DEN1A_XENLA
ID DEN1A_XENLA Reviewed; 1010 AA.
AC Q68F67;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=DENN domain-containing protein 1A;
DE AltName: Full=Connecdenn;
GN Name=dennd1a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) regulating clathrin-
CC mediated endocytosis through RAB35 activation. Promotes the exchange of
CC GDP to GTP, converting inactive GDP-bound RAB35 into its active GTP-
CC bound form. Regulates clathrin-mediated endocytosis of synaptic
CC vesicles and mediates exit from early endosomes. Binds
CC phosphatidylinositol-phosphates (PtdInsPs), with some preference for
CC PtdIns(3)P. {ECO:0000250|UniProtKB:Q8K382,
CC ECO:0000250|UniProtKB:Q8TEH3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000250|UniProtKB:Q8K382}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8K382}. Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q8K382}. Note=Associates to membranes via lipid-
CC binding activity. {ECO:0000250|UniProtKB:Q8K382}.
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DR EMBL; BC079977; AAH79977.1; -; mRNA.
DR RefSeq; NP_001087471.1; NM_001094002.1.
DR AlphaFoldDB; Q68F67; -.
DR SMR; Q68F67; -.
DR DNASU; 447295; -.
DR GeneID; 447295; -.
DR KEGG; xla:447295; -.
DR CTD; 447295; -.
DR Xenbase; XB-GENE-5729864; dennd1a.S.
DR OrthoDB; 189322at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 447295; Expressed in testis and 18 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISS:UniProtKB.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; ISS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; ISS:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.11500; -; 1.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR040032; DENND1A/B/C.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR005113; uDENN_dom.
DR PANTHER; PTHR13196; PTHR13196; 2.
DR Pfam; PF03455; dDENN; 1.
DR Pfam; PF02141; DENN; 1.
DR Pfam; PF03456; uDENN; 1.
DR SMART; SM00801; dDENN; 1.
DR SMART; SM00799; DENN; 1.
DR SMART; SM00800; uDENN; 1.
DR PROSITE; PS50211; DENN; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Guanine-nucleotide releasing factor; Lipid-binding; Membrane;
KW Protein transport; Reference proteome; Synapse; Transport.
FT CHAIN 1..1010
FT /note="DENN domain-containing protein 1A"
FT /id="PRO_0000342622"
FT DOMAIN 13..143
FT /note="uDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 160..296
FT /note="cDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 298..375
FT /note="dDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT REGION 455..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 378..382
FT /note="FXDXF motif"
FT /evidence="ECO:0000250|UniProtKB:Q8TEH3"
FT MOTIF 560..569
FT /note="Clathrin box"
FT /evidence="ECO:0000250|UniProtKB:Q8TEH3"
FT COMPBIAS 505..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1010 AA; 112377 MW; CFA08F5335CBE0C0 CRC64;
MGSRLKQNPD TTFEVYIEVN RPGSTDEDPE LQRIFPEDFS DQEVLQTVTK FCFPFSLDSL
TSSHVGQNFT FVLTDIDSKQ RFGFCRLSSG AKSCFCILSY LPWFEAFYKL LNILAEYSSK
NQDSQRNELL KTLHGHPIPE PGTPMHLSVH SHFTVPDSQE LPSIPENRNL TEYFVAVDVN
NMLHLYASML YERRILICCS KLSTLTACIH GSSAMLFPMY WQHVYIPVLP PHLLDYCCAP
MPYLIGIHSS LMEKVKGMSL DDVVFLNVDT NTLETPFDDL QNLPNEVVSA LKNRIRKMST
TTGDGVARAF LKAQASLFGS YRNALKIEPE EPITFCEETF VSHRSSGLRP FLQNAIQLQL
FKQFIDGRLD LLNSGNGFSD VFEEEINMGE YAGSDKLYHQ WLSTVKKGSG AFINTMKTRA
NPAMKTVYKF AKDHAKMGIK EVKNRLKQKD MAENGFSTAT EEPLPQISPS SIEKKRGEER
RPITVHFGQV RPPRPHVPRR PKSNAVVESR TTAGSSPDQP QQYRTLKESD ADGDEAISPE
KDSSEATVKE PQSTEVKHVS LLEDIFSNLQ TEPPLLSQAK SLEDLRTPKE DHENQFTFDY
QRMDLTAQER TRTIPAMKHG HPYNKLWSMG HDDMAIPNKY LQISPERHLT LPSNSTVTPH
KDSALTNIEK EVTIASSQGN ITIPRPHGRK TPELGIVPPP PAPRGIKLQT AMTDANKQQT
GDSSNYHGQI TEGSLRELSA DNGEKETAGS STSEILKPVK VSTEVGMNDD DLLSLLDPLK
AGRYQTASQP PMGTLPHSFE TPCCSSTPLL TSLQSDFVSP AFSHQLGFAP QPAFLHSPLN
PFAQALAAEK TASVMGPPMG VFKAPVATAL GSHSFLPTPG IYHSPRPLTS ALQGSNLFGQ
ISSGTPLNPV IRQSHSLSET QSNMPLMTSI PAGHRTLPMV QSRSKHQDGK PREYPPIPPR
PAKLLEPALL PTKSDQPIDP FEDLLNKTKQ TVTPASGKVE HLRKQWETFE
