ID   LST2_DANRE              Reviewed;         969 AA.
AC   A0JMD2;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Lateral signaling target protein 2 homolog;
DE   AltName: Full=Zinc finger FYVE domain-containing protein 28;
GN   Name=zfyve28; Synonyms=lst2; ORFNames=zgc:152894;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Negative regulator of epidermal growth factor receptor (EGFR)
CC       signaling. Acts by promoting EGFR degradation in endosomes when not
CC       monoubiquitinated (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Early endosome membrane.
CC       Note=Localizes to early endosome membrane in absence of Lys-87
CC       monoubiquitination. Localizes to cytosol when monoubiquitinated (By
CC       similarity). {ECO:0000250}.
CC   -!- DOMAIN: The FYVE-type zinc finger mediates the interaction with
CC       phosphatidylinositol 3-phosphate (PI3P) and localization to early
CC       endosome membranes when not monoubiquitinated at Lys-87. {ECO:0000250}.
CC   -!- PTM: Monoubiquitination at Lys-87 prevents binding to
CC       phosphatidylinositol 3-phosphate (PI3P) and localization to early
CC       endosome membranes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lst-2 family. {ECO:0000305}.
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DR   EMBL; BC125831; AAI25832.1; -; mRNA.
DR   RefSeq; NP_001071191.1; NM_001077723.1.
DR   AlphaFoldDB; A0JMD2; -.
DR   SMR; A0JMD2; -.
DR   STRING; 7955.ENSDARP00000116818; -.
DR   PaxDb; A0JMD2; -.
DR   GeneID; 777615; -.
DR   KEGG; dre:777615; -.
DR   CTD; 57732; -.
DR   ZFIN; ZDB-GENE-061103-208; zfyve28.
DR   eggNOG; KOG1819; Eukaryota.
DR   InParanoid; A0JMD2; -.
DR   OrthoDB; 451347at2759; -.
DR   PhylomeDB; A0JMD2; -.
DR   PRO; PR:A0JMD2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR   GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; ISS:UniProtKB.
DR   CDD; cd15731; FYVE_LST2; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR043269; FYVE_LST2.
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   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Endosome; Isopeptide bond; Membrane; Metal-binding;
KW   Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..969
FT                   /note="Lateral signaling target protein 2 homolog"
FT                   /id="PRO_0000378954"
FT   ZN_FING         899..959
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          290..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          715..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..351
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..429
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        732..775
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         905
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         908
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         921
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         924
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         929
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         932
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         951
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         954
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   CROSSLNK        87
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   969 AA;  106964 MW;  13F951920E647048 CRC64;
     MMNRFRKWLY KPKRSDPQLL AQFYYADEEL NQVATELDSL DGRKDPQRCT LLVNQFRSCQ
     DNVLNIINQI MDECIPEERA NRDFCVKFPE EIRHDNLAGQ LWFGAECLAA GSIIMNREIE
     SMAMRPLAKD LTRSLEEVRN ITRDQALRDL NHYTERIKEA LRHFDGLFAE FELSYVSAMV
     PVKSPKEYYI QQEVIVLFCE TVERALKLEY LTQDMIDDYE PALMFTIPRL AIVCGLVIYS
     EGPLNLDRKP EDMSELFRPF RTLLRKIRDL LQTLTEEELM TLERSLCISQ DGEFPTSSTN
     DPSASTGPDS QTEELEKEKG VEEVVDLTLF VTQEDSVWKE EEEKQVLPES SSESEEEEPI
     DADLACSMQY DEEEIEQLNM MVHQVGDEMS TLLSPPSQNQ SPAHRPRPYN GSSLEGSSAT
     SSTQASPRRA PGSYHDDDRV FFMDDLESGL SSELCRGQLP LPTVCLRSPE GSSCNGWLTV
     CQSSDATNLG CQRKLSQSTE SVGNSDRMVN GWEGLQDEDS VQTAEEIANR TGGMKLSATV
     IFNPHSPSLS DLAVVLPQSA DAPEGGEGGA LVATQCLLNS CVCCAGGCVD NHEDAMEPAG
     RSMALGFEKH KLTITSSVIQ SAVAAGSPGK GNGHLPLTLP PSQGHLTHSV PNCSVQNQAR
     EDEGSQDGIH YPCCEKCSPG VLLAQDRGSG HEGGPSCTLQ DTGCQTQHNA SVKGRSECFG
     KQSKDDNRKI NSSSQESPLS SVPSSDIDGV SVTTCSLSSS YAPSPVSSLT TSSDMSEDLD
     HQEIQVALQA AKLAAHNKIR SRFHSSSDLI HRLFVCISGV ADQLQTNYAS DLRSILKTLF
     EVMATKTDQG DNEKPKKGPC LGSAVLEDCA LCQETISSSE LAAKAREGQF EDPPEWVPDE
     ACNSCIACKA PFTVIRRKHH CRSCGKIFCS RCSSHSAPLP RYGQMKPVRV CTHCYMFHVT
     PFYSDRTGI