ID   EEA1_MOUSE              Reviewed;        1411 AA.
AC   Q8BL66; Q6DIC2;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Early endosome antigen 1;
GN   Name=Eea1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-946.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH RAB31.
RX   PubMed=22460790; DOI=10.1073/pnas.1103638109;
RA   Baeza-Raja B., Li P., Le Moan N., Sachs B.D., Schachtrup C., Davalos D.,
RA   Vagena E., Bridges D., Kim C., Saltiel A.R., Olefsky J.M., Akassoglou K.;
RT   "p75 neurotrophin receptor regulates glucose homeostasis and insulin
RT   sensitivity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:5838-5843(2012).
CC   -!- FUNCTION: Binds phospholipid vesicles containing phosphatidylinositol
CC       3-phosphate and participates in endosomal trafficking. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Binds STX6. Binds RAB5A, RAB5B, RAB5C and RAB22A
CC       that have been activated by GTP-binding. Interacts with ERBB2 (By
CC       similarity). Interacts with RAB31. Interacts with SAMD9 and SAMD9L (By
CC       similarity). May interact with PLEKHF2 (By similarity).
CC       {ECO:0000250|UniProtKB:Q15075}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The FYVE-type zinc finger domain mediates interactions with
CC       phosphatidylinositol 3-phosphate in membranes of early endosomes and
CC       penetrates bilayers. The FYVE domain insertion into PtdIns(3)P-enriched
CC       membranes is substantially increased in acidic conditions (By
CC       similarity). {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32647.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC075637; AAH75637.1; -; mRNA.
DR   EMBL; AK046231; BAC32647.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS36042.1; -.
DR   RefSeq; NP_001001932.1; NM_001001932.3.
DR   AlphaFoldDB; Q8BL66; -.
DR   SMR; Q8BL66; -.
DR   BioGRID; 229728; 36.
DR   IntAct; Q8BL66; 29.
DR   MINT; Q8BL66; -.
DR   STRING; 10090.ENSMUSP00000061493; -.
DR   GlyGen; Q8BL66; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8BL66; -.
DR   PhosphoSitePlus; Q8BL66; -.
DR   SwissPalm; Q8BL66; -.
DR   REPRODUCTION-2DPAGE; IPI00453776; -.
DR   EPD; Q8BL66; -.
DR   jPOST; Q8BL66; -.
DR   MaxQB; Q8BL66; -.
DR   PaxDb; 10090-ENSMUSP00000061493; -.
DR   PeptideAtlas; Q8BL66; -.
DR   ProteomicsDB; 275903; -.
DR   Pumba; Q8BL66; -.
DR   Antibodypedia; 3127; 601 antibodies from 44 providers.
DR   DNASU; 216238; -.
DR   Ensembl; ENSMUST00000053484.8; ENSMUSP00000061493.7; ENSMUSG00000036499.10.
DR   GeneID; 216238; -.
DR   KEGG; mmu:216238; -.
DR   UCSC; uc007gwu.1; mouse.
DR   AGR; MGI:2442192; -.
DR   CTD; 8411; -.
DR   MGI; MGI:2442192; Eea1.
DR   VEuPathDB; HostDB:ENSMUSG00000036499; -.
DR   eggNOG; ENOG502QWB5; Eukaryota.
DR   GeneTree; ENSGT00940000156910; -.
DR   HOGENOM; CLU_256550_0_0_1; -.
DR   InParanoid; Q8BL66; -.
DR   OMA; FIAVYQH; -.
DR   OrthoDB; 2881467at2759; -.
DR   PhylomeDB; Q8BL66; -.
DR   TreeFam; TF329698; -.
DR   Reactome; R-MMU-168138; Toll Like Receptor 9 (TLR9) Cascade.
DR   BioGRID-ORCS; 216238; 5 hits in 78 CRISPR screens.
DR   ChiTaRS; Eea1; mouse.
DR   PRO; PR:Q8BL66; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q8BL66; Protein.
DR   Bgee; ENSMUSG00000036499; Expressed in animal zygote and 257 other cell types or tissues.
DR   ExpressionAtlas; Q8BL66; baseline and differential.
DR   GO; GO:0044308; C:axonal spine; IDA:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005769; C:early endosome; IDA:MGI.
DR   GO; GO:0031901; C:early endosome membrane; ISO:MGI.
DR   GO; GO:0005768; C:endosome; IDA:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR   GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR   GO; GO:0005969; C:serine-pyruvate aminotransferase complex; IDA:MGI.
