ID F4W9K2_ACREC Unreviewed; 835 AA.
AC F4W9K2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Hepatocyte growth factor-regulated tyrosine kinase substrate {ECO:0000256|ARBA:ARBA00015450, ECO:0000256|PIRNR:PIRNR036956};
GN ORFNames=G5I_02154 {ECO:0000313|EMBL:EGI69120.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI69120.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential role in endosome membrane invagination and
CC formation of multivesicular bodies, MVBs. Required during gastrulation
CC and appears to regulate early embryonic signaling pathways. Inhibits
CC tyrosine kinase receptor signaling by promoting degradation of the
CC tyrosine-phosphorylated, active receptor, potentially by sorting
CC activated receptors into MVBs. The MVBs are then trafficked to the
CC lysosome where their contents are degraded.
CC {ECO:0000256|PIRNR:PIRNR036956}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000256|PIRNR:PIRNR036956}. Cytoplasm, perinuclear region
CC {ECO:0000256|PIRNR:PIRNR036956}.
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DR EMBL; GL888032; EGI69120.1; -; Genomic_DNA.
DR RefSeq; XP_011068926.1; XM_011070624.1.
DR AlphaFoldDB; F4W9K2; -.
DR STRING; 103372.F4W9K2; -.
DR EnsemblMetazoa; XM_011070624.1; XP_011068926.1; LOC105154858.
DR GeneID; 105154858; -.
DR KEGG; aec:105154858; -.
DR eggNOG; KOG1818; Eukaryota.
DR InParanoid; F4W9K2; -.
DR OrthoDB; 922060at2759; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd15720; FYVE_Hrs; 1.
DR CDD; cd21387; GAT_Hrs; 1.
DR CDD; cd03569; VHS_Hrs; 1.
DR Gene3D; 1.20.5.1940; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR017073; HGS/VPS27.
DR InterPro; IPR024641; HRS_helical.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002014; VHS_dom.
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; PTHR46275; HEPATOCYTE GROWTH FACTOR-REGULATED TYROSINE KINASE SUBSTRATE; 1.
DR PANTHER; PTHR46275:SF1; HEPATOCYTE GROWTH FACTOR-REGULATED TYROSINE KINASE SUBSTRATE; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF12210; Hrs_helical; 1.
DR Pfam; PF00790; VHS; 1.
DR PIRSF; PIRSF036956; Hrs_Vps27; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS50179; VHS; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EGI69120.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Transferase {ECO:0000313|EMBL:EGI69120.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 15..143
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT DOMAIN 160..220
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 287..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 458..541
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 358..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 835 AA; 93353 MW; 94CE86713E178168 CRC64;
MFRSSTNFDK LLDKATSHLQ LEPDWPTIMQ ICDLIRQSDV QPKAALTAIK KKMINSNPHV
ALYALLVLES CVKNCGTLIH DEIATKQYME QLKELVKTSP HENVRLKTLE LIQAWAHAFR
HSPKYRTVQD TLNIMKAEGY QFPALKESDA MFRADTAPAW ADGEVCHRCR VTFSMVQRKH
HCRACGQVFC GQCSSKVSTL PKFGIEKEVR VCEACYEQVN KPSTTQAKDT DLPAEYLKST
LAQQQQILQL NGTYVRVPKL THVPVRKTEE ELREEEELNL AIALSQSEAE QKEKEKKRAT
SVLKSNSTSI SRTTYSPPPS PGPSPSQVQD DDEIEPELAK YLNRKYWEQR QTANEDHGSR
VDVTSPSAPN ISSPMPQKLI LIKQENGEID TQMEEFVRGL RSQVEIFVNR MKSNSSRGRS
IANDSSVQTL FMNITAMHSR LLRYIQEQDD SRVYYEGLQD KLTQMKDARA ALDALREEHK
EKLRRRAEEA ERQRQMLMAQ KLAIMRKKKQ EYLQYQRQLA LRKIQEQERE MQMRQEQQKQ
QYIMGSYQGI PDFMGPSQGS PVRHVHYPNP GTNYNPMSPT NQGVYMYGQP AMSQYPMQGY
NMPPMSTLPV HMMPSLSNPE QQSPDPSIQG QENISHVSIS GPGIIPPQMT PSIQQLQPPS
NHQIEPPQGP TVHMSSGQTS AGRHISPQQG ASSQMPQQVS PLTQIRLPPI PQGHMGSSSG
PMASGSHVPT GAIVGLSSQI GSQSSTLPGT QGASIPTHVS NTAISSQPSG VIQVPSVGAN
SGPVPAASQT LPGSQTPNVP TMQGMGCHFN LLLQSQLQLT KLLKMQKKQN LEQQS
//