EEA1_MOUSE
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 03-AUG-2022, entry version 157.
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, Pancreas,
RC 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};
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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 iPTMnet; Q8BL66; -.
DR PhosphoSitePlus; Q8BL66; -.
DR REPRODUCTION-2DPAGE; IPI00453776; -.
DR EPD; Q8BL66; -.
DR jPOST; Q8BL66; -.
DR MaxQB; Q8BL66; -.
DR PaxDb; Q8BL66; -.
DR PeptideAtlas; Q8BL66; -.
DR PRIDE; Q8BL66; -.
DR ProteomicsDB; 275903; -.
DR Antibodypedia; 3127; 534 antibodies from 44 providers.
DR DNASU; 216238; -.
DR Ensembl; ENSMUST00000053484; ENSMUSP00000061493; ENSMUSG00000036499.
DR GeneID; 216238; -.
DR KEGG; mmu:216238; -.
DR UCSC; uc007gwu.1; mouse.
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; 753155at2759; -.
DR PhylomeDB; Q8BL66; -.
DR TreeFam; TF329698; -.
DR Reactome; R-MMU-168138; Toll Like Receptor 9 (TLR9) Cascade.
DR BioGRID-ORCS; 216238; 4 hits in 73 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 253 other tissues.
DR ExpressionAtlas; Q8BL66; baseline and differential.
DR Genevisible; Q8BL66; MM.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
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: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 Gene3D; 3.30.40.10; -; 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 Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
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
