ID F7BNL7_ORNAN Unreviewed; 744 AA.
AC F7BNL7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Hepatocyte growth factor-regulated tyrosine kinase substrate {ECO:0000256|ARBA:ARBA00015450, ECO:0000256|PIRNR:PIRNR036956};
GN Name=HGS {ECO:0000313|Ensembl:ENSOANP00000020605.3};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000020605.3, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000020605.3}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000020605.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Involved in intracellular signal transduction mediated by
CC cytokines and growth factors. When associated with STAM, it suppresses
CC DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct
CC effector of PI3-kinase in vesicular pathway via early endosomes and may
CC regulate trafficking to early and late endosomes by recruiting
CC clathrin. May concentrate ubiquitinated receptors within clathrin-
CC coated regions. Involved in down-regulation of receptor tyrosine kinase
CC via multivesicular body (MVBs) when complexed with STAM (ESCRT-0
CC complex). The ESCRT-0 complex binds ubiquitin and acts as sorting
CC machinery that recognizes ubiquitinated receptors and transfers them to
CC further sequential lysosomal sorting/trafficking processes. May
CC contribute to the efficient recruitment of SMADs to the activin
CC receptor complex. Involved in receptor recycling via its association
CC with the CART complex, a multiprotein complex required for efficient
CC transferrin receptor recycling but not for EGFR degradation.
CC {ECO:0000256|PIRNR:PIRNR036956}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR036956}. Early
CC endosome membrane {ECO:0000256|ARBA:ARBA00004469,
CC ECO:0000256|PIRNR:PIRNR036956}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004469, ECO:0000256|PIRNR:PIRNR036956};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004469,
CC ECO:0000256|PIRNR:PIRNR036956}. Endosome, multivesicular body membrane
CC {ECO:0000256|PIRNR:PIRNR036956}; Peripheral membrane protein
CC {ECO:0000256|PIRNR:PIRNR036956}.
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DR AlphaFoldDB; F7BNL7; -.
DR STRING; 9258.ENSOANP00000020605; -.
DR Ensembl; ENSOANT00000020608.4; ENSOANP00000020605.3; ENSOANG00000013033.4.
DR eggNOG; KOG1818; Eukaryota.
DR GeneTree; ENSGT00940000158297; -.
DR HOGENOM; CLU_013062_1_0_1; -.
DR InParanoid; F7BNL7; -.
DR OMA; DQQCSAK; -.
DR TreeFam; TF314470; -.
DR Proteomes; UP000002279; Unplaced.
DR Bgee; ENSOANG00000013033; Expressed in cerebellum and 7 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033565; C:ESCRT-0 complex; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IEA:Ensembl.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0010324; P:membrane invagination; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0072657; P:protein localization to membrane; IEA:Ensembl.
DR GO; GO:0006622; P:protein targeting to lysosome; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0031623; P:receptor internalization; IBA:GO_Central.
DR CDD; cd15720; FYVE_Hrs; 1.
DR CDD; cd21387; GAT_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};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR036956};
KW Endosome {ECO:0000256|PIRNR:PIRNR036956};
KW Membrane {ECO:0000256|PIRNR:PIRNR036956};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein transport {ECO:0000256|PIRNR:PIRNR036956};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW Transport {ECO:0000256|PIRNR:PIRNR036956};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 13..114
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT DOMAIN 131..191
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 210..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 441..524
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 259..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..357
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..737
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 81773 MW; 24D73FABCBE3ADCE CRC64;
MGRGGGTFER LLAKYAVSSI KKKVNDKNPH VALYALEVME SVVKNCGQTV HDEVANKQTM
EELKELLKRQ VEANVRNKIL YLVQAWAHAF RNEPKYKVVQ DTYQIMKVEG HVFPEFKESD
AMFAAERAPD WVDAEECHRC RVQFGVVTRK HHCRACGQIF CGKCSSRYST IPKFGIEKEV
RVCEPCYEQL NKKTEGKAAS ATELPPEYLT SPLSQQSQLP PKRDETALQE EEELQLAIAL
SQSEAEEKER MRQKTTYSMY PKADPTPVTS SAPAPGSLYS SPVNSSAPLA EDVDPELARY
LNRNYWEKKQ EEAGKSPTPS APVSVADAAP PPGEGHATPG PGAETPLPDP DAQPLPPSGG
PFGEQQYQNG ESEEEHEQFL KGLQNAVTTF VNRMKSNHLR GRSITNDSAV LSLFQSINNM
HPQLLHLLNQ LDERRLYYEG LQDKLAQVRD ARGALNALRD EHREKLRRAA EEAERQRQIQ
LAQKLEIMRQ KKQEYLEMQR QMAIQRLQEQ EKERQMRLEQ QKQTIQMRAQ MPAFSLPYAQ
LQAVPASGGV IYPPSGPGGF PATFSPAGSV EGSPMHTVYM TQAGGGPYPS VPAAGADPSM
VSAYMYQAGA GGGQAAQAGQ AVPTTNPAYS SYQPTPTQGY QNVASQAPQS LPPPISQPPQ
SGALGYLGNQ SVSLGYQPYG MQNLMTTLPG PDPALPPQQP YLSGQPPMYQ QMAAPGGPPQ
QPQPVAPPPP PPPGPGEAQL ISFD
//
