GenomeNet

Database: UniProt
Entry: Q0V8S0
LinkDB: Q0V8S0
Original site: Q0V8S0 
ID   HGS_BOVIN               Reviewed;         777 AA.
AC   Q0V8S0; Q2NKZ6;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   29-OCT-2014, entry version 75.
DE   RecName: Full=Hepatocyte growth factor-regulated tyrosine kinase substrate;
GN   Name=HGS;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in intracellular signal transduction mediated
CC       by cytokines and growth factors. When associated with STAM it
CC       suppresses DNA signaling upon stimulation by IL-2 and GM-CSF.
CC       Could be a direct effector of PI3-kinase in vesicular pathway via
CC       early endosomes and may regulate trafficking to early and late
CC       endosomes by recruiting clathrin. May concentrate ubiquitinated
CC       receptors within clathrin-coated regions. Involved in down-
CC       regulation of receptor tyrosine kinase via multivesicular body
CC       (MVBs) when complexed with STAM (ESCRT-0 complex). The ESCRT-0
CC       complex binds ubiquitin and acts as sorting machinery that
CC       recognizes ubiquitinated receptors and transfers them to further
CC       sequential lysosomal sorting/trafficking processes. May contribute
CC       to the efficient recruitment of SMADs to the activin receptor
CC       complex. Involved in receptor recycling via its association with
CC       the CART complex, a multiprotein complex required for efficient
CC       transferrin receptor recycling but not for EGFR degradation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the ESCRT-0 complex composed of STAM or
CC       STAM2 and HGS. Part of a complex at least composed of HSG, STAM2
CC       (or probably STAM) and EPS15. Interacts with STAM. Interacts with
CC       STAM2. Interacts with EPS15; the interaction is direct, calcium-
CC       dependent and inhibited by SNAP25. Interacts with NF2; the
CC       interaction is direct. Interacts with ubiquitin; the interaction
CC       is direct. Interacts with VPS37C. Interacts with SMAD1, SMAD2 and
CC       SMAD3. Interacts with TSG101. Interacts with SNAP25; the
CC       interaction is direct and decreases with addition of increasing
CC       concentrations of free calcium. Interacts with SNX1; the
CC       interaction is direct. Component of a 550 kDa membrane complex at
CC       least composed of HGS and SNX1 but excluding EGFR. Component of
CC       the CART complex, at least composed of ACTN4, HGS/HRS, MYO5B and
CC       TRIM3. Interacts with TRAK2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Early endosome membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Endosome, multivesicular body
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- DOMAIN: Has a double-sided UIM that can bind 2 ubiquitin
CC       molecules, one on each side of the helix. {ECO:0000250}.
CC   -!- DOMAIN: The FYVE-type zinc finger domain mediates interactions
CC       with phosphatidylinositol 3-phosphate in membranes of early
CC       endosomes and penetrates bilayers. The FYVE domain insertion into
CC       PtdIns(3)P-enriched membranes is substantially increased in acidic
CC       conditions (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated on Tyr-334. A minor site of phosphorylation on
CC       Tyr-329 is detected (By similarity). Phosphorylation occurs in
CC       response to EGF, IL-2, GM-CSF and HGF. {ECO:0000250}.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC       {ECO:0000255|PROSITE-ProRule:PRU00091}.
CC   -!- SIMILARITY: Contains 1 UIM (ubiquitin-interacting motif) repeat.
CC       {ECO:0000255|PROSITE-ProRule:PRU00213}.
CC   -!- SIMILARITY: Contains 1 VHS domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00218}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BT026148; ABG66987.1; -; mRNA.
DR   EMBL; BC111313; AAI11314.1; -; mRNA.
DR   RefSeq; NP_001039554.1; NM_001046089.1.
DR   RefSeq; XP_005221090.1; XM_005221033.1.
DR   UniGene; Bt.6724; -.
DR   ProteinModelPortal; Q0V8S0; -.
DR   SMR; Q0V8S0; 6-221.
DR   STRING; 9913.ENSBTAP00000000527; -.
DR   PaxDb; Q0V8S0; -.
DR   PRIDE; Q0V8S0; -.
DR   Ensembl; ENSBTAT00000000527; ENSBTAP00000000527; ENSBTAG00000000411.
DR   GeneID; 511582; -.
DR   KEGG; bta:511582; -.
DR   CTD; 9146; -.
DR   eggNOG; NOG257212; -.
DR   GeneTree; ENSGT00670000098022; -.
DR   HOGENOM; HOG000044175; -.
DR   HOVERGEN; HBG062917; -.
DR   InParanoid; Q0V8S0; -.
DR   KO; K12182; -.
