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NED4L_PONAB
ID   NED4L_PONAB             Reviewed;         959 AA.
AC   Q5RBF2;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=E3 ubiquitin-protein ligase NEDD4-like;
DE            EC=2.3.2.26 {ECO:0000250|UniProtKB:P46934};
DE   AltName: Full=HECT-type E3 ubiquitin transferase NED4L;
GN   Name=NEDD4L;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC       E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC       directly transfers the ubiquitin to targeted substrates. Inhibits TGF-
CC       beta signaling by triggering SMAD2 and TGFBR1 ubiquitination and
CC       proteasome-dependent degradation. Promotes ubiquitination and
CC       internalization of various plasma membrane channels such as ENaC,
CC       Nav1.2, Nav1.3, Nav1.5, Nav1.7, Nav1.8, Kv1.3, KCNH2, EAAT1 or CLC5.
CC       Promotes ubiquitination and degradation of SGK1 and TNK2. Ubiquitinates
CC       BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1.
CC       Plays a role in dendrite formation by melanocytes (By similarity).
CC       Involved in the regulation of TOR signaling (By similarity).
CC       {ECO:0000250|UniProtKB:Q8CFI0, ECO:0000250|UniProtKB:Q96PU5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.26; Evidence={ECO:0000250|UniProtKB:P46934};
CC   -!- ACTIVITY REGULATION: Activated by NDFIP1- and NDFIP2-binding.
CC       {ECO:0000250|UniProtKB:Q96PU5}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with UBE2E3 (By similarity). Interacts with NDFIP1;
CC       this interaction activates the E3 ubiquitin-protein ligase (By
CC       similarity). Interacts with NDFIP2; this interaction activates the E3
CC       ubiquitin-protein ligase (By similarity). Interacts (via WW domains)
CC       with SCNN1A (By similarity). Interacts (via WW domains) with SCNN1B (By
CC       similarity). Interacts (via WW domains) with SCNN1G (By similarity).
CC       Interacts (via WW domains) with SCN1A (By similarity). Interacts (via
CC       WW domains) with SCN2A (By similarity). Interacts (via WW domains) with
CC       SCN3A (By similarity). Interacts (via WW domains) with SCN5A (By
CC       similarity). Interacts (via WW domains) with SCN8A (By similarity).
CC       Interacts (via WW domains) with SCN9A (By similarity). Interacts (via
CC       WW domains) with SCN10A (By similarity). Interacts (via WW domains)
CC       with CLCN5 (By similarity). Interacts with SMAD2 (By similarity).
CC       Interacts with SMAD3 (By similarity). Interacts with SMAD6 (By
CC       similarity). Interacts with SMAD7 (By similarity). The phosphorylated
CC       form interacts with 14-3-3 proteins (By similarity). Interacts with
CC       TNK2 (By similarity). Interacts with WNK1 (By similarity). Interacts
CC       with SGK1 (By similarity). Interacts (via C2 domain) with NPC2 (By
CC       similarity). Interacts with ARRDC4 (By similarity). Interacts with
CC       KCNQ1; promotes internalization of KCNQ1 (By similarity). Interacts
CC       (via domains WW1, 3 and 4) with USP36; the interaction inhibits
CC       ubiquitination of, at least, NTRK1, KCNQ2 and KCNQ3 by NEDD4L (By
CC       similarity). Interacts with PRRG4 (via cytoplasmic domain) (By
CC       similarity). Interacts with LDLRAD3; the interaction is direct (By
CC       similarity). {ECO:0000250|UniProtKB:Q8CFI0,
CC       ECO:0000250|UniProtKB:Q96PU5}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96PU5}. Golgi
CC       apparatus {ECO:0000250|UniProtKB:Q96PU5}. Endosome, multivesicular body
CC       {ECO:0000250|UniProtKB:Q96PU5}.
CC   -!- PTM: Phosphorylated; which impairs interaction with SCNN. Interaction
CC       with YWHAH inhibits dephosphorylation (By similarity). {ECO:0000250}.
CC   -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q96PU5}.
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DR   EMBL; CR858697; CAH90908.1; -; mRNA.
DR   RefSeq; NP_001125518.1; NM_001132046.1.
DR   AlphaFoldDB; Q5RBF2; -.
DR   BMRB; Q5RBF2; -.
DR   SMR; Q5RBF2; -.
DR   STRING; 9601.ENSPPYP00000010317; -.