DR   GO; GO:0005545; F:1-phosphatidylinositol binding; ISS:UniProtKB.
DR   GO; GO:0030742; F:GTP-dependent protein binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0099565; P:chemical synaptic transmission, postsynaptic; IDA:SynGO.
DR   GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR   GO; GO:0044788; P:modulation by host of viral process; ISO:MGI.
DR   GO; GO:0006906; P:vesicle fusion; ISO:MGI.
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.
DR   Genevisible; Q8BL66; MM.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Endosome; Membrane; Metal-binding; Phosphoprotein;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..1411
FT                   /note="Early endosome antigen 1"
FT                   /id="PRO_0000098707"
FT   ZN_FING         41..64
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1352..1410
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1189..1217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          78..1348
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        11..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1358
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1361
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1374
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1377
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1382
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1385
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1402
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1405
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   MOD_RES         52
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15075"
FT   MOD_RES         70
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15075"
FT   CONFLICT        225
FT                   /note="V -> I (in Ref. 2; BAC32647)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1411 AA;  160915 MW;  2365A51EF92019FD CRC64;
     MFRRILQRTP GRVGSQGSDL DSSATPINTV DVNNESSSEG FICPQCMKSL GSADELFKHY
     QAVHDAGNDS GHGGEAGLAL TRDDITLLRQ EVQDLQASLK EEKWYSEELK KELEKYQGLQ
     QQEAKSDGLV TDSSAELQAL EQQLEEAQTE NFNIKQMKDL FEQKAAQLAT EIADIKSKYD
     EEKSLRAAAE QKVTHLTEDL NKQTTVIQDL KTELLQRPGI EDVAVLKKEL VQVQTLMDNM
     TLERERESEK LKDECKKLQS EHAHLEATIN QLRSELAKGP QEVAVYVQEI QKLKGSINEL
     TQKNQNLTEK LQKKDLDYTH LEEKHNEESA SRKTLQASLH QRDLDCQQLQ ARLTASESSL
     QRAQGELSEK AEAAQKLREE LREVESTRQH LKVEVKQLQQ QREEKEQHGL QLQGEVSQLH
     CKLLETERQL GEAHGRLKEQ RQLSSEKLME KEQQVADLQL KLSRLEEQLK EKVTNSTELQ
     HQLEKSKQQH QEQQALQQSA TAKLREAQND LEQVLRQIGD KDQKIQNLEA LLQKGKESVS
     LLEKEREDLY AKIQAGEGET AVLNQLQEKN HALQQQLTQL TEKLKNQSES HKQAEENLHD
     QVQEQKAHLR AAQDRVLSLE TSVSELSSQL NESKEKVSQL DIQIKAKTEL LLSAEAAKAA
     QRADLQNHLD TAQHALQDKQ QELNKVSVQL DQLTAKFQEK QEHCIQLESH LKDHKEKHLS
     LEQKVEDLEG HIKKLEADAL EVKASKEQAL QSLQQQRQLS TDLELRNAEL SRELQEQEEV
     VSCTKLDLQN KSEILENIKQ TLTKKEEENV VLKQEFEKLS QDSKTQHKEL GDRMQAAVTE
     LTAVKAQKDA LLAELSTTKE KLSKVSDSLK NSKSEFEKEN QKGKAAVLDL EKACKELKHQ
     LQVQAESALK EQEDLKKSLE KEKETSQQLK IELNSVKGEV SQAQNTLKQK EKDEQQLQGT
     INQLKQSAEQ KKKQIEALQG EVKNAVSQKT VLENKLQQQS SQAAQELAAE KGKLSALQSN
     YEKCQADLKQ LQSDLYGKES ELLATRQDLK SVEEKLTLAQ EDLISNRNQI GNQNKSIQEL
     QAAKASLEQD SAKKEALLKE QSKALEDAQR EKSVKEKELV AEKSKLAEME EIKCRQEKEI
     TKLNEELKSH KQESIKEITN LKDAKQLLIQ QKLELQGRVD SLKAALEQEK ESQQLMREQV
     KKEEEKRKEE FSEKEAKLHS EIKEKEAGMK KHEENEAKLT MQVTTLNENL GTVKKEWQSS
     QRRVSELEKQ TDDLRGEIAV LEATVQNNQD ERRALLERCL KGEGEIEKLQ TKALELQRKL
     DNTTAAVQEL GRENQSLQIK HTQALNRKWA EDNEVQNCMS CGKCFSVTVR RHHCRQCGNI
     FCAECSTKNA LTPSSKKPVR VCDACFNDLQ G
//