD; cd19817; Bbox1_ANCHR-like; 1.
DR   CDD; cd15749; FYVE_ZFY19; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR044553; Bbox1_ANCHR.
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   PANTHER; PTHR46603; ABSCISSION/NOCUT CHECKPOINT REGULATOR; 1.
DR   PANTHER; PTHR46603:SF1; ABSCISSION_NOCUT CHECKPOINT REGULATOR; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          17..76
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          101..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   446 AA;  49307 MW;  1D1A313D270A9A3B CRC64;
     MKATSPFCLD LGLVWMNDMD SRCYGCASKF SLFKKEAACK NCGRSYCAGC LGYSCLVPRC
     GNTQQKVCKQ CHGNLTSGGT LNNAAKWSPP ENYKKRVAAL EAKQSQQGPA SRPSSKSIAP
     RLPVARGLSK EDQAIAERLE RLKEDTTPRS IPSEKEIESR LAALKVPARP IPTAAEMEDR
     LAALQGVTPP SQVPRPIHQP PDARTQTEQA SDLITQLSEE VAIDNRFAPE SGSEGVTDGP
     LNNLNKADST LDENLDDLRQ DAKQLESEKS RLLAEAMEEL KQENLGREQV LQMARRLALL
     KGQDPGKITA NDFSQPDSEE ETEEESLKRI LKQLSEEAAL DEASGYNILP EQSGPINTEK
     PTGHKKMPCA PQSRANKKIA AAAPPSDSDE EELPWCCICN EDATIRCRSC DDELYCKRCF
     REGHDDFDRK DHRTTSYKAP RKSKKK
//
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