DR   GeneID; 100172429; -.
DR   KEGG; pon:100172429; -.
DR   CTD; 23327; -.
DR   eggNOG; KOG0940; Eukaryota.
DR   InParanoid; Q5RBF2; -.
DR   OrthoDB; 271539at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005771; C:multivesicular body; IEA:UniProtKB-SubCell.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:1902305; P:regulation of sodium ion transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 4.
DR   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 4.
DR   PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 4.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   SUPFAM; SSF51045; SSF51045; 4.
DR   SUPFAM; SSF56204; SSF56204; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 4.
DR   PROSITE; PS50020; WW_DOMAIN_2; 4.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Differentiation; Endosome; Golgi apparatus; Phosphoprotein;
KW   Reference proteome; Repeat; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN           1..959
FT                   /note="E3 ubiquitin-protein ligase NEDD4-like"
FT                   /id="PRO_0000120325"
FT   DOMAIN          10..130
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          197..230
FT                   /note="WW 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          369..402
FT                   /note="WW 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          481..514
FT                   /note="WW 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          532..565
FT                   /note="WW 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          624..958
FT                   /note="HECT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   REGION          183..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        926
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   MOD_RES         316
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PU5"
FT   MOD_RES         322
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PU5"
FT   MOD_RES         346
FT                   /note="Phosphoserine; by WNK1 and WNK4"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PU5"
FT   MOD_RES         430
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PU5"
FT   MOD_RES         432
FT                   /note="Phosphoserine; by SGK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PU5"
FT   MOD_RES         433
FT                   /note="Phosphoserine; by WNK1 and WNK4"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PU5"
FT   MOD_RES         448
FT                   /note="Phosphoserine; by SGK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PU5"
FT   MOD_RES         459
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PU5"
FT   MOD_RES         463
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PU5"
FT   MOD_RES         467
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PU5"
FT   MOD_RES         471
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PU5"
SQ   SEQUENCE   959 AA;  110511 MW;  E328E83DC8EEB79B CRC64;
     MAPLSAALLP WHGVCVPVCY GESRILRVKV VSGIDLAKKD IFGASDPYVK LSLYVADENR
     ELALVQTKTI KKTLNPKWNE EFYFRVNPSN HRLLFEVFDE NRLTRDDFLG QVDVPLSHLP
     TEDPTMERPY TFKDFLLRPR SHKSRVKGFL RLKMAYMPKN GGQEEENSEQ RDDMEHGWEV
     VDSNDSASQH QEELPPPPLP PGWEEKVDNL GRTYYVNHNN RTTQWHRPSL MDVSSESDNN
     IRQINQEAAH RRFRSRRHIS EDLEPEPSEG GDVPEPWETI SEEVNIAGDS LGLALPPPPA
     SPGSRTSPQE LSEELSRRLQ ITPDSNGEQF SSLIQREPSS RLRSCSVTDA VAEQGHLPPP
     SVAYVHTTPG LPSGWEERKD AKGRTYYVNH NNRTTTWTRP IMQLAEDGAS GSATNSNNHL
     IEPQIRRPRS LSSPTVTLSA PLEGAKDSPV RRAVKDTLSN PQSPQPSPYN SPKPQHKVTQ
     SFLPPGWEMR IAPNGRPFFI DHNTKTTTWE DPRLKFPVHM RSKTSLNPND LGPLPPGWEE
     RIHLDGRTFY IDHNSKITQW EDPRLQNPAI TGPAVPYSRE FKQKYDYFRK KLKKPADIPN
     RFEMKLHRNN IFEESYRRIM SVKRPDVLKA RLWIEFESEK GLDYGGVARE WFFLLSKEMF
     NPYYGLFEYS ATDNYTLQIN PNSGLCNEDH LSYFTFIGRV AGLAVFHGKL LDGFFIRPFY
     KMMLGKQITL NDMESVDSEY YNSLKWILEN DPTELDLMFC IDEENFGQTY QVDLEPNGSE
     IMVTNENKRE YIDLVIQWRF VNRVQKQMNA FLEGFTELLP IDLIKIFDEN ELELLMCGLG
     DVDVNDWRQH SIYKNGYCPN HPVIQWFWKA VLLMDAEKRI RLLQFVTGTS RVPMNGFAEL
     YGSNGPQLFT IEQWGSPEKL PRAHTCFNRL DLPPYETFED LREKLLMAVE NAQGFEGVD
 
 
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