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EHD1_PONAB
ID   EHD1_PONAB              Reviewed;         534 AA.
AC   Q5RBP4;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=EH domain-containing protein 1 {ECO:0000305};
GN   Name=EHD1 {ECO:0000250|UniProtKB:Q9H4M9};
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=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP- and membrane-binding protein that controls membrane
CC       reorganization/tubulation upon ATP hydrolysis. Acts in early endocytic
CC       membrane fusion and membrane trafficking of recycling endosomes.
CC       Recruited to endosomal membranes upon nerve growth factor stimulation,
CC       indirectly regulates neurite outgrowth. Plays a role in myoblast
CC       fusion. Involved in the unidirectional retrograde dendritic transport
CC       of endocytosed BACE1 and in efficient sorting of BACE1 to axons
CC       implicating a function in neuronal APP processing. Plays a role in the
CC       formation of the ciliary vesicle (CV), an early step in cilium
CC       biogenesis. Proposed to be required for the fusion of distal appendage
CC       vesicles (DAVs) to form the CV by recruiting SNARE complex component
CC       SNAP29. Is required for recruitment of transition zone proteins CEP290,
CC       RPGRIP1L, TMEM67 and B9D2, and of IFT20 following DAV reorganization
CC       before Rab8-dependent ciliary membrane extension. Required for the loss
CC       of CCP110 form the mother centriole essential for the maturation of the
CC       basal body during ciliogenesis. {ECO:0000250|UniProtKB:Q641Z6,
CC       ECO:0000250|UniProtKB:Q9H4M9, ECO:0000250|UniProtKB:Q9WVK4}.
CC   -!- SUBUNIT: Homooligomer, and heterooligomer with EHD2, EHD3 and EHD4,
CC       ATP-binding is required for heterooligomerization. Interacts (via EH
CC       domain) with MICALL1 (via NPF1 motif); the interaction is direct and
CC       recruits EHD1 to membranes. Interacts with RAB35; the interaction is
CC       indirect through MICALL1 and recruits EHD1 to membranes. Interacts (via
CC       EH domain) with PACSIN2 (via NPF motifs); regulates localization to
CC       tubular recycling endosome membranes. Interacts with PACSIN1. Interacts
CC       with RAB8A. Interacts with FER1L5 (via second C2 domain). Interacts
CC       with MYOF. Interacts with ZFYVE20. Interacts (via EH domain) with
CC       RAB11FIP2. {ECO:0000250|UniProtKB:Q9H4M9,
CC       ECO:0000250|UniProtKB:Q9WVK4}.
CC   -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC       {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane
CC       {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, cilium
CC       membrane {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Preferentially
CC       associates with tubular recycling endosomes (By similarity).
CC       Colocalizes with FER1L5 at plasma membrane in myoblasts and myotubes
CC       (By similarity). Localizes to the ciliary pocket from where the cilium
CC       protrudes (By similarity). Colocalizes with BACE1 in tubulovesicular
CC       cytoplasmic membranes. Colocalizes with BACE1 and APP amyloid beta
CC       proteins in hippocampal mossy fiber terminals (By similarity).
CC       {ECO:0000250|UniProtKB:Q9H4M9, ECO:0000250|UniProtKB:Q9WVK4}.
CC   -!- DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target
CC       proteins. {ECO:0000250|UniProtKB:Q9WVK4}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. Dynamin/Fzo/YdjA family. EHD subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU01055}.
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DR   EMBL; CR858594; CAH90816.1; -; mRNA.
DR   RefSeq; NP_001125465.1; NM_001131993.1.
DR   AlphaFoldDB; Q5RBP4; -.
DR   BMRB; Q5RBP4; -.
DR   SMR; Q5RBP4; -.
DR   STRING; 9601.ENSPPYP00000003578; -.
DR   Ensembl; ENSPPYT00000003705; ENSPPYP00000003578; ENSPPYG00000003093.
DR   GeneID; 100172373; -.
DR   KEGG; pon:100172373; -.
DR   CTD; 10938; -.
DR   eggNOG; KOG1954; Eukaryota.
DR   GeneTree; ENSGT00940000158249; -.
DR   HOGENOM; CLU_017595_1_1_1; -.
DR   InParanoid; Q5RBP4; -.
DR   OMA; WYEETIL; -.
DR   OrthoDB; 377342at2759; -.
DR   TreeFam; TF314429; -.
DR   Proteomes; UP000001595; Chromosome 11.
DR   GO; GO:0020018; C:ciliary pocket membrane; ISS:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR   GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR   GO; GO:2001137; P:positive regulation of endocytic recycling; ISS:UniProtKB.
DR   GO; GO:1901741; P:positive regulation of myoblast fusion; ISS:UniProtKB.
DR   GO; GO:0061512; P:protein localization to cilium; ISS:UniProtKB.
DR   CDD; cd00052; EH; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR040990; DUF5600.
DR   InterPro; IPR045063; Dynamin_N.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR000261; EH_dom.
DR   InterPro; IPR029951; EHD1/EHD3.
DR   InterPro; IPR031692; EHD_N.
DR   InterPro; IPR030381; G_DYNAMIN_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11216:SF127; PTHR11216:SF127; 1.
DR   Pfam; PF18150; DUF5600; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF12763; EF-hand_4; 1.
DR   Pfam; PF16880; EHD_N; 1.
DR   SMART; SM00027; EH; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50031; EH; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Calcium; Cell membrane; Cell projection; Cilium;
KW   Cilium biogenesis/degradation; Coiled coil; Endosome; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..534
FT                   /note="EH domain-containing protein 1"
FT                   /id="PRO_0000306857"
FT   DOMAIN          55..286
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   DOMAIN          444..532
FT                   /note="EH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT   DOMAIN          476..511
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          65..72
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          91..92
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          153..156
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          219..222
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          243
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   COILED          198..227
FT                   /evidence="ECO:0000255"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H4M9"
FT   BINDING         220
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BH64"
FT   BINDING         258
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BH64"
FT   BINDING         489
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         491
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         493
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         500
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H4M9"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H4M9"
FT   MOD_RES         456
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H4M9"
SQ   SEQUENCE   534 AA;  60627 MW;  3330218772A26CE4 CRC64;
     MFSWVSKDAR RKKEPELFQT VAEGLRQLYA QKLLPLEEHY RFHEFHSPAL EDADFDNKPM
     VLLVGQYSTG KTTFIRHLIE QDFPGMRIGP EPTTDSFIAV MHGPTEGVVP GNALVVDPRR
     PFRKLNAFGN AFLNRFMCAQ LPNPVLDSIS IIDTPGILSG EKQRISRGYD FAAVLEWFAE
     RVDRIILLFD AHKLDISDEF SEVIKALKNH EDKIRVVLNK ADQIETQQLM RVYGALMWSL
     GKIINTPEVV RVYIGSFWSH PLLIPDNRKL FEAEEQDLFK DIQSLPRNAA LRKLNDLIKR
     ARLAKVHAYI ISSLKKEMPN VFGKESKKKE LVNNLGEIYQ KIEREHQISP GDFPSLRKMQ
     ELLQTQDFSK FQALKPKLLD TVDDMLANDI ARLMVMVRQE ESLMPSQVVK GGAFDGTMNG
     PFGHGYGEGA GEGIDDVEWV VGKDKPTYDE IFYTLSPVNG KITGANAKKE MVKSKLPNTV
     LGKIWKLADV DKDGLLDDEE FALANHLIKV KLEGHELPAD LPPHLVPPSK RRHE
 
 
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