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Database: UniProt
Entry: A0A2R9C8H8_PANPA
LinkDB: A0A2R9C8H8_PANPA
Original site: A0A2R9C8H8_PANPA 
ID   A0A2R9C8H8_PANPA        Unreviewed;      1411 AA.
AC   A0A2R9C8H8;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Early endosome antigen 1 {ECO:0000313|Ensembl:ENSPPAP00000038246.1};
GN   Name=EEA1 {ECO:0000313|Ensembl:ENSPPAP00000038246.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000038246.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000038246.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000038246.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AJFE02082405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02082406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02082407; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02082408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02082409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003823443.1; XM_003823395.2.
DR   STRING; 9597.ENSPPAP00000038246; -.
DR   Ensembl; ENSPPAT00000061149.1; ENSPPAP00000038246.1; ENSPPAG00000041822.1.
DR   GeneID; 100995101; -.
DR   KEGG; pps:100995101; -.
DR   CTD; 8411; -.
DR   GeneTree; ENSGT00940000156910; -.
DR   OMA; FIAVYQH; -.
DR   OrthoDB; 2881467at2759; -.
DR   Proteomes; UP000240080; Chromosome 12.
DR   Bgee; ENSPPAG00000041822; Expressed in cerebellum and 6 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   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:UP000240080};
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..213
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   COILED          1172..1347
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;  162551 MW;  2E949506F9D3B9CC CRC64;
     MLRRILQRTP GRVGSQGSDL DSSATPINTV DVNNESSSEG FICPQCMKSL GSADELFKHY
     EAVHDAGNDS GHGGESNLAL KRDDVTLLRQ EVQDLQASLK EEKWYSEELK KELEKYQGLQ
     QQEAKPDGLV TDSSAELQSL EQQLEEAQTE NFNIKQMKDL FEQKAAQLAT EIADIKSKYD
     EERSLREAAE QKMTHLTEEL NKEATVIQDL KTELLQRPGI EDVAVLKKEL VQVQTLMDNM
     TLERERESEK LKDECKKLQS QYASSEATIS QLRSELAKGP QEVAVYVQEL QKLKSSVNEL
     TQKNQTLTEN LLKKEQDYTK LEEKHNEESV SKKNIQATLH QKDLDYQQLQ SRLSASETSL
     HRIHVELSEK GEATQKLKEE LSEVETKYQH LKVEFKQLQQ 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 LKEYKEKYLS
     LEQKTEELEG QIKKLEADSL EVKASKEQAL QDLQQQRQLN TDLELRATEL SKQLEMEKEI
     VSSTRLDLQK KSEALESIKQ KLTKQEEEKK ILKQEFETLS QEAKIQHEEL NNRIQTTVTE
     LQKVKMEKEA LMTELSTVKD KLSKVSDSLK NSKSEFEKEN QKGKAAILDL EKTCKELKHQ
     LQVQMENTLK EQKELKKSLE KEKEASHQLK LELNSMQEQL IQAQNTLKQN EKEEQQLQGN
     INELKQSSEQ KKKQIEALQG ELKIAVLQKT ELENKLQQQL TQAAQELAAE KEKISVLQNN
     YEKSQETFKQ LQSDFYGRES ELLATRQDLK SVEEKLSLAQ EDLISNRNQI GNQNKLIQEL
     KTAKATLEQD SAKKEQQLQE RCKALQDIQK EKSLKEKELV NEKSKLAEIE EIKCRQEKEI
     TKLNEELKSH KLESIKEITN 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
//
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