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Database: UniProt
Entry: E3LPC5_CAERE
LinkDB: E3LPC5_CAERE
Original site: E3LPC5_CAERE 
ID   E3LPC5_CAERE            Unreviewed;      1213 AA.
AC   E3LPC5;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=CRE-EEA-1 protein {ECO:0000313|EMBL:EFP05522.1};
GN   Name=Cre-eea-1 {ECO:0000313|EMBL:EFP05522.1};
GN   ORFNames=CRE_27564 {ECO:0000313|EMBL:EFP05522.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; DS268412; EFP05522.1; -; Genomic_DNA.
DR   RefSeq; XP_003114184.1; XM_003114136.1.
DR   AlphaFoldDB; E3LPC5; -.
DR   STRING; 31234.E3LPC5; -.
DR   EnsemblMetazoa; CRE27564.1; CRE27564.1; WBGene00052809.
DR   eggNOG; ENOG502QWB5; Eukaryota.
DR   HOGENOM; CLU_256550_0_0_1; -.
DR   InParanoid; E3LPC5; -.
DR   OMA; EAHWKTK; -.
DR   OrthoDB; 2881467at2759; -.
DR   Proteomes; UP000008281; Unassembled WGS sequence.
DR   GO; GO:0005769; C:early endosome; IEA:EnsemblMetazoa.
DR   GO; GO:0030139; C:endocytic vesicle; IEA:EnsemblMetazoa.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblMetazoa.
DR   GO; GO:0006897; P:endocytosis; IEA:EnsemblMetazoa.
DR   CDD; cd15730; FYVE_EEA1; 1.
DR   Gene3D; 1.10.287.1490; -; 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; 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:SF30; LD23155P; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF69979; Eea1 homodimerisation domain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          1154..1212
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          663..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          747..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          104..138
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          164..240
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          282..341
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        790..832
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1213 AA;  140767 MW;  C27FDE302DB385F8 CRC64;
     MLQRFKKQVS QVANELDGRL SNSSRASVSS QDSQSQPQQK SENEQEIEGF LCPICMIEHG
     SADELTAHFE NKHADFKTSA NRNHPEYAPP QAAPLAFGTK DQEIEELRIR VTEEKRFAER
     IKEELDNIKT VMANASDVTE DEIPYMAQQI QVLTADKGMV TRQFLELEKE SGQQTRELQQ
     VKQERGDLMA KLKQLSVNLR ELTDENETTK VEREDLKREL KVANSDVVRY EIEVARLEKM
     LDQRPSEDDV NVLRTELVNS QTIMDSISQE KDIEIKEHLN SIRNLSMERE KQHAINENLE
     KKILEGEETV KQLQISYDSQ SDELKQRNER ILQLEERIQE NVFELAENHQ LVKRLQDKVK
     EAESGVQLFS GINNSNEEMI NSLKAKFEKN SAEQKRMQTV FDEKVAAQGE RLKSMELSNL
     DLTNEMSSIS TLLDKERTLV EEKNAEISER DSSINELREK LAESEKKATK YSNDLKEQTT
     LVENLTLQLN KVQENSKELM EKISTGEGGA KMAIEQMEQE KEKLTKELQE LAEKNKKASE
     EFEHKISELE KKLREAEASR TDKEQKWKQE KETFERKIAE AEDEIRRKSE RFVEMEKEME
     EDRQKASDRT LKLKDALVKS EKDLETVKKE SEERDKVVRE KDAHLEENKK RIEDAVQKLE
     EAEKRARELE ASVSNRDSAV STKDSELAEM KSKLTESNSF IEELKVQVEK VSSELAEKQQ
     EVESLMTEMH EKEAHWKTKR DEFEAQIVRN QEENEEASTT LKSLQDQLTK EKEALSEEKS
     QLSSFKSQLE ESKNENERLL RSDEEKAEEI NKLKLSLSNS NHEREELIAT TESIRSENEN
     LTSKLQALED SRKQAEEKNS ANVESLIAEK SRLEKEVEER ESTIQSIQEA IESKDNEIES
     LKSTSRIVED ELLSKISLIE SFNSRIEEFE KEMASGKRKI EQLEAEKAEE MEKLVIVSRT
     QSQKQEEVEQ LQKEMAEKSK TIERVCSEFI MTSSKTQFEA MFTDVQQTLQ KEVNEKNQEI
     EKLLERIDSL ESSTQQKVED LESRLTQRER LVESLEAEMA AVRNAEQEKL DEQKKLKEEY
     DELKKAEAMW QAEKDMLIER CLGNESDIEY EKERAQENKR RFDEALSAMH ELGRANQSLQ
     IDADRYTSRK WLDDAEAINC TECGKVFSLT VRKHHCRVCG KIYCNPCSSK SVRIASAKHP
     VRACNHCFAE SQK
//
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