ID   LST2_XENTR              Reviewed;         951 AA.
AC   Q0P4S0;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Lateral signaling target protein 2 homolog;
DE   AltName: Full=Zinc finger FYVE domain-containing protein 28;
GN   Name=zfyve28; Synonyms=lst2;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-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; BC121929; AAI21930.1; -; mRNA.
DR   RefSeq; NP_001072498.1; NM_001079030.1.
DR   AlphaFoldDB; Q0P4S0; -.
DR   SMR; Q0P4S0; -.
DR   STRING; 8364.ENSXETP00000014953; -.
DR   PaxDb; Q0P4S0; -.
DR   PRIDE; Q0P4S0; -.
DR   GeneID; 779953; -.
DR   KEGG; xtr:779953; -.
DR   CTD; 57732; -.
DR   Xenbase; XB-GENE-1219057; zfyve28.
DR   eggNOG; KOG1819; Eukaryota.
DR   InParanoid; Q0P4S0; -.
DR   OrthoDB; 451347at2759; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; 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..951
FT                   /note="Lateral signaling target protein 2 homolog"
FT                   /id="PRO_0000378955"
FT   ZN_FING         881..941
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          360..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          641..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        641..670
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..706
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        708..726
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         887
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         890
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         903
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         906
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         911
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         914
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         933
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         936
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   951 AA;  106143 MW;  649616877F720657 CRC64;
     MMNRFRKWLY KPKRSDPQLL AQFYYADEEL NQVAAELDSL DGRKDPQRCT LLVNQFRSCQ
     DNVLNIINQI MEECIAHERA NRDFCVKFPE EIRHDNLAGQ LWFGAECLAA GSIIMNREIE
     SMAMRPLAKD LTRSLEEVRN LIRDQALRDL NIYTEKMKES LRHFDVLFAE FELSYVSAMV
     PVKSPKEYYV QQEVIVLFCE TVERALKLGY LTQDMIDDYE PALMFTIPRL AIVCGLVVYA
     EGPLNLERKP EDMSELFRPF HTLLRKIRDL LQTLTEDELH TLERNLCISQ DVEFPANADP
     EVPSAISPVL VTALPTEEPP MAKAENTEVE LACSMQYDEQ ELEQLNMMVH RVGDEMSSLL
     SPPSVYQSPA HRANTSNEAS PCRRALDNLT DEEDRVFFME DLDGSGEVLA RSRPSETTIS
     WVNNSCYNAK QPALYQDSVL QNGDLADVVS VKDGQRDISN NNNIDGSKML AASASLQNSC
     SCLEAPESQL YLNGWDTNGE DAETAEIIAH RTGGMKISAT VIFNPKSLTN SPETSPNLAS
     NRIPSSSDPL TSNEEDESHK LSIAATNCLI NSCVCCGSCE DTREDSLEGL RNVPSSGKVI
     NASYSLIKSK ELGHLDRSDC TVSAKELLKM DSPTVLLAEK ETTRQEQPYP NSSKCLPLNS
     GSQVEMDSES DEPLTASRDQ LRSESNRQET GNKERPSEEV EEPPSDRASA DNITSSSSSQ
     DGLRDSALSS ISSSDYESVS VTTCSLSSID SLSSCSSDDI DQEEIQLALQ AAKIASRQKI
     RSRFHSSNDL IHRLFVCISG VADQLQTNYA SDLRSILKTL FEVMATKQET DDKGKQKKAN
     QGLRSAALED CALCQETITS SELAAKARDG EFEDPPDWVP DEVCSLCTAC KAPFTVIRRK
     HHCRSCGKIF CSRCSSHSAP LPRYGQMKPV RVCTHCYMFH VTPFYSDRAG M