DR   OMA; ERMRQKS; -.
DR   OrthoDB; EOG7N37CN; -.
DR   TreeFam; TF314470; -.
DR   Reactome; REACT_212419; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   Reactome; REACT_217186; EGFR downregulation.
DR   NextBio; 20869998; -.
DR   GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IEA:Ensembl.
DR   Gene3D; 1.25.40.90; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR024641; HRS_helical.
DR   InterPro; IPR017073; Ubi-bd_Hrs_VPS27.
DR   InterPro; IPR003903; Ubiquitin-int_motif.
DR   InterPro; IPR002014; VHS.
DR   InterPro; IPR018205; VHS_subgr.
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   Pfam; PF12210; Hrs_helical; 1.
DR   Pfam; PF00790; VHS; 1.
DR   PIRSF; PIRSF036956; Hrs_Vps27; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00726; UIM; 1.
DR   SMART; SM00288; VHS; 1.
DR   SUPFAM; SSF48464; SSF48464; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS50179; VHS; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Complete proteome; Cytoplasm; Endosome; Membrane;
KW   Metal-binding; Phosphoprotein; Protein transport; Reference proteome;
KW   Transport; Zinc; Zinc-finger.
FT   CHAIN         1    777       Hepatocyte growth factor-regulated
FT                                tyrosine kinase substrate.
FT                                /FTId=PRO_0000274196.
FT   DOMAIN       15    143       VHS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00218}.
FT   REPEAT      258    277       UIM.
FT   ZN_FING     160    220       FYVE-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00091}.
FT   REGION      225    541       Interaction with SNX1. {ECO:0000250}.
FT   REGION      443    541       Interaction with SNAP25 and TRAK2.
FT                                {ECO:0000250}.
FT   REGION      452    570       Interaction with STAM1. {ECO:0000250}.
FT   REGION      478    777       Interaction with NF2. {ECO:0000250}.
FT   COMPBIAS    503    772       Gln-rich.
FT   MOD_RES     207    207       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     308    308       Phosphotyrosine. {ECO:0000250}.
FT   MOD_RES     329    329       Phosphotyrosine. {ECO:0000250}.
FT   MOD_RES     334    334       Phosphotyrosine. {ECO:0000250}.
FT   MOD_RES     549    549       N6-succinyllysine. {ECO:0000250}.
FT   CONFLICT    321    321       D -> E (in Ref. 2; AAI11314).
FT                                {ECO:0000305}.
FT   CONFLICT    392    392       Missing (in Ref. 2; AAI11314).
FT                                {ECO:0000305}.
SQ   SEQUENCE   777 AA;  85786 MW;  13DD0CE832AD56B4 CRC64;
     MGRGSGTFER LLDKATSQLL LETDWESILQ ICDLIRQGDT QAKYAVSSIK KKVNDKNPHV
     ALYALEVMES VVKNCGQTVH DEVANKQTME ELKDLLKRQV EVNVRNKILY LIQAWAHAFR
     NEPKYKVVQD TYQIMKVEGH VFPEFKESDA MFAAERAPDW VDAEECHRCR VQFGVMTRKH
     HCRACGQIFC GKCSSKYSTI PKFGIEKEVR VCEPCFEQLN KKAEGKAAST TELPPEYLTS
     PLSQQSQLPP KRDETALQEE EELQLALALS QSEAEEKERM RQKSAYTAYP KAEPTPVASS
     APPASSLYSS PVNSSAPLAE DIDPELARYL NRNYWEKKQE EARKSPTPSA PVPLTEPTAQ
     PGEGHAIPAN VETSLPETDP QAVTAAGAAF SEQYQNGESE ESHAQFLKAL QNAVTTFVNR
     MKSNHVRGRS ITNDSAVLSL FQSINTMHPQ LLELLNQLDE RRLYYEGLQD KLAQIRDARG
     ALSALREEHR EKLRRAAEEA ERQRQIQLAQ KLEIMRQKKQ EYLEVQRQLA IQRLQEQEKE
     RQMRLEQQKQ TIQMRAQMPA FSLPYAQLQA MPAAGGVLYQ PSGPASFAGT FSPAGSVEGS
     PMHTMYMSQP APAASGPYPS MPAAAADPSM VSAYMYPAGA AGAQAAAQGP AGPTTSPAYS
     SYQPTPTQGY QTVASQAPQS LPAISQPPQS GTMGYMGSQS VSMGYQPYSM QNLMPTLPGQ
     DAPLPPPQQP YISGQQPVYQ QMAPSSGPPQ QQPPVAQQPP AQGPPAQGSE AQLISFD
//
DBGET integrated database retrieval system