LST2_MOUSE
ID LST2_MOUSE Reviewed; 905 AA.
AC Q6ZPK7; B2RSX8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Lateral signaling target protein 2 homolog;
DE AltName: Full=Zinc finger FYVE domain-containing protein 28;
GN Name=Zfyve28; Synonyms=Kiaa1643, Lst2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=19460345; DOI=10.1016/j.devcel.2009.03.015;
RA Mosesson Y., Chetrit D., Schley L., Berghoff J., Ziv T., Carvalho S.,
RA Milanezi F., Admon A., Schmitt F., Ehrlich M., Yarden Y.;
RT "Monoubiquitinylation regulates endosomal localization of Lst2, a negative
RT regulator of EGF receptor signaling.";
RL Dev. Cell 16:687-698(2009).
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 -!- SUBUNIT: Interacts with TRIM3. {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 -!- TISSUE SPECIFICITY: Enriched in brain (at protein level).
CC {ECO:0000269|PubMed:19460345}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98224.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129414; BAC98224.1; ALT_INIT; mRNA.
DR EMBL; BC139050; AAI39051.1; -; mRNA.
DR EMBL; BC139051; AAI39052.1; -; mRNA.
DR CCDS; CCDS39068.1; -.
DR RefSeq; NP_001015039.1; NM_001015039.1.
DR AlphaFoldDB; Q6ZPK7; -.
DR SMR; Q6ZPK7; -.
DR STRING; 10090.ENSMUSP00000092464; -.
DR iPTMnet; Q6ZPK7; -.
DR PhosphoSitePlus; Q6ZPK7; -.
DR PaxDb; Q6ZPK7; -.
DR PRIDE; Q6ZPK7; -.
DR ProteomicsDB; 252681; -.
DR Antibodypedia; 22351; 93 antibodies from 20 providers.
DR DNASU; 231125; -.
DR Ensembl; ENSMUST00000094868; ENSMUSP00000092464; ENSMUSG00000037224.
DR GeneID; 231125; -.
DR KEGG; mmu:231125; -.
DR UCSC; uc008xca.1; mouse.
DR CTD; 57732; -.
DR MGI; MGI:2684992; Zfyve28.
DR VEuPathDB; HostDB:ENSMUSG00000037224; -.
DR eggNOG; KOG1819; Eukaryota.
DR GeneTree; ENSGT00940000157217; -.
DR HOGENOM; CLU_007360_1_0_1; -.
DR InParanoid; Q6ZPK7; -.
DR OMA; PELGYDR; -.
DR OrthoDB; 451347at2759; -.
DR PhylomeDB; Q6ZPK7; -.
DR TreeFam; TF320752; -.
DR BioGRID-ORCS; 231125; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Zfyve28; mouse.
DR PRO; PR:Q6ZPK7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6ZPK7; protein.
DR Bgee; ENSMUSG00000037224; Expressed in retinal neural layer and 106 other tissues.
DR ExpressionAtlas; Q6ZPK7; baseline and differential.
DR Genevisible; Q6ZPK7; MM.
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 1: Evidence at protein level;
KW Cytoplasm; Endosome; Isopeptide bond; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..905
FT /note="Lateral signaling target protein 2 homolog"
FT /id="PRO_0000378953"
FT ZN_FING 835..895
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 354..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 841
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 844
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 857
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 860
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 865
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 868
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 887
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 890
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCC9"
FT MOD_RES 512
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCC9"
FT MOD_RES 888
FT /note="Phosphothreonine; by MAP2K"
FT /evidence="ECO:0000250|UniProtKB:Q9HCC9"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9HCC9"
SQ SEQUENCE 905 AA; 99787 MW; E713EAB3E4DB0FEB CRC64;
MMNRFRKWLY KPKRSDPQLL AQFYYADEEL NQVAAELDSL DGRKEPQRCT LLVSQFRSCQ
DNVLNIINQI MEECIPQDRA PRDFCVKFPE EIRHDNLAGQ LWFGAECLAA GSIIMNRELE
SMAMRPLAKE LTRSLEDVRG TLRDQALRDL NTYTEKMREA LRRFDVLFAE FELSYVSAMV
PVKSPREYYV QQEVIVLFCE TVERALDFGY LTQDMIDDYE PALMFTIPRL AIVCGLVVYA
DGPLNLDRKV EDMSELFRPF HTLLRKIRDL LQALTEEELH TLERSLCVSQ DVELPIRADT
QAPSALAPTF SASLPPEETL SASANNPEAE LACSMQYDDQ ELEELSRMVH RAGDEMSSLL
SPPSACQSPA HRPGSEASPR GEASPARARL KSGSDEEERV FFMDDVEVTE SPARPESPGN
TFELTQGNAQ QRGQDGQSGE VGVEAPALVK EEDWSNNNVE GDKIKLASLM GSTSCSCLDS
QLYLDGWEVS AEDAETAEMI AHRTGGMKLS ATVIFNPKSP TSQDSAVAAQ EAPGHGTSPL
EPRAEGTGDN SHKLSTTATN CLLHSCVCCG SCGDSRDDAV ERLREKCGPG SVISASNPSV
SLAKGGDKEP ERIDEAQPSD VTLPAEDASN RQEPKAPASS KCLAHTSGPQ VDTASRLQGE
GEVKGQPEPE ARKQDPEKSP VVSGDSPRGD VAQTEHQHLL GSSSTVGSCS LDNTRLDVAT
AAMPVTPMAT REKIRSRFHG SHDLIHRLFV CISGVADQLQ TNYASDLRSI LKTLFEVMAT
KPETDDKEKL KKVTQTLRSA ALEDCALCQE TVSSSELAAK TRDGDFEDPP EWVPDEACGF
CTSCKAPFTV IRRKHHCRSC GKIFCSRCSS HSAPLPRYGQ VKPVRVCTHC YMFHVTPFYS
DKTGM
