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ARRD4_RAT
ID   ARRD4_RAT               Reviewed;         300 AA.
AC   Q7TP90;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Arrestin domain-containing protein 4;
DE   AltName: Full=Liver regeneration-related protein LRRG041/LRRGT00117;
GN   Name=Arrdc4; ORFNames=Ab1-209;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RA   Xu C.S., Zhang L., Chang C.F., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y.,
RA   Yang K.J., Zhao L.F., Ma H., Wang L., Wang S.F., Xing X.K., Shen G.M.,
RA   Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
RT   "Liver regeneration after PH.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions as an adapter recruiting ubiquitin-protein ligases
CC       to their specific substrates. Plays a role in endocytosis of activated
CC       G protein-coupled receptors (GPCRs) Through an ubiquitination-dependent
CC       mechanism also plays a role in the incorporation of SLC11A2 into
CC       extracellular vesicles. May play a role in glucose uptake.
CC       {ECO:0000250|UniProtKB:A0A0B4J1F4}.
CC   -!- SUBUNIT: Interacts with ADRB2. Interacts (via PPxY motifs) with ITCH,
CC       NEDD4L and WWP2. Interacts with AVPR2. Identified in a complex
CC       containing at least ARRDC4, AVPR2 and HGS. Interacts with SLC11A2;
CC       controls the incorporation of SLC11A2 into extracellular vesicles
CC       through an ubiquitination-dependent mechanism.
CC       {ECO:0000250|UniProtKB:A0A0B4J1F4, ECO:0000250|UniProtKB:Q8NCT1}.
CC   -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:Q8NCT1}.
CC       Cell membrane {ECO:0000250|UniProtKB:Q8NCT1}; Peripheral membrane
CC       protein {ECO:0000250|UniProtKB:Q8NCT1}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q8NCT1}. Cytoplasmic vesicle
CC       {ECO:0000250|UniProtKB:Q8NCT1}. Note=Also found in extracellular
CC       vesicles different from exosomes. {ECO:0000250|UniProtKB:A0A0B4J1F4}.
CC   -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR   EMBL; AY325151; AAP92552.1; -; mRNA.
DR   EMBL; AY539868; AAS66208.1; -; mRNA.
DR   RefSeq; NP_001041318.1; NM_001047853.1.
DR   AlphaFoldDB; Q7TP90; -.
DR   SMR; Q7TP90; -.
DR   STRING; 10116.ENSRNOP00000045721; -.
DR   PaxDb; Q7TP90; -.
DR   GeneID; 293019; -.
DR   KEGG; rno:293019; -.
DR   CTD; 91947; -.
DR   RGD; 1311763; Arrdc4.
DR   eggNOG; KOG3780; Eukaryota.
DR   HOGENOM; CLU_039221_1_0_1; -.
DR   InParanoid; Q7TP90; -.
DR   PRO; PR:Q7TP90; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000010775; Expressed in esophagus and 19 other tissues.
DR   ExpressionAtlas; Q7TP90; baseline and differential.
DR   Genevisible; Q7TP90; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; ISO:RGD.
DR   GO; GO:1903561; C:extracellular vesicle; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR   GO; GO:0140112; P:extracellular vesicle biogenesis; ISS:UniProtKB.
DR   GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; ISO:RGD.
DR   GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   Gene3D; 2.60.40.640; -; 2.
DR   InterPro; IPR014752; Arrestin-like_C.
DR   InterPro; IPR011021; Arrestin-like_N.
DR   InterPro; IPR011022; Arrestin_C-like.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF02752; Arrestin_C; 1.
DR   Pfam; PF00339; Arrestin_N; 1.
DR   SMART; SM01017; Arrestin_C; 1.
DR   SUPFAM; SSF81296; SSF81296; 2.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasmic vesicle; Endosome; Membrane; Reference proteome;
KW   Repeat.
FT   CHAIN           1..300
FT                   /note="Arrestin domain-containing protein 4"
FT                   /id="PRO_0000244354"
FT   MOTIF           231..234
FT                   /note="PPxY motif 1"
FT                   /evidence="ECO:0000305"
FT   MOTIF           276..279
FT                   /note="PPxY motif 2"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   300 AA;  33275 MW;  1EA8AA47BBD27E8A CRC64;
     MSSQSSILVD FRPLATSFTG KYGSIQYCVR AVLERPQVPD QSVRRELQVV SHVDVNTPPL
     LTPMLKTQEK MVGCWLFTSG PVSLSVKIER KGYCNGEAIP IYAEIENCSS RLVVPKAAIF
     QTQTYLASGK TKTVRHMVAN VRGNHIGSGS TDTWNGKMLK IPPVTPSILD CCIIRVYIHI
     PGAKKLMLEL PLVIGTIPYS GFGRRNSSMA SQFSMDMCWL ALALPEQPEA PPNYADVVSE
     EEFSRHIPPY PQPSACDGEA CYSMFACIQE FRFQPPPLYS ESHAQLFCLQ PVGPTNRAHF
 
 
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