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Database: UniProt
Entry: F4W9K2_ACREC
LinkDB: F4W9K2_ACREC
Original site: F4W9K2_ACREC 
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
//
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