ID A0A0D9QUQ1_CHLSB Unreviewed; 1411 AA.
AC A0A0D9QUQ1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Early endosome antigen 1 {ECO:0000313|Ensembl:ENSCSAP00000000090.1};
GN Name=EEA1 {ECO:0000313|Ensembl:ENSCSAP00000000090.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000000090.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000000090.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000000090.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AQIB01023632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01023633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01023634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008002427.1; XM_008004236.1.
DR STRING; 60711.ENSCSAP00000000090; -.
DR Ensembl; ENSCSAT00000001751.1; ENSCSAP00000000090.1; ENSCSAG00000003719.1.
DR GeneID; 103238861; -.
DR KEGG; csab:103238861; -.
DR CTD; 8411; -.
DR eggNOG; ENOG502QWB5; Eukaryota.
DR GeneTree; ENSGT00940000156910; -.
DR OMA; FIAVYQH; -.
DR OrthoDB; 2881467at2759; -.
DR BioGRID-ORCS; 103238861; 0 hits in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 11.
DR Bgee; ENSCSAG00000003719; Expressed in liver and 7 other cell types or tissues.
DR GO; GO:0044308; C:axonal spine; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031901; C:early endosome membrane; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0005969; C:serine-pyruvate aminotransferase complex; IEA:Ensembl.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IEA:Ensembl.
DR GO; GO:0030742; F:GTP-dependent protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0099565; P:chemical synaptic transmission, postsynaptic; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0044788; P:modulation by host of viral process; IEA:Ensembl.
DR GO; GO:0006906; P:vesicle fusion; IEA:Ensembl.
DR CDD; cd15730; FYVE_EEA1; 1.
DR Gene3D; 1.20.5.390; L1 transposable element, trimerization domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013087; Znf_C2H2_type.
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 PANTHER; PTHR23164; EARLY ENDOSOME ANTIGEN 1; 1.
DR PANTHER; PTHR23164:SF17; EARLY ENDOSOME ANTIGEN 1; 1.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 1.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 41..69
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1352..1410
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 130..199
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 241..324
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 367..418
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 11..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1411 AA; 162542 MW; 83EBC91B42BC822B CRC64;
MLRRILQRTP GRVGSQGSDL DSSATPINTV DVNNESSSEG FICPQCMKSL GSADELFKHY
EAVHDAGNDS GHGGESNLAL KRDDVTLLRQ EVQDLQASLK EEKWYSEELK KELEKYQGLQ
QQEAKPDGLV TDSSAELQSL EQQLEEAQTE NFNIKQMKDL FEQKAAQLAT EIADIKSKYD
EERSLREAAE QKVTHLTEEL NKEATVIQDL KTELLQRPGI EDVAVLKKEL VQVQTLMDNM
TLERERESEK LKDECKKLQS QYASSEATIS QLRSELAKGP QEVAVYVQEL QKLKSSVNEL
TQKNQTLTEN LLKKEQDYTK LEEKHNEESV SKKNIQATLH QKDLDCQQLQ SRLSASETSL
HRIHAELSEK GEATQKLKEE LSEVETKYQH LKAEFKQLQQ QREEKEQHGL QLQSEINQLH
SKLLETERQL GEAHGRLKEQ RQLSSEKLMD KEQQVADLQL KLSRLEEQLK EKVTNSTELQ
HQLDKTKQQH QEQQALQQST TAKLREAQND LEQVLRQIGD KDQKIQNLEA LLQKSKENIS
LLEKEREDLY AKIQAGEGET AVLNQLQEKN HTLQEQVTQL TEKLKNQSES HKQAQENLHD
QVQEQKAHLR AAQDRVLSLE TSVNELNSQL NESKEKVSQL DIQIKAKTEL LLSAEAAKTA
QRADLQNHLD TAQNALQDKQ QELNKITTQL DQVTAKLQDK QEHCSQLESH LKEYKEKHLS
LEQKTEELEG QIKKLEADSL EVKASKEQAL QDLQQQRQLN TDLELRATEL SKQLEMEKEI
VSSTRLDLQK KSEALENIKQ KLTKQEEEKK VLKQEFETLS QEAKIQHEEL NNRIQTTVTE
LQKVKMEKEA LMTELSTVKE KLSKVSDSLK HSKSEFEKEN QKGKAAILDL EKTCKELKHQ
LQVQMENTLR EQKELKKSLE KEKEASHQLK LELNSMQEQL IQAQNTLKQK EKEEQQLQEN
INELKQSSEQ KKKQIEALQG ELKIAVLQKT ELENKLQQQL TQAAQELAAE KEKISVLQNN
YEKSQETFKQ LQSDFYGKES ELLATRQDLK SIEEKLSLAQ EDLISNRNQI GNQNKLIQEL
KTAKATLEQD SAKKEQQLQE RCKALQDIQK EKSLKEKELV NEKSKLAEIE EIKCRQEKEI
TKLNEELKSH KQESIKEITN LKDAKQLLIQ QKLELQGKAD SLKAAVEQEK RNQQILKDQV
KKEEEELKKE FIEKEAKLHS EIKEKEVGMK KHEENEAKLT MQITALNENL GTVKKEWQSS
QRRVSELEKQ TDDLRGEIAV LEATVQNNQD ERRALLERCL KGEGEIEKLQ TKVLELQRKL
DNTTAAVQEL GRENQSLQIK HTQALNRKWA EDNEVQNCMA CGKGFSVTVR RHHCRQCGNI
FCAECSAKNA LTPSSKKPVR VCDACFNDLQ G
//
